We have cloned a protein, RBAP2, based upon its ability to bind to the retinoblastoma gene product in vitro. We have extended the clone to full- length status, shown that it is a nuclear phospho- protein, and that it binds to RB in vivo. This binding follows the same genetics as has been established for the interaction of RB and the viral oncoproteins large T antigen, E1A, and E7. This grant now proposes to investigate the biochemical and biological functions of RBAP2 and, in addition, the role of RBAP2 in RB mediated cell-cycle regulation.

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Physician Scientist Award (K11)
Project #
5K11CA065594-05
Application #
2895194
Study Section
Cancer Institutional Fellowship Review Committee (CT)
Program Officer
Gorelic, Lester S
Project Start
1995-04-01
Project End
2000-03-31
Budget Start
1999-04-01
Budget End
2000-03-31
Support Year
5
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Dana-Farber Cancer Institute
Department
Type
DUNS #
149617367
City
Boston
State
MA
Country
United States
Zip Code
02215
Vazquez, F; Ramaswamy, S; Nakamura, N et al. (2000) Phosphorylation of the PTEN tail regulates protein stability and function. Mol Cell Biol 20:5010-8