PTEN Interacts with Histone H1 and Controls Chromatin Condensation

被引：102

作者：

Chen, Zhu Hong ^{[1
,2
]}

Zhu, Minglu ^{[1
,2
]}

Yang, Jingyi ^{[1
]}

Liang, Hui ^{[1
]}

He, Jinxue ^{[2
]}

He, Shiming ^{[1
]}

Wang, Pan ^{[1
]}

Kang, Xi ^{[1
,2
]}

McNutt, Michael A. ^{[1
]}

Yin, Yuxin ^{[1
,2
]}

Shen, Wen H. ^{[2
]}

机构：

[1] Peking Univ, Beijing Key Lab Tumor Syst Biol, Peking Tsinghua Ctr Life Sci,Hlth Sci Ctr, Inst Syst Biomed,Dept Pathol,Sch Basic Med Sci, Beijing 100191, Peoples R China

[2] Cornell Univ, Weill Med Coll, Dept Radiat Oncol, New York, NY 10065 USA

来源：

CELL REPORTS | 2014年 / 8卷 / 06期

基金：

中国国家自然科学基金; 北京市自然科学基金;

关键词：

H4-K16; ACETYLATION; NUCLEAR PTEN; CANCER-CELLS; GENE; COMPLEX; TRANSCRIPTION; MAINTENANCE; MOF; ASSOCIATION; ACTIVATION;

D O I：

10.1016/j.celrep.2014.08.008

中图分类号：

Q2 [细胞生物学];

学科分类号：

071013 [干细胞生物学];

摘要：

Chromatin organization and dynamics are integral to global gene transcription. Histone modification influences chromatin status and gene expression. PTEN plays multiple roles in tumor suppression, development, and metabolism. Here, we report on the interplay of PTEN, histone H1, and chromatin. We show that loss of PTEN leads to dissociation of histone H1 from chromatin and decondensation of chromatin. PTEN deletion also results in elevation of histone H4 acetylation at lysine 16, an epigenetic marker for chromatin activation. We found that PTEN and histone H1 physically interact through their C-terminal domains. Disruption of the PTEN C terminus promotes the chromatin association of MOF acetyltransferase and induces H4K16 acetylation. Hyperacetylation of H4K16 impairs the association of PTEN with histone H1, which constitutes regulatory feedback that may reduce chromatin stability. Our results demonstrate that PTEN controls chromatin condensation, thus influencing gene expression. We propose that PTEN regulates global gene transcription profiling through histones and chromatin remodeling.

引用

页码：2003 / 2014

页数：12

共 55 条

[1]

Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila [J].