Modifications of P53: Competing for the Lysines

Overview

Journal Curr Opin Genet Dev

Publisher Elsevier

Specialties Biology
Genetics

Date 2009 Jan 31

PMID 19179064

Citations 32

Authors

Stephanie Carter

Karen H Vousden

Affiliations

Soon will be listed here.

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.

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