Renu Wadhwa

Dr. Renu Wadhwa

1. Biomedical Research Institute, National Institute of Advanced Industrial Science & Technology (AIST), Central 5-41, 1-1-1 Higashi, Tsukuba, Ibaraki - 305 8565, Japan</br>2. School of Integrative and Global Majors (SIGMA), University of Tsukuba, 1-1-1 Tennoudai, Tsukuba, Ibaraki, 305-8572, Japan
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Research Focus & Metrics

Academic Career Length

44Years (1983-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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15 February 1999 in Genes & Development
Verified
Journal Article
Open access
PDF file
TNTeruaki Nomura
Teruaki Nomura
MKMatiullah Khan
Matiullah Khan
Sunil KaulSunil Kaul
Sunil Kaul
HDHai-Dong Dong
Hai-Dong Dong
RWRenu Wadhwa
Renu Wadhwa
SIShunsuke Ishii
Shunsuke Ishii
The N-CoR/SMRT complex containing mSin3 and histone deacetylase (HDAC) mediates transcriptional repression by nuclear hormone receptors and Mad. The proteins encoded by the skiproto-oncogene family directly bind to N-CoR/SMRT and mSin3A, and forms a complex with HDAC. c-Ski and its related gene product Sno are required for transcriptional repression by Mad and thyroid hormone receptor (TRβ). The oncogenic form, v-Ski, which lacks the mSin3A-binding domain, acts in a dominant-negative fashion, and abrogates transcriptional repression by Mad and TRβ. Inski-deficient mouse embryos, the ornithine decarboxylase gene, whose expression is normally repressed by Mad–Max, is expressed ectopically. These results show that Ski is a component of the HDAC complex and that Ski is required for the transcriptional repression mediated by this complex. The involvement of c-Ski in the HDAC complex indicates that the function of the HDAC complex is important for oncogenesis.

1 January 2002 in Cell Stress and Chaperones
Verified
Journal Article
Closed access
RWRenu Wadhwa
Renu Wadhwa
KTKazunari Taira
Kazunari Taira
Sunil KaulSunil Kaul
Sunil Kaul
Mortalin/mthsp70/PBP74/Grp75 (called mortalin hereafter), a member of the Hsp70 family of chaperones, was shown to have different subcellular localizations in normal and immortal cells. It has been assigned to multiple subcellular sites and implicated in multiple functions ranging from stress response, intracellular trafficking, antigen processing, control of cell proliferation, differentiation, and tumorigenesis. The present article compiles and reviews information on the multiple sites and functions of mortalin in different organisms. The relevance of its differential distributions and functions in normal and immortal cell phenotypes is discussed.

1 April 2007 in Experimental Gerontology
Verified
Journal Article
Closed access
Sunil KaulSunil Kaul
Sunil Kaul
CDCuster C. Deocaris
Custer C. Deocaris
RWRenu Wadhwa
Renu Wadhwa

1 July 2006 in Molecular & Cellular Proteomics
Verified
Journal Article
Open access
PDF file
JJJinghua Jin
Jinghua Jin
CHChristine Hulette
Christine Hulette
YWYan Wang
Yan Wang
TZTerry Zhang
Terry Zhang
CPCatherine Pan
Catherine Pan
JZJing Zhang
Jing Zhang
Functional impairment of mitochondria and proteasomes and increased oxidative damage comprise the main pathological phenotypes of Parkinson disease (PD). Using an unbiased quantitative proteomic approach, we compared nigral mitochondrial proteins of PD patients with those from age-matched controls. 119 of 842 identified proteins displayed significant differences in their relative abundance (increase/decrease) between the two groups. We confirmed that one of these, mortalin (mthsp70/GRP75, a mitochondrial stress protein), is substantially decreased in PD brains as well as in a cellular model of PD. In addition, nine candidate mortalin-binding partners were identified as potential mediators of PD pathology. Manipulations of mortalin level in dopaminergic neurons resulted in significant changes in sensitivity to PD phenotypes via pathways involving mitochondrial and proteasomal function as well as oxidative stress.

19 January 2006 in International Journal of Cancer
Verified
Journal Article
Open access
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RWRenu Wadhwa
Renu Wadhwa
STSyuichi Takano
Syuichi Takano
KKKamaljit Kaur
Kamaljit Kaur
CDCuster C. Deocaris
Custer C. Deocaris
OPOlivia M. Pereira‐Smith
Olivia M. Pereira‐Smith
Sunil KaulSunil Kaul
Sunil Kaul
Mortalin, also known as mthsp70/GRP75/PBP74, interacts with the tumor suppressor protein p53 and inactivates its transcriptional activation and apoptotic functions. Here, we examined the level of mortalin expression in a large variety of tumor tissues, tumor‐derived and in vitro immortalized human cells. It was elevated in many human tumors, and in all of the tumor‐derived and in vitro immortalized cells. In human embryonic fibroblasts immortalized with an expression plasmid for hTERT, the telomerase catalytic subunit, with or without human papillomavirus E6 and E7 genes, we found that subclones with spontaneously increased mortalin expression levels became anchorage‐independent and acquired the ability to form tumors in nude mice. Furthermore, overexpression of mortalin was sufficient to increase the malignancy of breast carcinoma cells. The study demonstrates that upregulation of mortalin contributes significantly to tumorigenesis, and thus is a good candidate target for cancer therapy.

1 November 1998 in Journal of Biological Chemistry
Verified
Journal Article
Open access
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RWRenu Wadhwa
Renu Wadhwa
STSyuichi Takano
Syuichi Takano
MRMartin Robert
Martin Robert
AYAkiko Yoshida
Akiko Yoshida
HNHitoshi Nomura
Hitoshi Nomura
Sunil KaulSunil Kaul
Sunil Kaul
The mortalin genes, mot-1 andmot-2, are hsp70 family members that were originally cloned from normal and immortal murine cells, respectively. Their proteins differ by only two amino acid residues but exhibit different subcellular localizations, arise from two distinct genes, and have contrasting biological activities. We report here that the two proteins also differ in their interactions with the tumor suppressor protein p53. The pancytosolic mot-1 protein in normal cells did not show colocalization with p53; in contrast, nonpancytosolic mot-2 and p53 overlapped significantly in immortal cells. Transfection ofmot-2 but not mot-1 resulted in the repression of p53-mediated transactivation in p53-responsive reporter assays. Inactivation of p53 by mot-2 was supported by the down-regulation of p53-responsive genes p21WAF-1 andmdm-2 in mot-2-transfected cells only. Furthermore, NIH 3T3 cells transfected with expression plasmid encoding green fluorescent protein-taggedmot-2 but not mot-1 showed an abrogation of nuclear translocation of wild-type p53. These results demonstrate a novel mechanism of p53 inactivation by mot-2 protein.