4.5 Article

A novel site of AKT-mediated phosphorylation in the human MDM2 onco-protein

Journal

FEBS LETTERS
Volume 577, Issue 1-2, Pages 270-276

Publisher

WILEY
DOI: 10.1016/j.febslet.2004.09.081

Keywords

MDM2; AKT; phosphorylation; p53; survival signaling

Ask authors/readers for more resources

MDM2 is an E3 ubiquitin ligase which mediates ubiquitylation and proteasome-dependent degradation of the p53 tumor suppressor protein. Phosphorylation of MDM2 by the protein kinase AKT is thought to regulate MDM2 function in response to survival signals, but there has been uncertainty concerning the identity of the sites phosphorylated by AKT. In the present study, we identify Ser-166, a site previously reported as an AKT target, and Ser-188, a novel site which is the major site of phosphorylation of MDM2 by AKT in vitro. Analysis of MDM2 in cultured cells confirms that Ser-166 and Ser-188 are phosphorylated by AKT in a physiological context. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available