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Updated: Jun 26, 2026

Yeast As a Chassis for Developing Functional Assays to Study Human P53
Published on: August 4, 2019
Modifications of p53: competing for the lysines
Stephanie Carter1, Karen H Vousden
1The Beatson Institute for Cancer Research, Garscube Estate, Switchback Road, Bearsden, Glasgow, UK.
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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