Journal
CANCER CELL
Volume 5, Issue 1, Pages 67-78Publisher
CELL PRESS
DOI: 10.1016/S1535-6108(03)00331-3
Keywords
-
Categories
Funding
- NCI NIH HHS [CA 80240] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA080240] Funding Source: NIH RePORTER
Ask authors/readers for more resources
We show in this study that endogenous NEP and PTEN associate in cells directly through electrostatic interactions between a highly basic residue stretch in the intracellular domain of NEP and the major phosphorylation site in PTEN's tail. NEP binds and engages in higher order complexes both phosphorylated and unphosphorylated PTEN. NEP recruits PTEN to the plasma membrane and enhances its stability and phosphatase activity. As a result, an enzymatically inactive NEP mutant preserves the ability to bind PTEN, inactivates the Akt/PKB kinase, and partially suppresses the growth of PC cells. This study demonstrates a molecular cooperation between NEP and PTEN tumor suppressors in which NEP constitutively recruits and activates PTEN to inhibit the PI3K/Akt oncogenic pathway.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available