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Semin Cancer Biol. 2010 Feb;20(1):29-39. doi: 10.1016/j.semcancer.2009.10.004. Epub 2009 Nov 6.

Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy.

Author information

  • 1CR-UK Cell Transformation Research Group, Department of Surgery and Molecular Oncology, Ninewells Hospital and Medical School, University of Dundee, Dundee, Scotland, United Kingdom.

Abstract

Ubiquitination plays a key role in regulating the tumour suppressor p53. It targets p53 for degradation by the 26S proteasome. The ubiquitin pathway also regulates the activity and localisation of p53. Ubiquitination requires ubiquitin-activating and -conjugating enzymes and ubiquitin ligases. In addition, ubiquitination can be reversed by the action of deubiquitinating enzymes. Here we give an overview of the role of components of the ubiquitin-proteasome system in the regulation of p53 and review progress in targeting these proteins to activate wild-type p53 for the treatment of cancer.

Copyright (c) 2009. Published by Elsevier Ltd.

PMID:
19897040
[PubMed - indexed for MEDLINE]
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