Arginine methylation regulates the p53 response

Martin Jansson; Stephen T Durant; Er-Chieh Cho; Sharon Sheahan; Mariola Edelmann; Benedikt Kessler; Nicholas B La Thangue

doi:10.1038/ncb1802

Arginine methylation regulates the p53 response

Martin Jansson, Stephen T Durant, Er-Chieh Cho, Sharon Sheahan, Mariola Edelmann, Benedikt Kessler, Nicholas B La Thangue

303 Citations (Scopus)

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.

Original language	English
Journal	Nature Cell Biology
Volume	10
Issue number	12
Pages (from-to)	1431-9
Number of pages	8
ISSN	1465-7392
DOIs	https://doi.org/10.1038/ncb1802
Publication status	Published - 2008

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title = "Arginine methylation regulates the p53 response",

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.",

author = "Martin Jansson and Durant, {Stephen T} and Er-Chieh Cho and Sharon Sheahan and Mariola Edelmann and Benedikt Kessler and {La Thangue}, {Nicholas B}",

note = "Keywords: Amino Acid Sequence; Apoptosis; Arginine; Carrier Proteins; Hela Cells; Humans; Methylation; Molecular Sequence Data; Mutant Proteins; Protein Binding; Protein Methyltransferases; Protein Structure, Quaternary; Protein Transport; Tumor Suppressor Protein p53",

year = "2008",

doi = "10.1038/ncb1802",

language = "English",

volume = "10",

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journal = "Nature Cell Biology",

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TY - JOUR

T1 - Arginine methylation regulates the p53 response

AU - Jansson, Martin

AU - Durant, Stephen T

AU - Cho, Er-Chieh

AU - Sheahan, Sharon

AU - Edelmann, Mariola

AU - Kessler, Benedikt

AU - La Thangue, Nicholas B

N1 - Keywords: Amino Acid Sequence; Apoptosis; Arginine; Carrier Proteins; Hela Cells; Humans; Methylation; Molecular Sequence Data; Mutant Proteins; Protein Binding; Protein Methyltransferases; Protein Structure, Quaternary; Protein Transport; Tumor Suppressor Protein p53

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

U2 - 10.1038/ncb1802

DO - 10.1038/ncb1802

M3 - Journal article

C2 - 19011621

SN - 1465-7392

VL - 10

SP - 1431

EP - 1439

JO - Nature Cell Biology

JF - Nature Cell Biology

IS - 12

ER -

Arginine methylation regulates the p53 response

Abstract

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