Modifications of p53: competing for the lysines

Carter, S. and Vousden, K. (2009) Modifications of p53: competing for the lysines. Current Opinion in Genetics and Development, 19(1), pp. 18-24. (doi:10.1016/j.gde.2008.11.010)

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Publisher's URL: http://dx.doi.org/10.1016/j.gde.2008.11.010

Abstract

The p53 tumour suppressor protein is subject to numerous post-translational modifications, which coalesce in various combinations and patterns to regulate its activity. In addition to a multitude of phosphorylated serines and threonines, many of the lysine residues in p53 can be modified to regulate activity, stability and subcellular localization of the protein. This complexity is amplified by the variety of modifications that can target the same lysine residue - often with opposing effects on p53 function

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Vousden, Karen and Carter, Dr Stephanie
Authors: Carter, S., and Vousden, K.
College/School:College of Medical Veterinary and Life Sciences > Institute of Cancer Sciences
Journal Name:Current Opinion in Genetics and Development
ISSN:0959437X

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