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Research Scientist at the National Institute for Infectious Diseases, IRCCS L. Spallanzani, Rome- Italy
Complex systems are inherently multilevel and multiscale systems. The infectious disease system is considered a complex system resulting from the interaction between three sub-systems (host, pathogen, and environment) organized into a hierarchical structure, ranging from the cellular to the macro-ecosystem level, with multiscales. Therefore, to describe infectious disease phenomena that change through time and space and at different scales, we built a model framework where infectious disease must be considered the set of biological responses of human hosts to pathogens, with biological pathways shared with other pathologies in an ecological interaction context. In this paper, we aimed to design a framework for building a disease model for COVID-19 based on current literature evidence. The model was set up by identifying the molecular pathophysiology related to the COVID-19 phenotypes, collecting the mechanistic knowledge scattered across scientific literature and bioinformatic databases, and integrating it using a logical/conceptual model systems biology. The model framework building process began from the results of a domain-based literature review regarding a multiomics approach to COVID-19. This evidence allowed us to define a framework of COVID-19 conceptual model and to report all concepts in a multilevel and multiscale structure. The same interdisciplinary working groups that carried out the scoping review were involved. The conclusive result is a conceptual method to design multiscale models of infectious diseases. The methodology, applied in this paper, is a set of partially ordered research and development activities that result in a COVID-19 multiscale model.
Francesco Messina; Chiara Montaldo; Isabella Abbate; Manuela Antonioli; Veronica Bordoni; Giulia Matusali; Alessandra Sacchi; Emanuela Giombini; Gian Fimia; Mauro Piacentini; Maria Capobianchi; Francesco Lauria; Giuseppe Ippolito; on behalf of COVID-19 Scoping Review Working Group. Rationale and Criteria for a COVID-19 Model Framework. Viruses 2021, 13, 1309 .
AMA StyleFrancesco Messina, Chiara Montaldo, Isabella Abbate, Manuela Antonioli, Veronica Bordoni, Giulia Matusali, Alessandra Sacchi, Emanuela Giombini, Gian Fimia, Mauro Piacentini, Maria Capobianchi, Francesco Lauria, Giuseppe Ippolito, on behalf of COVID-19 Scoping Review Working Group. Rationale and Criteria for a COVID-19 Model Framework. Viruses. 2021; 13 (7):1309.
Chicago/Turabian StyleFrancesco Messina; Chiara Montaldo; Isabella Abbate; Manuela Antonioli; Veronica Bordoni; Giulia Matusali; Alessandra Sacchi; Emanuela Giombini; Gian Fimia; Mauro Piacentini; Maria Capobianchi; Francesco Lauria; Giuseppe Ippolito; on behalf of COVID-19 Scoping Review Working Group. 2021. "Rationale and Criteria for a COVID-19 Model Framework." Viruses 13, no. 7: 1309.
Oropharyngeal squamous cell carcinoma (OPSCC) is an increasing world health problem with a more favourable prognosis for patients with human papillomavirus (HPV)-positive tumors compared to those with HPV-negative OPSCC. How HPV confers a less aggressive phenotype, however, remains undefined. We demonstrated that HPV-positive OPSCC cells display reduced macroautophagy/autophagy activity, mediated by the ability of HPV-E7 to interact with AMBRA1, to compete with its binding to BECN1 and to trigger its calpain-dependent degradation. Moreover, we have shown that AMBRA1 downregulation and pharmacological inhibition of autophagy sensitized HPV-negative OPSCC cells to the cytotoxic effects of cisplatin. Importantly, semi-quantitative immunohistochemical analysis in primary OPSCCs confirmed that AMBRA1 expression is reduced in HPV-positive compared to HPV-negative tumors. Collectively, these data identify AMBRA1 as a key target of HPV to impair autophagy and propose the targeting of autophagy as a viable therapeutic strategy to improve treatment response of HPV-negative OPSCC.
Manuela Antonioli; Benedetta Pagni; Tiziana Vescovo; Rob Ellis; Benjamin Cosway; Francesca Rollo; Veronica Bordoni; Chiara Agrati; Marie Labus; Renato Covello; Maria Benevolo; Giuseppe Ippolito; Max Robinson; Mauro Piacentini; Penny Lovat; Gian Maria Fimia. HPV sensitizes OPSCC cells to cisplatin-induced apoptosis by inhibiting autophagy through E7-mediated degradation of AMBRA1. Autophagy 2020, 1 -14.
AMA StyleManuela Antonioli, Benedetta Pagni, Tiziana Vescovo, Rob Ellis, Benjamin Cosway, Francesca Rollo, Veronica Bordoni, Chiara Agrati, Marie Labus, Renato Covello, Maria Benevolo, Giuseppe Ippolito, Max Robinson, Mauro Piacentini, Penny Lovat, Gian Maria Fimia. HPV sensitizes OPSCC cells to cisplatin-induced apoptosis by inhibiting autophagy through E7-mediated degradation of AMBRA1. Autophagy. 2020; ():1-14.
Chicago/Turabian StyleManuela Antonioli; Benedetta Pagni; Tiziana Vescovo; Rob Ellis; Benjamin Cosway; Francesca Rollo; Veronica Bordoni; Chiara Agrati; Marie Labus; Renato Covello; Maria Benevolo; Giuseppe Ippolito; Max Robinson; Mauro Piacentini; Penny Lovat; Gian Maria Fimia. 2020. "HPV sensitizes OPSCC cells to cisplatin-induced apoptosis by inhibiting autophagy through E7-mediated degradation of AMBRA1." Autophagy , no. : 1-14.
Mitochondria-associated membranes (MAMs) are essential communication subdomains of the endoplasmic reticulum (ER) that interact with mitochondria. We previously demonstrated that, upon macroautophagy/autophagy induction, AMBRA1 is recruited to the BECN1 complex and relocalizes to MAMs, where it regulates autophagy by interacting with raft-like components. ERLIN1 is an endoplasmic reticulum lipid raft protein of the prohibitin family. However, little is known about its association with the MAM interface and its involvement in autophagic initiation. In this study, we investigated ERLIN1 association with MAM raft-like microdomains and its interaction with AMBRA1 in the regulation of the autophagic process. We show that ERLIN1 interacts with AMBRA1 at MAM raft-like microdomains, which represents an essential condition for autophagosome formation upon nutrient starvation, as demonstrated by knocking down ERLIN1 gene expression. Moreover, this interaction depends on the "integrity" of key molecules, such as ganglioside GD3 and MFN2. Indeed, knocking down ST8SIA1/GD3-synthase or MFN2 expression impairs AMBRA1-ERLIN1 interaction at the MAM level and hinders autophagy. In conclusion, AMBRA1-ERLIN1 interaction within MAM raft-like microdomains appears to be pivotal in promoting the formation of autophagosomes. Abbreviations: ACSL4/ACS4: acyl-CoA synthetase long chain family member 4; ACTB/β-actin: actin beta; AMBRA1: autophagy and beclin 1 regulator 1; ATG14: autophagy related 14; BECN1: beclin 1; CANX: calnexin; Cy5: cyanine 5; ECL: enhanced chemiluminescence; ER: endoplasmic reticulum; ERLIN1/KE04: ER lipid raft associated 1; FB1: fumonisin B1; FE: FRET efficiency; FRET: Förster/fluorescence resonance energy transfer; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; GD3: aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(1-4)bDGlcp(1-1)ceramide; HBSS: Hanks' balanced salt solution; HRP: horseradish peroxidase; LMNB1: lamin B1; mAb: monoclonal antibody; MAMs: mitochondria-associated membranes; MAP1LC3B/LC3: microtubule associated protein 1 light chain 3 beta; MFN2: mitofusin 2; MTOR: mechanistic target of rapamycin kinase; MYC/cMyc: proto-oncogene, bHLH transcription factor; P4HB: prolyl 4-hydroxylase subunit beta; pAb: polyclonal antibody; PE: phycoerythrin; SCAP/SREBP: SREBF chaperone; SD: standard deviation; ST8SIA1: ST8 alpha-N-acetyl-neuraminide alpha-2,8 sialyltransferase 1; SQSTM1/p62: sequestosome 1; TOMM20: translocase of outer mitochondrial membrane 20; TUBB/beta-tubulin: tubulin beta class I; ULK1: unc-51 like autophagy activating kinase 1; VDAC1/porin: voltage dependent anion channel 1.
Valeria Manganelli; Paola Matarrese; Manuela Antonioli; Lucrezia Gambardella; Tiziana Vescovo; Christine Gretzmeier; Agostina Longo; Antonella Capozzi; Serena Recalchi; Gloria Riitano; Roberta Misasi; Joern Dengjel; Walter Malorni; Gian Maria Fimia; Maurizio Sorice; Tina Garofalo. Raft-like lipid microdomains drive autophagy initiation via AMBRA1-ERLIN1 molecular association within MAMs. Autophagy 2020, 1 -21.
AMA StyleValeria Manganelli, Paola Matarrese, Manuela Antonioli, Lucrezia Gambardella, Tiziana Vescovo, Christine Gretzmeier, Agostina Longo, Antonella Capozzi, Serena Recalchi, Gloria Riitano, Roberta Misasi, Joern Dengjel, Walter Malorni, Gian Maria Fimia, Maurizio Sorice, Tina Garofalo. Raft-like lipid microdomains drive autophagy initiation via AMBRA1-ERLIN1 molecular association within MAMs. Autophagy. 2020; ():1-21.
Chicago/Turabian StyleValeria Manganelli; Paola Matarrese; Manuela Antonioli; Lucrezia Gambardella; Tiziana Vescovo; Christine Gretzmeier; Agostina Longo; Antonella Capozzi; Serena Recalchi; Gloria Riitano; Roberta Misasi; Joern Dengjel; Walter Malorni; Gian Maria Fimia; Maurizio Sorice; Tina Garofalo. 2020. "Raft-like lipid microdomains drive autophagy initiation via AMBRA1-ERLIN1 molecular association within MAMs." Autophagy , no. : 1-21.
About 20% of total cancer cases are associated to infections. To date, seven human viruses have been directly linked to cancer development: high-risk human papillomaviruses (hrHPVs), Merkel cell polyomavirus (MCPyV), hepatitis B virus (HBV), hepatitis C virus (HCV), Epstein–Barr virus (EBV), Kaposi’s sarcoma-associated herpesvirus (KSHV), and human T-lymphotropic virus 1 (HTLV-1). These viruses impact on several molecular mechanisms in the host cells, often resulting in chronic inflammation, uncontrolled proliferation, and cell death inhibition, and mechanisms, which favor viral life cycle but may indirectly promote tumorigenesis. Recently, the ability of oncogenic viruses to alter autophagy, a catabolic process activated during the innate immune response to infections, is emerging as a key event for the onset of human cancers. Here, we summarize the current understanding of the molecular mechanisms by which human oncogenic viruses regulate autophagy and how this negative regulation impacts on cancer development. Finally, we highlight novel autophagy-related candidates for the treatment of virus-related cancers.
Tiziana Vescovo; Benedetta Pagni; Mauro Piacentini; Gian Maria Fimia; Manuela Antonioli. Regulation of Autophagy in Cells Infected With Oncogenic Human Viruses and Its Impact on Cancer Development. Frontiers in Cell and Developmental Biology 2020, 8, 47 .
AMA StyleTiziana Vescovo, Benedetta Pagni, Mauro Piacentini, Gian Maria Fimia, Manuela Antonioli. Regulation of Autophagy in Cells Infected With Oncogenic Human Viruses and Its Impact on Cancer Development. Frontiers in Cell and Developmental Biology. 2020; 8 ():47.
Chicago/Turabian StyleTiziana Vescovo; Benedetta Pagni; Mauro Piacentini; Gian Maria Fimia; Manuela Antonioli. 2020. "Regulation of Autophagy in Cells Infected With Oncogenic Human Viruses and Its Impact on Cancer Development." Frontiers in Cell and Developmental Biology 8, no. : 47.
Autophagy, a main intracellular catabolic process, is induced in response to a variety of cellular stresses to promptly degrade harmful agents and to coordinate the activity of prosurvival and prodeath processes in order to determine the fate of the injured cells. While the main components of the autophagy machinery are well characterized, the molecular mechanisms that confer selectivity to this process both in terms of stress detection and cargo engulfment have only been partly elucidated. Here, we discuss the emerging role played by the E3 ubiquitin ligases of the TRIM family in regulating autophagy in physiological and pathological conditions, such as inflammation, infection, tumorigenesis, and muscle atrophy. TRIM proteins employ different strategies to regulate the activity of the core autophagy machinery, acting either as scaffold proteins or via ubiquitin-mediated mechanisms. Moreover, they confer high selectivity to the autophagy-mediated degradation as described for the innate immune response, where TRIM proteins mediate both the engulfment of pathogens within autophagosomes and modulate the immune response by controlling the stability of signaling regulators. Importantly, the elucidation of the molecular mechanisms underlying the regulation of autophagy by TRIMs is providing important insights into how selective types of autophagy are altered under pathological conditions, as recently shown in cancer and muscular dystrophy.
Martina Di Rienzo; Alessandra Romagnoli; Manuela Antonioli; Mauro Piacentini; Gian Maria Fimia. TRIM proteins in autophagy: selective sensors in cell damage and innate immune responses. Cell Death & Differentiation 2020, 27, 887 -902.
AMA StyleMartina Di Rienzo, Alessandra Romagnoli, Manuela Antonioli, Mauro Piacentini, Gian Maria Fimia. TRIM proteins in autophagy: selective sensors in cell damage and innate immune responses. Cell Death & Differentiation. 2020; 27 (3):887-902.
Chicago/Turabian StyleMartina Di Rienzo; Alessandra Romagnoli; Manuela Antonioli; Mauro Piacentini; Gian Maria Fimia. 2020. "TRIM proteins in autophagy: selective sensors in cell damage and innate immune responses." Cell Death & Differentiation 27, no. 3: 887-902.
Optimal autophagic activity is crucial to maintain muscle integrity, with either reduced or excessive levels leading to specific myopathies. LGMD2H is a muscle dystrophy caused by mutations in the ubiquitin ligase TRIM32, whose function in muscles remains not fully understood. Here, we show that TRIM32 is required for the induction of muscle autophagy in atrophic conditions using both in vitro and in vivo mouse models. Trim32 inhibition results in a defective autophagy response to muscle atrophy, associated with increased ROS and MuRF1 levels. The proautophagic function of TRIM32 relies on its ability to bind the autophagy proteins AMBRA1 and ULK1 and stimulate ULK1 activity via unanchored K63-linked polyubiquitin. LGMD2H-causative mutations impair TRIM32’s ability to bind ULK1 and induce autophagy. Collectively, our study revealed a role for TRIM32 in the regulation of muscle autophagy in response to atrophic stimuli, uncovering a previously unidentified mechanism by which ubiquitin ligases activate autophagy regulators.
M. Di Rienzo; M. Antonioli; C. Fusco; Y. Liu; M. Mari; I. Orhon; G. Refolo; F. Germani; M. Corazzari; A. Romagnoli; F. Ciccosanti; B. Mandriani; M. T. Pellico; R. De La Torre; H. Ding; M. Dentice; M. Neri; A. Ferlini; F. Reggiori; M. Kulesz-Martin; M. Piacentini; G. Merla; G. M. Fimia. Autophagy induction in atrophic muscle cells requires ULK1 activation by TRIM32 through unanchored K63-linked polyubiquitin chains. Science Advances 2019, 5, eaau8857 .
AMA StyleM. Di Rienzo, M. Antonioli, C. Fusco, Y. Liu, M. Mari, I. Orhon, G. Refolo, F. Germani, M. Corazzari, A. Romagnoli, F. Ciccosanti, B. Mandriani, M. T. Pellico, R. De La Torre, H. Ding, M. Dentice, M. Neri, A. Ferlini, F. Reggiori, M. Kulesz-Martin, M. Piacentini, G. Merla, G. M. Fimia. Autophagy induction in atrophic muscle cells requires ULK1 activation by TRIM32 through unanchored K63-linked polyubiquitin chains. Science Advances. 2019; 5 (5):eaau8857.
Chicago/Turabian StyleM. Di Rienzo; M. Antonioli; C. Fusco; Y. Liu; M. Mari; I. Orhon; G. Refolo; F. Germani; M. Corazzari; A. Romagnoli; F. Ciccosanti; B. Mandriani; M. T. Pellico; R. De La Torre; H. Ding; M. Dentice; M. Neri; A. Ferlini; F. Reggiori; M. Kulesz-Martin; M. Piacentini; G. Merla; G. M. Fimia. 2019. "Autophagy induction in atrophic muscle cells requires ULK1 activation by TRIM32 through unanchored K63-linked polyubiquitin chains." Science Advances 5, no. 5: eaau8857.
The mechanisms underpinning the regenerative capabilities of mesenchymal stem cells (MSC) were originally thought to reside in their ability to recognise damaged tissue and to differentiate into specific cell types that would replace defective cells. However, recent work has shown that molecules produced by MSCs (secretome), particularly those packaged in extracellular vesicles (EVs), rather than the cells themselves are responsible for tissue repair. Here we have produced a secretome from adipose-derived mesenchymal stem cells (ADSC) that is free of exogenous molecules by incubation within a saline solution. Various in vitro models were used to evaluate the effects of the secretome on cellular processes that promote tissue regeneration. A cardiotoxin-induced skeletal muscle injury model was used to test the regenerative effects of the whole secretome or isolated extracellular vesicle fraction in vivo. This was followed by bioinformatic analysis of the components of the protein and miRNA content of the secretome and finally compared to a secretome generated from a secondary stem cell source. Here we have demonstrated that the secretome from adipose-derived mesenchymal stem cells shows robust effects on cellular processes that promote tissue regeneration. Furthermore, we show that the whole ADSC secretome is capable of enhancing the rate of skeletal muscle regeneration following acute damage. We assessed the efficacy of the total secretome compared with the extracellular vesicle fraction on a number of assays that inform on tissue regeneration and demonstrate that both fractions affect different aspects of the process in vitro and in vivo. Our in vitro, in vivo, and bioinformatic results show that factors that promote regeneration are distributed both within extracellular vesicles and the soluble fraction of the secretome. Taken together, our study implies that extracellular vesicles and soluble molecules within ADSC secretome act in a synergistic manner to promote muscle generation.
Robert Mitchell; Ben Mellows; Jonathan Sheard; Manuela Antonioli; Oliver Kretz; David Chambers; Marie-Theres Zeuner; James Tomkins; Bernd Denecke; Luca Musante; Barbara Joch; Florence Debacq-Chainiaux; Harry Holthofer; Steve Ray; Tobias B. Huber; Joern Dengjel; Paolo De Coppi; Darius Widera; Ketan Patel. Secretome of adipose-derived mesenchymal stem cells promotes skeletal muscle regeneration through synergistic action of extracellular vesicle cargo and soluble proteins. Stem Cell Research & Therapy 2019, 10, 1 -19.
AMA StyleRobert Mitchell, Ben Mellows, Jonathan Sheard, Manuela Antonioli, Oliver Kretz, David Chambers, Marie-Theres Zeuner, James Tomkins, Bernd Denecke, Luca Musante, Barbara Joch, Florence Debacq-Chainiaux, Harry Holthofer, Steve Ray, Tobias B. Huber, Joern Dengjel, Paolo De Coppi, Darius Widera, Ketan Patel. Secretome of adipose-derived mesenchymal stem cells promotes skeletal muscle regeneration through synergistic action of extracellular vesicle cargo and soluble proteins. Stem Cell Research & Therapy. 2019; 10 (1):1-19.
Chicago/Turabian StyleRobert Mitchell; Ben Mellows; Jonathan Sheard; Manuela Antonioli; Oliver Kretz; David Chambers; Marie-Theres Zeuner; James Tomkins; Bernd Denecke; Luca Musante; Barbara Joch; Florence Debacq-Chainiaux; Harry Holthofer; Steve Ray; Tobias B. Huber; Joern Dengjel; Paolo De Coppi; Darius Widera; Ketan Patel. 2019. "Secretome of adipose-derived mesenchymal stem cells promotes skeletal muscle regeneration through synergistic action of extracellular vesicle cargo and soluble proteins." Stem Cell Research & Therapy 10, no. 1: 1-19.
Summary Transglutaminase type 2 (TG2) is a multifunctional enzyme that plays a key role in mitochondria homeostasis under stressful cellular conditions. TG2 interactome analysis reveals an enzyme interaction with GRP75 (glucose-regulated protein 75). GRP75 localizes in mitochondria-associated membranes (MAMs) and acts as a bridging molecule between the two organelles by assembling the IP3R-GRP75-VDAC complex, which is involved in the transport of Ca2+ from the endoplasmic reticulum (ER) to mitochondria. We demonstrate that the TG2 and GRP75 interaction occurs in MAMs. The absence of the TG2-GRP75 interaction leads to an increase of the interaction between IP3R-3 and GRP75; a decrease of the number of ER-mitochondria contact sites; an impairment of the ER-mitochondrial Ca2+ flux; and an altered profile of the MAM proteome. These findings indicate TG2 is a key regulatory element of the MAMs.
Manuela D'Eletto; Federica Rossin; Luca Occhigrossi; Maria Grazia Farrace; Danilo Faccenda; Radha Desai; Saverio Marchi; Giulia Refolo; Laura Falasca; Manuela Antonioli; Fabiola Ciccosanti; Gian Maria Fimia; Paolo Pinton; Michelangelo Campanella; Mauro Piacentini. Transglutaminase Type 2 Regulates ER-Mitochondria Contact Sites by Interacting with GRP75. Cell Reports 2018, 25, 3573 -3581.e4.
AMA StyleManuela D'Eletto, Federica Rossin, Luca Occhigrossi, Maria Grazia Farrace, Danilo Faccenda, Radha Desai, Saverio Marchi, Giulia Refolo, Laura Falasca, Manuela Antonioli, Fabiola Ciccosanti, Gian Maria Fimia, Paolo Pinton, Michelangelo Campanella, Mauro Piacentini. Transglutaminase Type 2 Regulates ER-Mitochondria Contact Sites by Interacting with GRP75. Cell Reports. 2018; 25 (13):3573-3581.e4.
Chicago/Turabian StyleManuela D'Eletto; Federica Rossin; Luca Occhigrossi; Maria Grazia Farrace; Danilo Faccenda; Radha Desai; Saverio Marchi; Giulia Refolo; Laura Falasca; Manuela Antonioli; Fabiola Ciccosanti; Gian Maria Fimia; Paolo Pinton; Michelangelo Campanella; Mauro Piacentini. 2018. "Transglutaminase Type 2 Regulates ER-Mitochondria Contact Sites by Interacting with GRP75." Cell Reports 25, no. 13: 3573-3581.e4.
The secretome of human amniotic fluid stem cells (AFSCs) has great potential as a therapeutic agent in regenerative medicine. However, it must be produced in a clinically compliant manner before it can be used in humans. In this study, we developed a means of producing a biologically active secretome from AFSCs that is free of all exogenous molecules. We demonstrate that the full secretome is capable of promoting stem cell proliferation, migration, and protection of cells against senescence. Furthermore, it has significant anti-inflammatory properties. Most importantly, we show that it promotes tissue regeneration in a model of muscle damage. We then demonstrate that the secretome contains extracellular vesicles (EVs) that harbor much, but not all, of the biological activity of the whole secretome. Proteomic characterization of the EV and free secretome fraction shows the presence of numerous molecules specific to each fraction that could be key regulators of tissue regeneration. Intriguingly, we show that the EVs only contain miRNA and not mRNA. This suggests that tissue regeneration in the host is mediated by the action of EVs modifying existing, rather than imposing new, signaling pathways. The EVs harbor significant anti-inflammatory activity as well as promote angiogenesis, the latter may be the mechanistic explanation for their ability to promote muscle regeneration after cardiotoxin injury.
Ben Mellows; Robert Mitchell; Manuela Antonioli; Oliver Kretz; David Chambers; Marie-Theres Zeuner; Bernd Denecke; Luca Musante; Durrgah L. Ramachandra; Florence Debacq-Chainiaux; Harry Holthofer; Barbara Joch; Steve Ray; Darius Widera; Anna David; Tobias B. Huber; Joern Dengjel; Paolo De Coppi; Ketan Patel. Protein and Molecular Characterization of a Clinically Compliant Amniotic Fluid Stem Cell-Derived Extracellular Vesicle Fraction Capable of Accelerating Muscle Regeneration Through Enhancement of Angiogenesis. Stem Cells and Development 2017, 26, 1316 -1333.
AMA StyleBen Mellows, Robert Mitchell, Manuela Antonioli, Oliver Kretz, David Chambers, Marie-Theres Zeuner, Bernd Denecke, Luca Musante, Durrgah L. Ramachandra, Florence Debacq-Chainiaux, Harry Holthofer, Barbara Joch, Steve Ray, Darius Widera, Anna David, Tobias B. Huber, Joern Dengjel, Paolo De Coppi, Ketan Patel. Protein and Molecular Characterization of a Clinically Compliant Amniotic Fluid Stem Cell-Derived Extracellular Vesicle Fraction Capable of Accelerating Muscle Regeneration Through Enhancement of Angiogenesis. Stem Cells and Development. 2017; 26 (18):1316-1333.
Chicago/Turabian StyleBen Mellows; Robert Mitchell; Manuela Antonioli; Oliver Kretz; David Chambers; Marie-Theres Zeuner; Bernd Denecke; Luca Musante; Durrgah L. Ramachandra; Florence Debacq-Chainiaux; Harry Holthofer; Barbara Joch; Steve Ray; Darius Widera; Anna David; Tobias B. Huber; Joern Dengjel; Paolo De Coppi; Ketan Patel. 2017. "Protein and Molecular Characterization of a Clinically Compliant Amniotic Fluid Stem Cell-Derived Extracellular Vesicle Fraction Capable of Accelerating Muscle Regeneration Through Enhancement of Angiogenesis." Stem Cells and Development 26, no. 18: 1316-1333.
Autophagy is an extremely dynamic process that mediates the rapid degradation of intracellular components in response to different stress conditions. The autophagic response is executed by specific protein complexes, whose function is regulated by posttranslational modifications and interactions with positive and negative regulators. A comprehensive analysis of how autophagy complexes are temporally modified upon stress stimuli is therefore particularly relevant to understand how this pathway is regulated. Here, we describe a method to define the protein-protein interaction network of a central complex involved in autophagy induction, the Beclin 1 complex. This method is based on the quantitative comparison of protein complexes immunopurified at different time points using a stable isotope labeling by amino acids in cell culture approach. Understanding how the Beclin 1 complex dynamically changes in response to different stress stimuli may provide useful insights to disclose novel molecular mechanisms responsible for the dysregulation of autophagy in pathological conditions, such as cancer, neurodegeneration, and infections.
Manuela Antonioli; Fabiola Ciccosanti; Joern Dengjel; G.M. Fimia. Methods to Study the BECN1 Interactome in the Course of Autophagic Responses. Methods in Enzymology 2017, 587, 429 -445.
AMA StyleManuela Antonioli, Fabiola Ciccosanti, Joern Dengjel, G.M. Fimia. Methods to Study the BECN1 Interactome in the Course of Autophagic Responses. Methods in Enzymology. 2017; 587 ():429-445.
Chicago/Turabian StyleManuela Antonioli; Fabiola Ciccosanti; Joern Dengjel; G.M. Fimia. 2017. "Methods to Study the BECN1 Interactome in the Course of Autophagic Responses." Methods in Enzymology 587, no. : 429-445.
NAADP (nicotinic acid adenine dinucleotide phosphate) has been proposed as a second messenger for glutamate in neuronal and glial cells via the activation of the lysosomal Ca2+ channels TPC1 and TPC2. However, the activities of glutamate that are mediated by NAADP remain unclear. In this study, we evaluated the effect of glutamate on autophagy in astrocytes at physiological, non-toxic concentration. We found that glutamate induces autophagy at similar extent as NAADP. By contrast, the NAADP antagonist NED-19 or SiRNA-mediated inhibition of TPC1/2 decreases autophagy induced by glutamate, confirming a role for NAADP in this pathway. The involvement of TPC1/2 in glutamate-induced autophagy was also confirmed in SHSY5Y neuroblastoma cells. Finally, we show that glutamate leads to a NAADP-dependent activation of AMPK, which is required for autophagy induction, while mTOR activity is not affected by this treatment. Taken together, our results indicate that glutamate stimulates autophagy via NAADP/TPC/AMPK axis, providing new insights of how Ca2+ signalling glutamate-mediated can control the cell metabolism in the central nervous system.
Gustavo Pereira; Manuela Antonioli; Hanako Hirata; Rodrigo Ureshino; Aline R. Nascimento; Claudia Bincoletto; Tiziana Vescovo; Mauro Piacentini; Gian Maria Fimia; Soraya S. Smaili. Glutamate induces autophagy via the two-pore channels in neural cells. Oncotarget 2016, 8, 12730 -12740.
AMA StyleGustavo Pereira, Manuela Antonioli, Hanako Hirata, Rodrigo Ureshino, Aline R. Nascimento, Claudia Bincoletto, Tiziana Vescovo, Mauro Piacentini, Gian Maria Fimia, Soraya S. Smaili. Glutamate induces autophagy via the two-pore channels in neural cells. Oncotarget. 2016; 8 (8):12730-12740.
Chicago/Turabian StyleGustavo Pereira; Manuela Antonioli; Hanako Hirata; Rodrigo Ureshino; Aline R. Nascimento; Claudia Bincoletto; Tiziana Vescovo; Mauro Piacentini; Gian Maria Fimia; Soraya S. Smaili. 2016. "Glutamate induces autophagy via the two-pore channels in neural cells." Oncotarget 8, no. 8: 12730-12740.
Autophagy is an intracellular degradation pathway whose levels are tightly controlled to secure cell homeostasis. Unc-51–like kinase 1 (ULK1) is a conserved serine–threonine kinase that plays a central role in the initiation of autophagy. Here, we report that upon autophagy progression, ULK1 protein levels are specifically down-regulated by the E3 ligase NEDD4L, which ubiquitylates ULK1 for degradation by the proteasome. However, whereas ULK1 protein is degraded, ULK1 mRNA is actively transcribed. Upon reactivation of mTOR-dependent protein synthesis, basal levels of ULK1 are promptly restored, but the activity of newly synthesized ULK1 is inhibited by mTOR. This prepares the cell for a new possible round of autophagy stimulation. Our results thus place NEDD4L and ULK1 in a key position to control oscillatory activation of autophagy during prolonged stress to keep the levels of this process under a safe and physiological threshold.
Francesca Nazio; Marianna Carinci; Cristina Valacca; Pamela Bielli; Flavie Strappazzon; Manuela Antonioli; Fabiola Ciccosanti; Carlo Rodolfo; Silvia Campello; Gian Maria Fimia; Claudio Sette; Paolo Bonaldo; Francesco Cecconi. Fine-tuning of ULK1 mRNA and protein levels is required for autophagy oscillation. Journal of Cell Biology 2016, 215, 841 -856.
AMA StyleFrancesca Nazio, Marianna Carinci, Cristina Valacca, Pamela Bielli, Flavie Strappazzon, Manuela Antonioli, Fabiola Ciccosanti, Carlo Rodolfo, Silvia Campello, Gian Maria Fimia, Claudio Sette, Paolo Bonaldo, Francesco Cecconi. Fine-tuning of ULK1 mRNA and protein levels is required for autophagy oscillation. Journal of Cell Biology. 2016; 215 (6):841-856.
Chicago/Turabian StyleFrancesca Nazio; Marianna Carinci; Cristina Valacca; Pamela Bielli; Flavie Strappazzon; Manuela Antonioli; Fabiola Ciccosanti; Carlo Rodolfo; Silvia Campello; Gian Maria Fimia; Claudio Sette; Paolo Bonaldo; Francesco Cecconi. 2016. "Fine-tuning of ULK1 mRNA and protein levels is required for autophagy oscillation." Journal of Cell Biology 215, no. 6: 841-856.
Autophagy is a major degradative process activated in a rapid and transient manner to cope with stress conditions. Whether autophagy is beneficial or detrimental depends upon the rate of induction and the appropriateness of the duration. Alterations in both autophagy initiation and termination predispose the cell to death, and affect the execution of other inducible processes such as inflammation. In this review we discuss how stress signaling pathways dynamically control the activity of the autophagy machinery by mediating post-translational modifications and regulatory protein interactions. In particular, we highlight the emerging role of TRIM and CULLIN families of ubiquitin ligases which play opposite roles in the autophagy response by promoting or inhibiting, respectively, the activity of the autophagy initiation complex.
Manuela Antonioli; Martina Di Rienzo; Mauro Piacentini; Gian Maria Fimia. Emerging Mechanisms in Initiating and Terminating Autophagy. Trends in Biochemical Sciences 2016, 42, 28 -41.
AMA StyleManuela Antonioli, Martina Di Rienzo, Mauro Piacentini, Gian Maria Fimia. Emerging Mechanisms in Initiating and Terminating Autophagy. Trends in Biochemical Sciences. 2016; 42 (1):28-41.
Chicago/Turabian StyleManuela Antonioli; Martina Di Rienzo; Mauro Piacentini; Gian Maria Fimia. 2016. "Emerging Mechanisms in Initiating and Terminating Autophagy." Trends in Biochemical Sciences 42, no. 1: 28-41.
The estimation and quantification of potentially toxic cyanobacteria in lakes and reservoirs are often used as a proxy of risk for water intended for human consumption and recreational activities. Here, we present data sets collected from three volcanic Italian lakes (Albano, Vico, Nemi) that present filamentous cyanobacteria strains at different environments. Presented data sets were used to estimate abundance and morphometric characteristics of potentially toxic cyanobacteria comparing manual Vs. automated estimation performed by ACQUA ("ACQUA: Automated Cyanobacterial Quantification Algorithm for toxic filamentous genera using spline curves, pattern recognition and machine learning" (Gandola et al., 2016) [1]). This strategy was used to assess the algorithm performance and to set up the denoising algorithm. Abundance and total length estimations were used for software development, to this aim we evaluated the efficiency of statistical tools and mathematical algorithms, here described. The image convolution with the Sobel filter has been chosen to denoise input images from background signals, then spline curves and least square method were used to parameterize detected filaments and to recombine crossing and interrupted sections aimed at performing precise abundances estimations and morphometric measurements.
Emanuele Gandola; Manuela Antonioli; Alessio Traficante; Simone Franceschini; Michele Scardi; Roberta Congestri. Dataset exploited for the development and validation of automated cyanobacteria quantification algorithm, ACQUA. Data in Brief 2016, 8, 817 -23.
AMA StyleEmanuele Gandola, Manuela Antonioli, Alessio Traficante, Simone Franceschini, Michele Scardi, Roberta Congestri. Dataset exploited for the development and validation of automated cyanobacteria quantification algorithm, ACQUA. Data in Brief. 2016; 8 ():817-23.
Chicago/Turabian StyleEmanuele Gandola; Manuela Antonioli; Alessio Traficante; Simone Franceschini; Michele Scardi; Roberta Congestri. 2016. "Dataset exploited for the development and validation of automated cyanobacteria quantification algorithm, ACQUA." Data in Brief 8, no. : 817-23.
Numerous studies are revealing a role of exosomes in intercellular communication, and growing evidence indicates an important function for these vesicles in the progression and pathogenesis of cancer and neurodegenerative diseases. However, the biogenesis process of exosomes is still unclear. Tissue transglutaminase (TG2) is a multifunctional enzyme with different subcellular localizations. Particularly, under stressful conditions, the enzyme has been also detected in the extracellular matrix, but the mechanism(s) by which TG2 is released outside the cells requires further investigation. Therefore, the goal of the present study was to determine whether exosomes might be a vehicle for TG2 to reach the extracellular space, and whether TG2 could be involved in exosomes biogenesis. To address this issue, we isolated and characterized exosomes derived from cells either expressing or not TG2, under stressful conditions (i.e. proteasome impairment or expressing a mutated form of huntingtin (mHtt) containing 84 polyglutamine repeats). Our results show that TG2 is present in the exosomes only upon proteasome blockade, a condition in which TG2 interacts with TSG101 and ALIX, two key proteins involved in exosome biogenesis. Interestingly, we found that TG2 favours the assembly of a protein complex including mHtt, ALIX, TSG101 and BAG3, a co-chaperone involved in the clearance of mHtt. The formation of this complex is paralleled by the selective recruitment of mHtt and BAG3 in the exosomes derived from TG2 proficient cells only. Overall, our data indicate that TG2 is an important player in the biogenesis of exosomes controlling the selectivity of their cargo under stressful cellular conditions. In addition, these vesicles represent the way by which cells can release TG2 into the extracellular space under proteostasis impairment.
Laura Diaz-Hidalgo; Sara Altuntas; Federica Rossin; Manuela D'Eletto; Claudia Marsella; Maria Grazia Farrace; Laura Falasca; Manuela Antonioli; Gian Maria Fimia; Mauro Piacentini. Transglutaminase type 2-dependent selective recruitment of proteins into exosomes under stressful cellular conditions. Biochimica et Biophysica Acta (BBA) - Bioenergetics 2016, 1863, 2084 -2092.
AMA StyleLaura Diaz-Hidalgo, Sara Altuntas, Federica Rossin, Manuela D'Eletto, Claudia Marsella, Maria Grazia Farrace, Laura Falasca, Manuela Antonioli, Gian Maria Fimia, Mauro Piacentini. Transglutaminase type 2-dependent selective recruitment of proteins into exosomes under stressful cellular conditions. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 2016; 1863 (8):2084-2092.
Chicago/Turabian StyleLaura Diaz-Hidalgo; Sara Altuntas; Federica Rossin; Manuela D'Eletto; Claudia Marsella; Maria Grazia Farrace; Laura Falasca; Manuela Antonioli; Gian Maria Fimia; Mauro Piacentini. 2016. "Transglutaminase type 2-dependent selective recruitment of proteins into exosomes under stressful cellular conditions." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1863, no. 8: 2084-2092.
Toxigenic cyanobacteria are one of the main health risks associated with water resources worldwide, as their toxins can affect humans and fauna exposed via drinking water, aquaculture and recreation. Microscopy monitoring of cyanobacteria in water bodies and massive growth systems is a routine operation for cell abundance and growth estimation. Here we present ACQUA (Automated Cyanobacterial Quantification Algorithm), a new fully automated image analysis method designed for filamentous genera in Bright field microscopy. A pre-processing algorithm has been developed to highlight filaments of interest from background signals due to other phytoplankton and dust. A spline-fitting algorithm has been designed to recombine interrupted and crossing filaments in order to perform accurate morphometric analysis and to extract the surface pattern information of highlighted objects. In addition, 17 specific pattern indicators have been developed and used as input data for a machine-learning algorithm dedicated to the recognition between five widespread toxic or potentially toxic filamentous genera in freshwater: Aphanizomenon, Cylindrospermopsis, Dolichospermum, Limnothrix and Planktothrix. The method was validated using freshwater samples from three Italian volcanic lakes comparing automated vs. manual results. ACQUA proved to be a fast and accurate tool to rapidly assess freshwater quality and to characterize cyanobacterial assemblages in aquatic environments.
Emanuele Gandola; Manuela Antonioli; Alessio Traficante; Simone Franceschini; Michele Scardi; Roberta Congestri. ACQUA: Automated Cyanobacterial Quantification Algorithm for toxic filamentous genera using spline curves, pattern recognition and machine learning. Journal of Microbiological Methods 2016, 124, 48 -56.
AMA StyleEmanuele Gandola, Manuela Antonioli, Alessio Traficante, Simone Franceschini, Michele Scardi, Roberta Congestri. ACQUA: Automated Cyanobacterial Quantification Algorithm for toxic filamentous genera using spline curves, pattern recognition and machine learning. Journal of Microbiological Methods. 2016; 124 ():48-56.
Chicago/Turabian StyleEmanuele Gandola; Manuela Antonioli; Alessio Traficante; Simone Franceschini; Michele Scardi; Roberta Congestri. 2016. "ACQUA: Automated Cyanobacterial Quantification Algorithm for toxic filamentous genera using spline curves, pattern recognition and machine learning." Journal of Microbiological Methods 124, no. : 48-56.
Klionsky, Daniel J. eta l.This work was supported in part by the National Institutes of Health, including Public Health Service grant GM053396 to D.J.K. Due to space and other limitations, it is not possible to include all other sources of financial support.Peer reviewe
Daniel J Klionsky; Kotb Abdelmohsen; Akihisa Abe; Joynal Abedin; Hagai Abeliovich; Abraham Acevedo-Arozena; Hiroaki Adachi; Christopher Adams; Peter D Adams; Khosrow Adeli; Peter J Adhihetty; Sharon G Adler; Galila Agam; Rajesh Agarwal; Manish K Aghi; Maria Agnello; Patrizia Agostinis; Patricia V Aguilar; Julio Aguirre-Ghiso; Edoardo M Airoldi; Slimane Ait-Si-Ali; Takahiko Akematsu; Emmanuel T Akporiaye; Mohamed Al-Rubeai; Guillermo M. Albaiceta; Chris Albanese; Diego Albani; Matthew L Albert; Jesus Aldudo; Hana Algül; Mehrdad Alirezaei; Iraide Alloza; Alexandru Almasan; Maylin Almonte-Beceril; Emad S Alnemri; Covadonga Alonso; Nihal Altan-Bonnet; Dario C Altieri; Lydia Alvarez; Lydia Alvarez-Erviti; Sandro Alves; Giuseppina Amadoro; Atsuo Amano; Consuelo Amantini; Santiago Ambrosio; Ivano Amelio; Amal O Amer; Mohamed Amessou; Angelika Amon; Kairee Ryplanski; Frank A Anania; Stig U. Andersen; Usha Andley; Catherine K Andreadi; Nathalie Andrieu-Abadie; Alberto Anel; David K Ann; Shailendra Anoopkumar-Dukie; Manuela Antonioli; Hiroshi Aoki; Nadezda Apostolova; Saveria Aquila; Katia Aquilano; Koichi Araki; Eli Arama; Agustin Aranda; Jun Araya; Alexandre Arcaro; Esperanza Arias; Hirokazu Arimoto; Aileen R Ariosa; Jane Armstrong; Thierry Arnould; Ivica Arsov; Katsuhiko Asanuma; Valerie Askanas; Eric Asselin; Ryuichiro Atarashi; Sally S Atherton; Julie Atkin; Laura D Attardi; Patrick Auberger; Georg Auburger; Laure Aurelian; Riccardo Autelli; Laura Avagliano; Maria Laura Avantaggiati; Limor Avrahami; Suresh Awale; Neelam Azad; Tiziana Bachetti; Jonathan M Backer; Dong-Hun Bae; Jae-Sung Bae; Ok-Nam Bae; Soo Han Bae; Eric H Baehrecke; Seung-Hoon Baek; Stephen Baghdiguian; Agnieszka Bagniewska-Zadworna; Hua Bai; Jie Bai; Xue-Yuan Bai; Yannick Bailly; Kithiganahalli Narayanaswamy Balaji; Walter Balduini; Andrea Ballabio; Rena Balzan; Rajkumar Banerjee; Gábor Bánhegyi; Haijun Bao; Benoit Barbeau; Maria D Barrachina; Esther Barreiro; Bonnie Bartel; Alberto Bartolome; Diane C Bassham; Maria Teresa Bassi; Robert Bast; Alakananda Basu; Maria Teresa Batista; Henri Batoko; Maurizio Battino; Kyle Bauckman; Bradley L Baumgarner; K Ulrich Bayer; Rupert Beale; Jean-François Beaulieu; George R. Beck; Christoph Becker; J David Beckham; Pierre-André Bédard; Patrick J Bednarski; Thomas J Begley; Christian Behl; Christian Behrends; Georg Mn Behrens; Kevin E Behrns; Eloy Bejarano; Amine Belaid; Francesca Belleudi; Giovanni Bénard; Guy Berchem; Daniele Bergamaschi; Matteo Bergami; Ben Berkhout; Laura Berliocchi; Amelie Bernard; Monique Bernard; Francesca Bernassola; Anne Bertolotti; Amanda S Bess; Sébastien Besteiro; Saverio Bettuzzi; Savita Bhalla; Shalmoli Bhattacharyya; Sujit K Bhutia; Caroline Biagosch; Michele Wolfe Bianchi; Martine Biard-Piechaczyk; Viktor Billes; Claudia Bincoletto; Baris Bingol; Sara W Bird; Marc Bitoun; Ivana Bjedov; Craig Blackstone; Lionel Blanc; Guillermo A Blanco; Heidi Kiil Blomhoff; Emilio Boada Romero; Stefan Böckler; Marianne Boes; Kathleen Boesze-Battaglia; Lawrence Boise; Alessandra Bolino; Andrea Boman; Paolo Bonaldo; Matteo Bordi; Jürgen Bosch; Luis M Botana; Joelle Botti; German Bou; Marina Bouche; Marion Bouchecareilh; Marie-Josee Boucher; Michael E Boulton; Sebastien Bouret; Patricia Boya; Michaël Boyer-Guittaut; Peter Bozhkov; Nathan Brady; Vania Braga; Claudio Brancolini; Gerhard Braus; Jose Manuel Bravo-San Pedro; Lisa A Brennan; Emery H Bresnick; Patrick Brest; Dave Bridges; Marie-Agnès Bringer; Marisa Brini; Glauber C Brito; Bertha Brodin; Paul Brookes; Eric J Brown; Karen Brown; Hal E Broxmeyer; Alain Bruhat; Patricia Chakur Brum; John H Brumell; Nicola Brunetti-Pierri; Robert Bryson-Richardson; Shilpa Buch; Alastair M Buchan; Hikmet Budak; Dmitry V Bulavin; Scott J Bultman; Geert Bultynck; Vladimir Bumbasirevic; Yan Burelle; Robert E Burke; Margit Burmeister; Peter Bütikofer; Laura Caberlotto; Ken Cadwell; Monika Cahová; Dongsheng Cai; Jingjing Cai; Qian Cai; Sara Calatayud; Nadine Camougrand; Michelangelo Campanella; Grant R Campbell; Matthew Campbell; Silvia Campello; Robin Candau; Isabella Caniggia; Lavinia Cantoni; Lizhi Cao; Allan B Caplan; Michele Caraglia; Claudio Cardinali; Sandra M Cardoso; Jennifer S Carew; Laura A Carleton; Cathleen R Carlin; Silvia Carloni; Sven R Carlsson; Didac Carmona-Gutierrez; Leticia Carneiro; Oliana Carnevali; Serena Carra; Alice Carrier; Bernadette Carroll; Caty Casas; Josefina Casas; Giuliana Cassinelli; Perrine Castets; Susana Castro-Obregon; Gabriella Cavallini; Isabella Ceccherini; Francesco Cecconi; Arthur I Cederbaum; Valentín Ceña; Simone Cenci; Claudia Cerella; Davide Cervia; Silvia Cetrullo; Hassan Chaachouay; Han-Jung Chae; Andrei Chagin; Chee-Yin Chai; Gopal Chakrabarti; Georgios Chamilos; Edmond Yw Chan; Matthew Chan; Dhyan Chandra; Pallavi Chandra; Chih-Peng Chang; Raymond Chuen-Chung Chang; Ta Yuan Chang; John C Chatham; Saurabh Chatterjee; Santosh Chauhan; Yongsheng Che; Michael Cheetham; Rajkumar Cheluvappa; Chun-Jung Chen; Gang Chen; Guang-Chao Chen; Guoqiang Chen; Hongzhuan Chen; Jeff W Chen; Jian-Kang Chen; Min Chen; Mingzhou Chen; Peiwen Chen; Qi Chen; Quan Chen; Shang-Der Chen; Si Chen; Steve S-L Chen; Wei Chen; Wen Qiang Chen; Wenli Chen; Xiangmei Chen; Yau-Hung Chen; Ye-Guang Chen; Yin Chen; Yingyu Chen; Yongshun Chen; Yu-Jen Chen; Yue-Qin Chen; Yujie Chen; Zhen Chen; Zhong Chen; Alan Cheng; Christopher Hon-Ki Cheng; Hua Cheng; Heesun Cheong; Sara Cherry; Jason Chesney; Chun Hei Antonio Cheung; Eric Chevet; Hsiang Cheng Chi; Sung-Gil Chi; Fulvio Chiacchiera; Hui-Ling Chiang; Roberto Chiarelli; Mario Chiariello; Marcello Chieppa; Lih-Shen Chin; Mario Chiong; Gigi Nc Chiu; Dong-Hyung Cho; Ssang-Goo Cho; William C Cho; Yong-Yeon Cho; Young-Seok Cho; Augustine Mk Choi; Eui-Ju Choi; Eun-Kyoung Choi; Jayoung Choi; Mary E Choi; Seung-Il Choi; Tsui-Fen Chou; Salem Chouaib; Divaker Choubey; Vinay Choubey; Kuan-Chih Chow; Kamal Chowdhury; Charleen Chu; Tsung-Hsien Chuang; Taehoon Chun; Hyewon Chung; Taijoon Chung; Yuen-Li Chung; Yong-Joon Chwae; Valentina Cianfanelli; Roberto Ciarcia; Iwona Ciechomska; Maria Rosa Ciriolo; Mara Cirone; Sofie Claerhout; Michael J Clague; Joan Claria; Peter Gh Clarke; Robert Clarke; Emilio Clementi; Cedric Cleyrat; Miriam Cnop; Eliana M Coccia; Tiziana Maria Cocco; Patrice Codogno; Jörn Coers; Ezra Ew Cohen; David Colecchia; Luisa Coletto; Núria Sánchez Coll; Emma Colucci-Guyon; Sergio Comincini; Maria Condello; Katherine Cook; Graham H Coombs; Cynthia D Cooper; J Mark Cooper; Isabelle Coppens; Maria Tiziana Corasaniti; Marco Corazzari; Ramon Corbalan; Elisabeth Corcelle-Termeau; Mario D Cordero; Cristina Corral Ramos; Olga Corti; Andrea Cossarizza; Paola Costelli; Safia Costes; Susan L Cotman; Ana Coto-Montes; Sandra Cottet; Eduardo Couve; Lori R Covey; L Ashley Cowart; Jeffery S Cox; Fraser P Coxon; Carolyn B Coyne; Mark Cragg; Rolf J Craven; Tiziana Crepaldi; Jose L Crespo; Alfredo Criollo; Valeria Crippa; Maria Teresa Cruz; Ana Maria Cuervo; Jose M Cuezva; Taixing Cui; Pedro R Cutillas; Mark J Czaja; Maria F Czyzyk-Krzeska; Ruben K Dagda; Uta Dahmen; Chunsun Dai; Wenjie Dai; Yun Dai; Kevin Dalby; Luisa Dalla Valle; Guillaume Dalmasso; Marcello D'Amelio; Markus Damme; Arlette Darfeuille-Michaud; Catherine Dargemont; Victor Darley-Usmar; Srinivasan Dasarathy; Biplab Dasgupta; Srikanta Dash; Crispin R Dass; Hazel Davey; Lester M Davids; David Dávila; Roger J Davis; Ted M Dawson; Valina L Dawson; Paula Daza; Jackie De Belleroche; Paul De Figueiredo; Regina Figueiredo; José De La Fuente; Luisa De Martino; Maria Antonietta De Matteis; Guido De Meyer; Angelo De Milito; Mauro De Santi; Wanderley De Souza; Vincenzo De Tata; Daniela De Zio; Jayanta Debnath; Reinhard Dechant; Jean-Paul Decuypere; Shane Deegan; Benjamin Dehay; Barbara Del Bello; Dominic P Del Re; Régis Delage-Mourroux; Lea Md Delbridge; Louise Deldicque; Elizabeth Delorme-Axford; Yizhen Deng; Joern Dengjel; Melanie Denizot; Paul Dent; Channing Der; Vojo Deretic; Benoît Derrien; Eric Deutsch; Timothy P Devarenne; Rodney J Devenish; Sabrina Di Bartolomeo; Nicola Di Daniele; Fabio Di Domenico; Alessia Di Nardo; Simone Di Paola; Antonio Di Pietro; Livia Di Renzo; Aaron DiAntonio; Guillermo Díaz-Araya; Ines Diaz-Laviada; Maria T Diaz-Meco; Javier Diaz-Nido; Chad A Dickey; Robert C Dickson; Marc Diederich; Paul Digard; Ivan Dikic; Savithrama P Dinesh-Kumar; Chan Ding; Wen-Xing Ding; Zufeng Ding; Luciana Dini; Jörg Hw Distler; Abhinav Diwan; Mojgan Djavaheri-Mergny; Kostyantyn Dmytruk; Renwick Cj Dobson; Volker Dotsch; Karol Dokladny; Svetlana Dokudovskaya; Massimo Donadelli; X Charlie Dong; Zheng Dong; Terrence M Donohue; Kelly S Doran; Gabriella D'Orazi; Gerald W Dorn; Victor Dosenko; Sami Dridi; Liat Drucker; Jie Du; Li-Lin Du; Lihuan Du; André Du Toit; Priyamvada Dua; Lei Duan; Pu Duann; Vikash Kumar Dubey; Michael Duchen; Michel A Duchosal; Helene Duez; Isabelle Dugail; Verónica I Dumit; Mara Duncan; Elaine Dunlop; William A Dunn; Nicolas Dupont; Luc Dupuis; Raul V. 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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy 2016, 12, 1 -222.
AMA StyleDaniel J Klionsky, Kotb Abdelmohsen, Akihisa Abe, Joynal Abedin, Hagai Abeliovich, Abraham Acevedo-Arozena, Hiroaki Adachi, Christopher Adams, Peter D Adams, Khosrow Adeli, Peter J Adhihetty, Sharon G Adler, Galila Agam, Rajesh Agarwal, Manish K Aghi, Maria Agnello, Patrizia Agostinis, Patricia V Aguilar, Julio Aguirre-Ghiso, Edoardo M Airoldi, Slimane Ait-Si-Ali, Takahiko Akematsu, Emmanuel T Akporiaye, Mohamed Al-Rubeai, Guillermo M. Albaiceta, Chris Albanese, Diego Albani, Matthew L Albert, Jesus Aldudo, Hana Algül, Mehrdad Alirezaei, Iraide Alloza, Alexandru Almasan, Maylin Almonte-Beceril, Emad S Alnemri, Covadonga Alonso, Nihal Altan-Bonnet, Dario C Altieri, Lydia Alvarez, Lydia Alvarez-Erviti, Sandro Alves, Giuseppina Amadoro, Atsuo Amano, Consuelo Amantini, Santiago Ambrosio, Ivano Amelio, Amal O Amer, Mohamed Amessou, Angelika Amon, Kairee Ryplanski, Frank A Anania, Stig U. Andersen, Usha Andley, Catherine K Andreadi, Nathalie Andrieu-Abadie, Alberto Anel, David K Ann, Shailendra Anoopkumar-Dukie, Manuela Antonioli, Hiroshi Aoki, Nadezda Apostolova, Saveria Aquila, Katia Aquilano, Koichi Araki, Eli Arama, Agustin Aranda, Jun Araya, Alexandre Arcaro, Esperanza Arias, Hirokazu Arimoto, Aileen R Ariosa, Jane Armstrong, Thierry Arnould, Ivica Arsov, Katsuhiko Asanuma, Valerie Askanas, Eric Asselin, Ryuichiro Atarashi, Sally S Atherton, Julie Atkin, Laura D Attardi, Patrick Auberger, Georg Auburger, Laure Aurelian, Riccardo Autelli, Laura Avagliano, Maria Laura Avantaggiati, Limor Avrahami, Suresh Awale, Neelam Azad, Tiziana Bachetti, Jonathan M Backer, Dong-Hun Bae, Jae-Sung Bae, Ok-Nam Bae, Soo Han Bae, Eric H Baehrecke, Seung-Hoon Baek, Stephen Baghdiguian, Agnieszka Bagniewska-Zadworna, Hua Bai, Jie Bai, Xue-Yuan Bai, Yannick Bailly, Kithiganahalli Narayanaswamy Balaji, Walter Balduini, Andrea Ballabio, Rena Balzan, Rajkumar Banerjee, Gábor Bánhegyi, Haijun Bao, Benoit Barbeau, Maria D Barrachina, Esther Barreiro, Bonnie Bartel, Alberto Bartolome, Diane C Bassham, Maria Teresa Bassi, Robert Bast, Alakananda Basu, Maria Teresa Batista, Henri Batoko, Maurizio Battino, Kyle Bauckman, Bradley L Baumgarner, K Ulrich Bayer, Rupert Beale, Jean-François Beaulieu, George R. Beck, Christoph Becker, J David Beckham, Pierre-André Bédard, Patrick J Bednarski, Thomas J Begley, Christian Behl, Christian Behrends, Georg Mn Behrens, Kevin E Behrns, Eloy Bejarano, Amine Belaid, Francesca Belleudi, Giovanni Bénard, Guy Berchem, Daniele Bergamaschi, Matteo Bergami, Ben Berkhout, Laura Berliocchi, Amelie Bernard, Monique Bernard, Francesca Bernassola, Anne Bertolotti, Amanda S Bess, Sébastien Besteiro, Saverio Bettuzzi, Savita Bhalla, Shalmoli Bhattacharyya, Sujit K Bhutia, Caroline Biagosch, Michele Wolfe Bianchi, Martine Biard-Piechaczyk, Viktor Billes, Claudia Bincoletto, Baris Bingol, Sara W Bird, Marc Bitoun, Ivana Bjedov, Craig Blackstone, Lionel Blanc, Guillermo A Blanco, Heidi Kiil Blomhoff, Emilio Boada Romero, Stefan Böckler, Marianne Boes, Kathleen Boesze-Battaglia, Lawrence Boise, Alessandra Bolino, Andrea Boman, Paolo Bonaldo, Matteo Bordi, Jürgen Bosch, Luis M Botana, Joelle Botti, German Bou, Marina Bouche, Marion Bouchecareilh, Marie-Josee Boucher, Michael E Boulton, Sebastien Bouret, Patricia Boya, Michaël Boyer-Guittaut, Peter Bozhkov, Nathan Brady, Vania Braga, Claudio Brancolini, Gerhard Braus, Jose Manuel Bravo-San Pedro, Lisa A Brennan, Emery H Bresnick, Patrick Brest, Dave Bridges, Marie-Agnès Bringer, Marisa Brini, Glauber C Brito, Bertha Brodin, Paul Brookes, Eric J Brown, Karen Brown, Hal E Broxmeyer, Alain Bruhat, Patricia Chakur Brum, John H Brumell, Nicola Brunetti-Pierri, Robert Bryson-Richardson, Shilpa Buch, Alastair M Buchan, Hikmet Budak, Dmitry V Bulavin, Scott J Bultman, Geert Bultynck, Vladimir Bumbasirevic, Yan Burelle, Robert E Burke, Margit Burmeister, Peter Bütikofer, Laura Caberlotto, Ken Cadwell, Monika Cahová, Dongsheng Cai, Jingjing Cai, Qian Cai, Sara Calatayud, Nadine Camougrand, Michelangelo Campanella, Grant R Campbell, Matthew Campbell, Silvia Campello, Robin Candau, Isabella Caniggia, Lavinia Cantoni, Lizhi Cao, Allan B Caplan, Michele Caraglia, Claudio Cardinali, Sandra M Cardoso, Jennifer S Carew, Laura A Carleton, Cathleen R Carlin, Silvia Carloni, Sven R Carlsson, Didac Carmona-Gutierrez, Leticia Carneiro, Oliana Carnevali, Serena Carra, Alice Carrier, Bernadette Carroll, Caty Casas, Josefina Casas, Giuliana Cassinelli, Perrine Castets, Susana Castro-Obregon, Gabriella Cavallini, Isabella Ceccherini, Francesco Cecconi, Arthur I Cederbaum, Valentín Ceña, Simone Cenci, Claudia Cerella, Davide Cervia, Silvia Cetrullo, Hassan Chaachouay, Han-Jung Chae, Andrei Chagin, Chee-Yin Chai, Gopal Chakrabarti, Georgios Chamilos, Edmond Yw Chan, Matthew Chan, Dhyan Chandra, Pallavi Chandra, Chih-Peng Chang, Raymond Chuen-Chung Chang, Ta Yuan Chang, John C Chatham, Saurabh Chatterjee, Santosh Chauhan, Yongsheng Che, Michael Cheetham, Rajkumar Cheluvappa, Chun-Jung Chen, Gang Chen, Guang-Chao Chen, Guoqiang Chen, Hongzhuan Chen, Jeff W Chen, Jian-Kang Chen, Min Chen, Mingzhou Chen, Peiwen Chen, Qi Chen, Quan Chen, Shang-Der Chen, Si Chen, Steve S-L Chen, Wei Chen, Wen Qiang Chen, Wenli Chen, Xiangmei Chen, Yau-Hung Chen, Ye-Guang Chen, Yin Chen, Yingyu Chen, Yongshun Chen, Yu-Jen Chen, Yue-Qin Chen, Yujie Chen, Zhen Chen, Zhong Chen, Alan Cheng, Christopher Hon-Ki Cheng, Hua Cheng, Heesun Cheong, Sara Cherry, Jason Chesney, Chun Hei Antonio Cheung, Eric Chevet, Hsiang Cheng Chi, Sung-Gil Chi, Fulvio Chiacchiera, Hui-Ling Chiang, Roberto Chiarelli, Mario Chiariello, Marcello Chieppa, Lih-Shen Chin, Mario Chiong, Gigi Nc Chiu, Dong-Hyung Cho, Ssang-Goo Cho, William C Cho, Yong-Yeon Cho, Young-Seok Cho, Augustine Mk Choi, Eui-Ju Choi, Eun-Kyoung Choi, Jayoung Choi, Mary E Choi, Seung-Il Choi, Tsui-Fen Chou, Salem Chouaib, Divaker Choubey, Vinay Choubey, Kuan-Chih Chow, Kamal Chowdhury, Charleen Chu, Tsung-Hsien Chuang, Taehoon Chun, Hyewon Chung, Taijoon Chung, Yuen-Li Chung, Yong-Joon Chwae, Valentina Cianfanelli, Roberto Ciarcia, Iwona Ciechomska, Maria Rosa Ciriolo, Mara Cirone, Sofie Claerhout, Michael J Clague, Joan Claria, Peter Gh Clarke, Robert Clarke, Emilio 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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy. 2016; 12 (1):1-222.
Chicago/Turabian StyleDaniel J Klionsky; Kotb Abdelmohsen; Akihisa Abe; Joynal Abedin; Hagai Abeliovich; Abraham Acevedo-Arozena; Hiroaki Adachi; Christopher Adams; Peter D Adams; Khosrow Adeli; Peter J Adhihetty; Sharon G Adler; Galila Agam; Rajesh Agarwal; Manish K Aghi; Maria Agnello; Patrizia Agostinis; Patricia V Aguilar; Julio Aguirre-Ghiso; Edoardo M Airoldi; Slimane Ait-Si-Ali; Takahiko Akematsu; Emmanuel T Akporiaye; Mohamed Al-Rubeai; Guillermo M. Albaiceta; Chris Albanese; Diego Albani; Matthew L Albert; Jesus Aldudo; Hana Algül; Mehrdad Alirezaei; Iraide Alloza; Alexandru Almasan; Maylin Almonte-Beceril; Emad S Alnemri; Covadonga Alonso; Nihal Altan-Bonnet; Dario C Altieri; Lydia Alvarez; Lydia Alvarez-Erviti; Sandro Alves; Giuseppina Amadoro; Atsuo Amano; Consuelo Amantini; Santiago Ambrosio; Ivano Amelio; Amal O Amer; Mohamed Amessou; Angelika Amon; Kairee Ryplanski; Frank A Anania; Stig U. 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Cathleen R Carlin; Silvia Carloni; Sven R Carlsson; Didac Carmona-Gutierrez; Leticia Carneiro; Oliana Carnevali; Serena Carra; Alice Carrier; Bernadette Carroll; Caty Casas; Josefina Casas; Giuliana Cassinelli; Perrine Castets; Susana Castro-Obregon; Gabriella Cavallini; Isabella Ceccherini; Francesco Cecconi; Arthur I Cederbaum; Valentín Ceña; Simone Cenci; Claudia Cerella; Davide Cervia; Silvia Cetrullo; Hassan Chaachouay; Han-Jung Chae; Andrei Chagin; Chee-Yin Chai; Gopal Chakrabarti; Georgios Chamilos; Edmond Yw Chan; Matthew Chan; Dhyan Chandra; Pallavi Chandra; Chih-Peng Chang; Raymond Chuen-Chung Chang; Ta Yuan Chang; John C Chatham; Saurabh Chatterjee; Santosh Chauhan; Yongsheng Che; Michael Cheetham; Rajkumar Cheluvappa; Chun-Jung Chen; Gang Chen; Guang-Chao Chen; Guoqiang Chen; Hongzhuan Chen; Jeff W Chen; Jian-Kang Chen; Min Chen; Mingzhou Chen; Peiwen Chen; Qi Chen; Quan Chen; Shang-Der Chen; Si Chen; Steve S-L Chen; Wei Chen; Wen Qiang Chen; Wenli Chen; Xiangmei Chen; Yau-Hung Chen; Ye-Guang Chen; Yin Chen; Yingyu Chen; Yongshun Chen; Yu-Jen Chen; Yue-Qin Chen; Yujie Chen; Zhen Chen; Zhong Chen; Alan Cheng; Christopher Hon-Ki Cheng; Hua Cheng; Heesun Cheong; Sara Cherry; Jason Chesney; Chun Hei Antonio Cheung; Eric Chevet; Hsiang Cheng Chi; Sung-Gil Chi; Fulvio Chiacchiera; Hui-Ling Chiang; Roberto Chiarelli; Mario Chiariello; Marcello Chieppa; Lih-Shen Chin; Mario Chiong; Gigi Nc Chiu; Dong-Hyung Cho; Ssang-Goo Cho; William C Cho; Yong-Yeon Cho; Young-Seok Cho; Augustine Mk Choi; Eui-Ju Choi; Eun-Kyoung Choi; Jayoung Choi; Mary E Choi; Seung-Il Choi; Tsui-Fen Chou; Salem Chouaib; Divaker Choubey; Vinay Choubey; Kuan-Chih Chow; Kamal Chowdhury; Charleen Chu; Tsung-Hsien Chuang; Taehoon Chun; Hyewon Chung; Taijoon Chung; Yuen-Li Chung; Yong-Joon Chwae; Valentina Cianfanelli; Roberto Ciarcia; Iwona Ciechomska; Maria Rosa Ciriolo; Mara Cirone; Sofie Claerhout; Michael J Clague; Joan Claria; Peter Gh Clarke; Robert Clarke; Emilio Clementi; Cedric Cleyrat; Miriam Cnop; Eliana M Coccia; Tiziana Maria Cocco; Patrice Codogno; Jörn Coers; Ezra Ew Cohen; David Colecchia; Luisa Coletto; Núria Sánchez Coll; Emma Colucci-Guyon; Sergio Comincini; Maria Condello; Katherine Cook; Graham H Coombs; Cynthia D Cooper; J Mark Cooper; Isabelle Coppens; Maria Tiziana Corasaniti; Marco Corazzari; Ramon Corbalan; Elisabeth Corcelle-Termeau; Mario D Cordero; Cristina Corral Ramos; Olga Corti; Andrea Cossarizza; Paola Costelli; Safia Costes; Susan L Cotman; Ana Coto-Montes; Sandra Cottet; Eduardo Couve; Lori R Covey; L Ashley Cowart; Jeffery S Cox; Fraser P Coxon; Carolyn B Coyne; Mark Cragg; Rolf J Craven; Tiziana Crepaldi; Jose L Crespo; Alfredo Criollo; Valeria Crippa; Maria Teresa Cruz; Ana Maria Cuervo; Jose M Cuezva; Taixing Cui; Pedro R Cutillas; Mark J Czaja; Maria F Czyzyk-Krzeska; Ruben K Dagda; Uta Dahmen; Chunsun Dai; Wenjie Dai; Yun Dai; Kevin Dalby; Luisa Dalla Valle; Guillaume Dalmasso; Marcello D'Amelio; Markus Damme; Arlette Darfeuille-Michaud; Catherine Dargemont; Victor Darley-Usmar; Srinivasan Dasarathy; Biplab Dasgupta; Srikanta Dash; Crispin R Dass; Hazel Davey; Lester M Davids; David Dávila; Roger J Davis; Ted M Dawson; Valina L Dawson; Paula Daza; Jackie De Belleroche; Paul De Figueiredo; Regina Figueiredo; José De La Fuente; Luisa De Martino; Maria Antonietta De Matteis; Guido De Meyer; Angelo De Milito; Mauro De Santi; Wanderley De Souza; Vincenzo De Tata; Daniela De Zio; Jayanta Debnath; Reinhard Dechant; Jean-Paul Decuypere; Shane Deegan; Benjamin Dehay; Barbara Del Bello; Dominic P Del Re; Régis Delage-Mourroux; Lea Md Delbridge; Louise Deldicque; Elizabeth Delorme-Axford; Yizhen Deng; Joern Dengjel; Melanie Denizot; Paul Dent; Channing Der; Vojo Deretic; Benoît Derrien; Eric Deutsch; Timothy P Devarenne; Rodney J Devenish; Sabrina Di Bartolomeo; Nicola Di Daniele; Fabio Di Domenico; Alessia Di Nardo; Simone Di Paola; Antonio Di Pietro; Livia Di Renzo; Aaron DiAntonio; Guillermo Díaz-Araya; Ines Diaz-Laviada; Maria T Diaz-Meco; Javier Diaz-Nido; Chad A Dickey; Robert C Dickson; Marc Diederich; Paul Digard; Ivan Dikic; Savithrama P Dinesh-Kumar; Chan Ding; Wen-Xing Ding; Zufeng Ding; Luciana Dini; Jörg Hw Distler; Abhinav Diwan; Mojgan Djavaheri-Mergny; Kostyantyn Dmytruk; Renwick Cj Dobson; Volker Dotsch; Karol Dokladny; Svetlana Dokudovskaya; Massimo Donadelli; X Charlie Dong; Zheng Dong; Terrence M Donohue; Kelly S Doran; Gabriella D'Orazi; Gerald W Dorn; Victor Dosenko; Sami Dridi; Liat Drucker; Jie Du; Li-Lin Du; Lihuan Du; André Du Toit; Priyamvada Dua; Lei Duan; Pu Duann; Vikash Kumar Dubey; Michael Duchen; Michel A Duchosal; Helene Duez; Isabelle Dugail; Verónica I Dumit; Mara Duncan; Elaine Dunlop; William A Dunn; Nicolas Dupont; Luc Dupuis; Raul V. Duran; Thomas M Durcan; Stéphane Duvezin-Caubet; Umamaheswar Duvvuri; Vinay Eapen; Darius Ebrahimi-Fakhari; Arnaud Echard; Leopold Eckhart; Charles L Edelstein; Aimee L Edinger; Ludwig Eichinger; Tobias Eisenberg; Avital Eisenberg-Lerner; N Tony Eissa; Wafik S El-Deiry; Victoria El-Khoury; Zvulun Elazar; Hagit Eldar-Finkelman; Chris Elliott; Enzo Emanuele; Urban Emmenegger; Nikolai Engedal; Anna-Mart Engelbrecht; Simone Engelender; Jorrit M Enserink; Ralf Erdmann; Jekaterina Erenpreisa; Rajaraman Eri; Jason L Eriksen; Andreja Erman; Ricardo Escalante; Eeva-Liisa Eskelinen; Lucile Espert; Lorena Esteban-Martínez; Thomas J Evans; Mario Fabri; Gemma Fabrias; Cinzia Fabrizi; Antonio Facchiano; Nils Færgeman; Alberto Faggioni; Walter Fairlie; Chunhai Fan; Daping Fan; Jie Fan; Shengyun Fang; Manolis Fanto; Alessandro Fanzani; Thomas Farkas; Mathias Faure; Francois B Favier; Howard Fearnhead; Massimo Federici; Erkang Fei; Tania C Felizardo; Hua Feng; Yibin Feng; Yuchen Feng; Thomas A Ferguson; Álvaro Fernández Fernández; Maite G Fernandez-Barrena; José Carlos Fernández-Checa; Arsenio Fernández-López; Martin E Fernandez-Zapico; Olivier Feron; Elisabetta Ferraro; Carmen Veríssima Ferreira-Halder; Laszlo Fesus; Ralph Feuer; Fabienne Fiesel; Eduardo Chiela; Giuseppe Filomeni; Gian Maria Fimia; John Fingert; Steven Finkbeiner; Toren Finkel; Filomena Fiorito; Paul B Fisher; Marc Flajolet; Flavio Flamigni; Oliver Florey; Salvatore Florio; R Andres Floto; Marco Folini; Carlo Follo; Edward A Fon; Francesco Fornai; Franco Fortunato; Alessandro Fraldi; Rodrigo Franco; Arnaud Francois. 2016. "Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)." Autophagy 12, no. 1: 1-222.
Autophagy is a self-degradative physiological process by which the cell removes worn-out or damaged components. Constant at basal level it may become highly active in response to cellular stress. The type 2 transglutaminase (TG2), which accumulates under stressful cell conditions, plays an important role in the regulation of autophagy and cells lacking this enzyme display impaired autophagy/mitophagy and a consequent shift their metabolism to glycolysis. To further define the molecular partners of TG2 involved in these cellular processes, we analysed the TG2 interactome under normal and starved conditions discovering that TG2 interacts with various proteins belonging to different functional categories. Herein we show that TG2 interacts with pyruvate kinase M2 (PKM2), a rate limiting enzyme of glycolysis which is responsible for maintaining a glycolytic phenotype in malignant cells and displays non metabolic functions, including transcriptional co-activation and protein kinase activity. Interestingly, the ablation of PKM2 led to the decrease of intracellular TG2’s transamidating activity paralleled by an increase of its tyrosine phosphorylation. Along with this, a significant decrease of ULK1 and Beclin1 was also recorded, thus suggesting a block in the upstream regulation of autophagosome formation. These data suggest that the PKM2/TG2 interplay plays an important role in the regulation of autophagy in particular under cellular stressful conditions such as those displayed by cancer cells.
Sara Altuntas; Federica Rossin; Claudia Marsella; Manuela D'Eletto; Laura Diaz-Hidalgo; Maria Grazia Farrace; Michelangelo Campanella; Manuela Antonioli; Gian Maria Fimia; Mauro Piacentini. The transglutaminase type 2 and pyruvate kinase isoenzyme M2 interplay in autophagy regulation. Oncotarget 2015, 6, 44941 -44954.
AMA StyleSara Altuntas, Federica Rossin, Claudia Marsella, Manuela D'Eletto, Laura Diaz-Hidalgo, Maria Grazia Farrace, Michelangelo Campanella, Manuela Antonioli, Gian Maria Fimia, Mauro Piacentini. The transglutaminase type 2 and pyruvate kinase isoenzyme M2 interplay in autophagy regulation. Oncotarget. 2015; 6 (42):44941-44954.
Chicago/Turabian StyleSara Altuntas; Federica Rossin; Claudia Marsella; Manuela D'Eletto; Laura Diaz-Hidalgo; Maria Grazia Farrace; Michelangelo Campanella; Manuela Antonioli; Gian Maria Fimia; Mauro Piacentini. 2015. "The transglutaminase type 2 and pyruvate kinase isoenzyme M2 interplay in autophagy regulation." Oncotarget 6, no. 42: 44941-44954.
Nat. Cell Biol. 17, 20–30 (2015); published online 1 December 2014; corrected after print 1 April 2015 In the version of this Article originally published, incorrect western blot scans were provided for the actin panels in Figure 4h,i. These panels have been corrected online and are shown above. All samples in 4i were collected and processed simultaneously, on the same or on parallel gels/blots.
Valentina Cianfanelli; Claudia Fuoco; Mar Lorente; Maria Salazar; Fabio Quondamatteo; Pier Federico Gherardini; Daniela De Zio; Francesca Nazio; Manuela Antonioli; Melania D'Orazio; Tatjana Skobo; Matteo Bordi; Mikkel Rohde; Luisa Dalla Valle; Manuela Helmer-Citterich; Christine Gretzmeier; Joern Dengjel; Gian Maria Fimia; Mauro Piacentini; Sabrina DI Bartolomeo; Guillermo Velasco; Francesco Cecconi. Erratum: Corrigendum: AMBRA1 links autophagy to cell proliferation and tumorigenesis by promoting c-Myc dephosphorylation and degradation. Nature 2015, 17, 706 -706.
AMA StyleValentina Cianfanelli, Claudia Fuoco, Mar Lorente, Maria Salazar, Fabio Quondamatteo, Pier Federico Gherardini, Daniela De Zio, Francesca Nazio, Manuela Antonioli, Melania D'Orazio, Tatjana Skobo, Matteo Bordi, Mikkel Rohde, Luisa Dalla Valle, Manuela Helmer-Citterich, Christine Gretzmeier, Joern Dengjel, Gian Maria Fimia, Mauro Piacentini, Sabrina DI Bartolomeo, Guillermo Velasco, Francesco Cecconi. Erratum: Corrigendum: AMBRA1 links autophagy to cell proliferation and tumorigenesis by promoting c-Myc dephosphorylation and degradation. Nature. 2015; 17 (5):706-706.
Chicago/Turabian StyleValentina Cianfanelli; Claudia Fuoco; Mar Lorente; Maria Salazar; Fabio Quondamatteo; Pier Federico Gherardini; Daniela De Zio; Francesca Nazio; Manuela Antonioli; Melania D'Orazio; Tatjana Skobo; Matteo Bordi; Mikkel Rohde; Luisa Dalla Valle; Manuela Helmer-Citterich; Christine Gretzmeier; Joern Dengjel; Gian Maria Fimia; Mauro Piacentini; Sabrina DI Bartolomeo; Guillermo Velasco; Francesco Cecconi. 2015. "Erratum: Corrigendum: AMBRA1 links autophagy to cell proliferation and tumorigenesis by promoting c-Myc dephosphorylation and degradation." Nature 17, no. 5: 706-706.
Autophagy controls cell homeostasis and provides a rapid response to a variety of stresses. Although many steps of the autophagy process have been elucidated, how they are temporally regulated is less well characterized. Recently, we reported that dynamic interaction of the pro-autophagic factor AMBRA1 with CULLIN E3 ubiquitin ligases ensures the timely onset and termination of the autophagy response.
Manuela Antonioli; Federica Albiero; Mauro Piacentini; Gian Maria Fimia. Temporal regulation of autophagy response by the CULLIN 4-AMBRA1-CULLIN 5 axis. Molecular & Cellular Oncology 2015, 3, e1008304 .
AMA StyleManuela Antonioli, Federica Albiero, Mauro Piacentini, Gian Maria Fimia. Temporal regulation of autophagy response by the CULLIN 4-AMBRA1-CULLIN 5 axis. Molecular & Cellular Oncology. 2015; 3 (5):e1008304.
Chicago/Turabian StyleManuela Antonioli; Federica Albiero; Mauro Piacentini; Gian Maria Fimia. 2015. "Temporal regulation of autophagy response by the CULLIN 4-AMBRA1-CULLIN 5 axis." Molecular & Cellular Oncology 3, no. 5: e1008304.