Arginine methylation regulates the p53 response

The tumour suppressor p53 is subject to complex regulation and arginine methylation is now shown to provide an additional level of control. The protein arginine methyltransferase (PRMT) 5 is recruited by Strap to methylate p53 in response to DNA damage, governing the p53 response. Activation of the...

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Bibliographic Details
Published in:	Nature cell biology Vol. 10; no. 12; pp. 1431 - 1439
Main Authors:	Jansson, Martin, Durant, Stephen T., Cho, Er-Chieh, Sheahan, Sharon, Edelmann, Mariola, Kessler, Benedikt, La Thangue, Nicholas B.
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 01.12.2008 Nature Publishing Group
Subjects:	Amino Acid Sequence Apoptosis Arginine - metabolism Biomedical and Life Sciences Cancer Research Carrier Proteins - isolation & purification Carrier Proteins - metabolism Cell Biology Cyclin-dependent kinases Deoxyribonucleic acid Developmental Biology DNA DNA damage DNA methylation HeLa Cells Humans Kinases Life Sciences Methylation Molecular Sequence Data Mutant Proteins - metabolism Phosphorylation Polypeptides Protein Binding Protein Methyltransferases - chemistry Protein Methyltransferases - metabolism Protein Structure, Quaternary Protein Transport Protein-Arginine N-Methyltransferases Proteins Stem Cells Tumor Suppressor Protein p53 - metabolism United Kingdom > UK
ISSN:	1465-7392, 1476-4679, 1476-4679
Online Access:	Get full text
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