Paving the way for H2AX phosphorylation Chromatin changes in the DNA damage response

被引：30

作者：

Ayoub, Nabieh ^{[1
]}

Jeyasekharan, Anand D. ^{[1
]}

Bernal, Juan A. ^{[1
]}

Venkitaraman, Ashok R. ^{[1
]}

机构：

[1] MRC, Canc Cell Unit, Cambridge, England

来源：

CELL CYCLE | 2009年 / 8卷 / 10期

基金：

英国惠康基金; 英国医学研究理事会;

关键词：

heterochromatin; euchromatin; HP1; beta; casein kinase 2 (CK2); DNA damage; H2AX phosphorylation; FRAP; FLIP; 2D gels; PROTEIN-KINASE CK2; HETEROCHROMATIN-ASSOCIATED PROTEIN; HISTONE METHYLTRANSFERASE ACTIVITY; NONHISTONE CHROMOSOMAL-PROTEIN; DOUBLE-STRAND BREAKS; JMJC DOMAIN PROTEIN; FACILITATES REPAIR; H4-K16; ACETYLATION; REMODELER RSC; NUCLEAR FOCI;

D O I：

10.4161/cc.8.10.8501

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The dynamics of chromatin-associated proteins control the accessibility of DNA to essential biological transactions like transcription, replication, recombination and repair. Here, we briefly outline what is known about the chromatin changes that occur during the cellular response to DNA breakage, focusing on our recent findings revealing that the chromatin factor HP1 beta is mobilized within seconds after DNA damage by an unrecognized signaling cascade mediated by casein kinase 2 (CK2) phosphorylation, paving the way for histone H2AX phosphorylation. We also show here that HP1 beta mobilization is neither associated with histone H3 modification on Ser10, an alteration proposed to assist in HP1 ejection from chromatin, nor with evidence of a physical interaction between HP1 beta and the CK2 regulatory subunit. Interestingly, following its rapid mobilization, we find that HP1 beta gradually re-accumulates on damaged chromatin over a longer time period, suggesting that temporal changes in HP1 beta dynamics and interaction with chromatin may assist in different stages of the cellular response to DNA breakage.

引用

页码：1494 / 1500

页数：7

共 91 条

[1] Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31 [J].