Prof. Michelle Hill
Precision & Systems Biomedicine Laboratory, QIMR Berghofer Medical Research Institute, Brisbane, QLD 4006, Australia
+1
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Academic Career Length
30Years (1997-Present)
(Calculated once Scilit publication data is synced: current year − year of first publication + 1)
Representative Publications
View All Publications1 January 2008 in Cell
Journal Article
Michelle HillMBMichele Bastiani
Michele BastianiRLRobert Luetterforst
Robert Luetterforst
MKMatthew Kirkham
Matthew KirkhamAKAnnika Kirkham
Annika Kirkham
RPRobert G. Parton
Robert G. Parton +6
10 November 2014 in Bioinformatics
Journal Article
DKDae-Kyum Kim
Dae-Kyum Kim
JLJaewook Lee
Jaewook Lee
SKSae Rom Kim
Sae Rom Kim
DCDongsic Choi
Dongsic ChoiYYYae Jin Yoon
Yae Jin Yoon
YGYong Song Gho
Yong Song Gho +89
Motivation: Extracellular vesicles (EVs) are spherical bilayered proteolipids, harboring various bioactive molecules. Due to the complexity of the vesicular nomenclatures and components, online searches for EV-related publications and vesicular components are currently challenging. Results: We present an improved version of EVpedia, a public database for EVs research. This community web portal contains a database of publications and vesicular components, identification of orthologous vesicular components, bioinformatic tools and a personalized function. EVpedia includes 6879 publications, 172 080 vesicular components from 263 high-throughput datasets, and has been accessed more than 65 000 times from more than 750 cities. In addition, about 350 members from 73 international research groups have participated in developing EVpedia. This free web-based database might serve as a useful resource to stimulate the emerging field of EV research. Availability and implementation: The web site was implemented in PHP, Java, MySQL and Apache, and is freely available at http://evpedia.info. Contact:ysgho@postech.ac.kr
16 August 2010 in Journal of Cell Biology
Journal Article
MHMark T. Howes
Mark T. HowesMKMatthew Kirkham
Matthew KirkhamJRJames Riches
James Riches
Katia CortesePWPiers J. Walser
Piers J. Walser
RPRobert G. Parton
Robert G. Parton +15
Although the importance of clathrin- and caveolin-independent endocytic pathways has recently emerged, key aspects of these routes remain unknown. Using quantitative ultrastructural approaches, we show that clathrin-independent carriers (CLICs) account for approximately three times the volume internalized by the clathrin-mediated endocytic pathway, forming the major pathway involved in uptake of fluid and bulk membrane in fibroblasts. Electron tomographic analysis of the 3D morphology of the earliest carriers shows that they are multidomain organelles that form a complex sorting station as they mature. Proteomic analysis provides direct links between CLICs, cellular adhesion turnover, and migration. Consistent with this, CLIC-mediated endocytosis of key cargo proteins, CD44 and Thy-1, is polarized at the leading edge of migrating fibroblasts, while transient ablation of CLICs impairs their ability to migrate. These studies provide the first quantitative ultrastructural analysis and molecular characterization of the major endocytic pathway in fibroblasts, a pathway that provides rapid membrane turnover at the leading edge of migrating cells.
22 June 2009 in Journal of Cell Biology
Journal Article
MBMichele Bastiani
Michele BastianiLLLibin Liu
Libin LiuMichelle HillMJMark P. Jedrychowski
Mark P. Jedrychowski
SNSusan J. Nixon
Susan J. NixonRPRobert G. Parton
Robert G. Parton +11
Polymerase I and transcript release factor (PTRF)/Cavin is a cytoplasmic protein whose expression is obligatory for caveola formation. Using biochemistry and fluorescence resonance energy transfer–based approaches, we now show that a family of related proteins, PTRF/Cavin-1, serum deprivation response (SDR)/Cavin-2, SDR-related gene product that binds to C kinase (SRBC)/Cavin-3, and muscle-restricted coiled-coil protein (MURC)/Cavin-4, forms a multiprotein complex that associates with caveolae. This complex can constitutively assemble in the cytosol and associate with caveolin at plasma membrane caveolae. Cavin-1, but not other cavins, can induce caveola formation in a heterologous system and is required for the recruitment of the cavin complex to caveolae. The tissue-restricted expression of cavins suggests that caveolae may perform tissue-specific functions regulated by the composition of the cavin complex. Cavin-4 is expressed predominantly in muscle, and its distribution is perturbed in human muscle disease associated with Caveolin-3 dysfunction, identifying Cavin-4 as a novel muscle disease candidate caveolar protein.
22 April 2004 in The EMBO Journal
Journal Article
Michelle Hill
Colin AdrainPDPatrick J Duriez
Patrick J Duriez
ECEmma M Creagh
Emma M CreaghSMSeamus J Martin
Seamus J MartinThe Apaf‐1 apoptosome is a multi‐subunit caspase‐activating scaffold that is assembled in response to diverse forms of cellular stress that culminate in apoptosis. To date, most studies on apoptosome composition and function have used apoptosomes reassembled from recombinant or purified proteins. Thus, the precise composition of native apoptosomes remains unresolved. Here, we have used a one‐step immunopurification approach to isolate catalytically active Apaf‐1/caspase‐9 apoptosomes, and have identified the major constituents of these complexes using mass spectrometry methods. Using this approach, we have also assessed the ability of putative apoptosome regulatory proteins, such as Smac/DIABLO and PHAPI, to regulate the activity of native apoptosomes. We show that Apaf‐1, caspase‐9, caspase‐3 and XIAP are the major constituents of native apoptosomes and that cytochrome c is not stably associated with the active complex. We also demonstrate that the IAP‐neutralizing protein Smac/DIABLO and the tumor‐suppressor protein PHAPI can enhance the catalytic activity of apoptosome complexes in distinct ways. Surprisingly, PHAPI also enhanced the activity of purified caspase‐3, suggesting that it may act as a co‐factor for this protease.
25 June 2012 in EMBO Molecular Medicine
Journal Article
NSNicholas A. Saunders
Nicholas A. SaundersFSFiona Simpson
Fiona SimpsonETErik Walter Thompson
Erik Walter ThompsonMichelle HillLELiliana Endo‐Munoz
Liliana Endo‐MunozAGAlexander Guminski
Alexander Guminski
+2
Drug resistance continues to be a major barrier to the delivery of curative therapies in cancer. Historically, drug resistance has been associated with over‐expression of drug transporters, changes in drug kinetics or amplification of drug targets. However, the emergence of resistance in patients treated with new‐targeted therapies has provided new insight into the complexities underlying cancer drug resistance. Recent data now implicate intratumoural heterogeneity as a major driver of drug resistance. Single cell sequencing studies that identified multiple genetically distinct variants within human tumours clearly demonstrate the heterogeneous nature of human tumours. The major contributors to intratumoural heterogeneity are (i) genetic variation, (ii) stochastic processes, (iii) the microenvironment and (iv) cell and tissue plasticity. Each of these factors impacts on drug sensitivity. To deliver curative therapies to patients, modification of current therapeutic strategies to include methods that estimate intratumoural heterogeneity and plasticity will be essential.
About Me
Michelle Hill obtained her PhD at the University of Queensland on insulin signalling using phosphoproteomics. Her postdoctoral work in Switzerland, Ireland and at the Institute for Molecular Bioscience, University of Queensland focussed on various aspects of signalling using subcellular proteomics. With a passion for translational proteomics research, she established the Cancer Proteomics Group at the University of Queensland Diamantina Institute in 2009. After successfully developing clinical proteomics research, and establishing a proteomics amyloid typing test for the Princess Alexandra Hospital in Brisbane, Associate Professor Hill moved her laboratory to QIMR Berghofer in 2017 to broaden her research. The Precision and Systems BioMedicine Laboratory aims to improve modifiable health outcomes by developing better diagnostics and integrative study of cell membrane disturbance that lead to diseases such as cancers, chronic diseases and infection. The program focus on early disease detection and non-drug prevention approaches, to provide tools for actively maintaining health. Their research combines cell biology and biochemistry knowledge with cutting edge multi-omics technologies in the wet-lab with sophisticated computational algorithms (dry-lab) to model the complex biomolecular systems.