Posttranslational Modification of MDM2

The functions of the MDM2 protein, in particular its E3 ubiquitin ligase activity and its ability to interact with a number of cellular proteins intimately involved in growth regulation, are modulated by sumoylation and multisite phosphorylation. These posttranslational mechanisms not only regulate...

Full description

Saved in:
Bibliographic Details
Published inMolecular cancer research Vol. 1; no. 14; pp. 1017 - 1026
Main Authors Meek, David W, Knippschild, Uwe
Format Journal Article
LanguageEnglish
Published United States American Association for Cancer Research 01.12.2003
Subjects
Humans
Nuclear Proteins - metabolism
Protein Processing, Post-Translational - physiology
Proto-Oncogene Proteins - metabolism
Proto-Oncogene Proteins c-mdm2
Online AccessGet full text

Cover

More Information
Summary:The functions of the MDM2 protein, in particular its E3 ubiquitin ligase activity and its ability to interact with a number of cellular proteins intimately involved in growth regulation, are modulated by sumoylation and multisite phosphorylation. These posttranslational mechanisms not only regulate the intrinsic activity of MDM2 in response to cellular stresses, but also govern its subcellular localization, differentiate between MDM2-mediated ubiquitination of p53 and autoubiquitination, integrate the stress response with mechanisms that mediate cell survival, and modulate the interaction of MDM2 with cellular and viral proteins. In this review, we summarize our current knowledge of the role of posttranslational modifications of MDM2 and their functional relevance.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ISSN:1541-7786
1557-3125