The γ-H2A.X:: Is it just a surrogate marker of double-strand breaks or much more?

被引：91

作者：

Ismail, Ismail Hassan ^{[1
,2
]}

Hendzel, Michael J. ^{[1
]}

机构：

[1] Univ Alberta, Dept Oncol, Edmonton, AB, Canada

[2] Cairo Univ, Fac Sci, Dept Biophys, Giza, Egypt

来源：

ENVIRONMENTAL AND MOLECULAR MUTAGENESIS | 2008年 / 49卷 / 01期

关键词：

histone H2A.X; DNA damage; DNA repair; chromatin; epigenetics;

D O I：

10.1002/em.20358

中图分类号：

X [环境科学、安全科学];

学科分类号：

08 ; 0830 ;

摘要：

In recent years, several histone modifications have been implicated in the cellular response to DNA double-strand breaks (DSBs). One of the best characterized histone modifications important in DSB repair is the phosphorylation of histone H2A variant, H2AX In response to DSBs, H2A.X is phosphorylated and this phosphorylation is required for DSB signaling and the retention of repair proteins at the break site. Despite the existing picture that the function of H2A.X is to promote DNA repair, very recent data suggest that the phosphorylation of histone H2A.X has additional functions. This is analogous to histone H3 phosphorylation on serine 10, which participates in seemingly incompatible functions-transcriptional activation and mitosis. In this review, we discuss the role of histone H2A.X in maintaining genomic stability and review emerging evidence that histone H2A.X is multifunctional.

引用

页码：73 / 82

页数：10

共 88 条

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