The critical tumour suppressor p53 plays a major role in response to DNA damage and, more generally, to genotoxic stress. The regulation of its expression and functions is under very tight controls, and involves, in particular, an extremely complex set of post-translational modifications, thanks to a variety of ‘modifiers’, including ubiquitylation E3s and acetyltransferases, that fine-tune the stability and activity of the protein. Work of the last few years has revealed that, in addition to targeting p53, these modifiers also modify each other, forming an intricate network of regulatory molecules and events that must be taken into account to understand p53 regulation. We propose that this network allows a metastable equilibrium that confers both sensitivity and robustness on the p53 pathway, two properties that allow the pathway to respectively answer to a variety of stimuli and return to its initial stage when the stimuli disappear.
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February 2010
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Conference Article|
January 19 2010
Lessons from interconnected ubiquitylation and acetylation of p53: think metastable networks
Monsef Benkirane;
Monsef Benkirane
*IGH, CNRS, UPR 1142, 141 rue de la Cardonille, 34396 Montpellier cedex 5, France
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Claude Sardet;
Claude Sardet
†IGMM, CNRS, UMR 5535, Montpellier University, 1919 route de Mende, 34293 Montpellier cedex 5, France
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Olivier Coux
Olivier Coux
1
‡CRBM, CNRS, UMR 5237, Montpellier University, 1919 route de Mende, 34293 Montpellier cedex 5, France
1To whom correspondence should be addressed (email olivier.coux@crbm.cnrs.fr).
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Publisher: Portland Press Ltd
Received:
November 09 2009
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2010 Biochemical Society
2010
Biochem Soc Trans (2010) 38 (1): 98–103.
Article history
Received:
November 09 2009
Citation
Monsef Benkirane, Claude Sardet, Olivier Coux; Lessons from interconnected ubiquitylation and acetylation of p53: think metastable networks. Biochem Soc Trans 1 February 2010; 38 (1): 98–103. doi: https://doi.org/10.1042/BST0380098
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