Article abstract
Nature Cell Biology 10, 1431 - 1439 (2008)
Published online: 16 November 2008 | doi:10.1038/ncb1802
Arginine methylation regulates the p53 response
Martin Jansson1, Stephen T. Durant1, Er-Chieh Cho1, Sharon Sheahan1, Mariola Edelmann2, Benedikt Kessler2 & Nicholas B. La Thangue1
Abstract
Activation of the p53 tumour suppressor protein in response to DNA damage leads to apoptosis or cell-cycle arrest. Enzymatic modifications are widely believed to affect and regulate p53 activity. We describe here a level of post-translational control that has an important functional consequence on the p53 response. We show that the protein arginine methyltransferase (PRMT) 5, as a co-factor in a DNA damage responsive co-activator complex that interacts with p53, is responsible for methylating p53. Arginine methylation is regulated during the p53 response and affects the target gene specificity of p53. Furthermore, PRMT5 depletion triggers p53-dependent apoptosis. Thus, methylation on arginine residues is an underlying mechanism of control during the p53 response.
- Laboratory of Cancer Biology, Department of Clinical Pharmacology, Medical Sciences Division, University of Oxford, Old Road Campus Research Building, Old Road Campus, off Roosevelt Drive, Oxford, OX3 7DQ, UK.
- Henry Wellcome Building for Molecular Physiology, Nuffield Department of Clinical Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
Correspondence to: Nicholas B. La Thangue1 e-mail: nick.lathangue@ndcls.ox.ac.uk
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