Abstract

This is an R29 proposal to study the interaction of c-abl and p53. The c-abl binding site on p53 will be determined by mutagenesis and correlated with biological activity. The effects of c-abl on p53 DNA binding and in vitro transcription activity will be tested. Finally the possibility that c-abl is a coactivator will be studied by testing for a transcriptional activation domain in c-abl using GAL4-c-abl constructs.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
First Independent Research Support & Transition (FIRST) Awards (R29)
Project #
5R29CA075180-02
Application #
2733376
Study Section
Biological Sciences 2 (BIOL)
Program Officer
Marks, Cheryl L
Project Start
1997-07-15
Project End
2002-06-30
Budget Start
1998-07-01
Budget End
1999-06-30
Support Year
2
Fiscal Year
1998
Total Cost
Indirect Cost

  Institution

Name
University of California Riverside
Department
Biochemistry
Type
Schools of Earth Sciences/Natur
DUNS #
City
Riverside
State
CA
Country
United States
Zip Code
92521

  Publications

Wu, Yong; Lee, Sangkyu; Bobadilla, Selene et al. (2017) High glucose-induced p53 phosphorylation contributes to impairment of endothelial antioxidant system. Biochim Biophys Acta Mol Basis Dis 1863:2355-2362
Wu, Yong; Zhou, Hillary; Wu, Ke et al. (2014) PTEN phosphorylation and nuclear export mediate free fatty acid-induced oxidative stress. Antioxid Redox Signal 20:1382-95
Shouse, G P; Nobumori, Y; Panowicz, M J et al. (2011) ATM-mediated phosphorylation activates the tumor-suppressive function of B56?-PP2A. Oncogene 30:3755-65
Shouse, G P; Nobumori, Y; Liu, X (2010) A B56gamma mutation in lung cancer disrupts the p53-dependent tumor-suppressor function of protein phosphatase 2A. Oncogene 29:3933-41