Modulating molecular chaperone Hsp90 functions through reversible acetylation

被引：110
作者：
Aoyagi, S [1 ]
Archer, TK [1 ]
机构：
[1] NIEHS, Chromatin & Gene Express Sect, Mol Carcinogenesis Lab, NIH, Res Triangle Pk, NC 27709 USA
来源：
TRENDS IN CELL BIOLOGY | 2005年 / 15卷 / 11期
关键词：
D O I：
10.1016/j.tcb.2005.09.003
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
The molecular chaperone protein Hsp90 is a key regulator of approximately 100 'client' proteins crucial for numerous cell signaling processes. Consequently, understanding the molecular underpinnings that regulate Hsp90 activity is an important biological endeavor. Exciting new results now suggest that, at least for nuclear receptor activity, Hsp90 function is directly regulated by histone deacetylase 6 (HDAC6). These observations have consequences for various biological processes and potentially important implications for the development of cancer therapeutics.
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收藏
页码：565 / 567
页数：3
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