p53 regulation by ubiquitin.

Abstract

The ubiquitination pathway is a highly dynamic and coordinated process that regulates degradation as well as numerous processes of proteins within a cell. The p53 tumor suppressor and several factors in the pathway are regulated by ubiquitin as well as ubiquitin-like proteins. These modifications are critical for the function of p53 and control both the degradation of the protein as well as localization and activity. Importantly, more recent studies have identified deubiquitination enzymes that can specifically remove ubiquitin moieties from p53 or other factors in the pathway, and the reversible nature of this process adds yet another layer of regulatory control of p53. This review highlights the recent advances in our knowledge of ubiquitin and the p53 pathway.

• Authors: Christopher L Brooks, Wei Gu
• Journal: FEBS letters (FEBS Lett) Vol. 585 Issue 18 Pg. 2803-9 (Sep 16 2011) ISSN: 1873-3468 [Electronic] England
• PMID: 21624367 (Publication Type: Journal Article, Review)
• Copyright: Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Chemical References

• Tumor Suppressor Protein p53
• Ubiquitin
• Proto-Oncogene Proteins c-mdm2
• Proteasome Endopeptidase Complex
• ATP dependent 26S protease

Topics

• Active Transport, Cell Nucleus
• Animals
• Humans
• Models, Biological
• Proteasome Endopeptidase Complex (metabolism)
• Proto-Oncogene Proteins c-mdm2 (metabolism)
• Transcriptional Activation
• Tumor Suppressor Protein p53 (genetics, metabolism)
• Ubiquitin (metabolism)
• Ubiquitination