Human POGZ modulates dissociation of HP1α from mitotic chromosome arms through Aurora B activation

被引：202

作者：

Nozawa, Ryu-Suke ^{[1
]}

Nagao, Koji ^{[1
,2
]}

Masuda, Hiro-Taka ^{[1
]}

Iwasaki, Osamu ^{[1
]}

Hirota, Toru ^{[3
]}

Nozaki, Naohito ^{[4
]}

Kimura, Hiroshi ^{[5
]}

Obuse, Chikashi ^{[1
]}

机构：

[1] Hokkaido Univ, Grad Sch Life Sci, Sapporo, Hokkaido 0010021, Japan

[2] Okinawa Inst Sci & Technol, Initial Res Project, Okinawa 9042234, Japan

[3] Japanese Fdn Canc Res, Inst Canc, Tokyo 1358550, Japan

[4] Kanagawa Dent Coll, Yokosuka, Kanagawa 2388580, Japan

[5] Osaka Univ, Grad Sch Frontier Biosci, Suita, Osaka 5650871, Japan

来源：

NATURE CELL BIOLOGY | 2010年 / 12卷 / 07期

基金：

日本学术振兴会;

关键词：

HP1; PROTEINS; PERICENTRIC HETEROCHROMATIN; KINETOCHORE PROTEIN; OUTER KINETOCHORE; HUMAN-CELLS; COMPLEX; METHYLATION; DOMAIN; GENE; CENTROMERE;

D O I：

10.1038/ncb2075

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Heterochromatin protein 1 (HP1) has an essential role in heterochromatin formation and mitotic progression through its interaction with various proteins. We have identified a unique HP1 alpha-binding protein, POGZ (pogo transposable element-derived protein with zinc finger domain), using an advanced proteomics approach. Proteins generally interact with HP1 through a PxVxL (where x is any amino-acid residue) motif; however, POGZ was found to bind to HP1 alpha through a zinc-finger-like motif. Binding by POGZ, mediated through its zinc-finger-like motif, competed with PxVxL proteins and destabilized the HP1 alpha-chromatin interaction. Depletion experiments confirmed that the POGZ HP1-binding domain is essential for normal mitotic progression and dissociation of HP1 alpha from mitotic chromosome arms. Furthermore, POGZ is required for the correct activation and dissociation of Aurora B kinase from chromosome arms during M phase. These results reveal POGZ as an essential protein that links HP1 alpha dissociation with Aurora B kinase activation during mitosis.

引用

页码：719 / U212

页数：35

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