Modulating molecular chaperone Hsp90 functions through reversible acetylation
Modulating molecular chaperone Hsp90 functions through reversible acetylation
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DOI：
10.1016/j.tcb.2005.09.003
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发表时间：
2005-11-01
影响因子：
19
通讯作者：
Archer, TK
中科院分区：
文献类型：
--
作者：
Aoyagi, S;Archer, TK
分子伴侣蛋白Hsp90是大约100个“客户”蛋白的关键调节器，对许多细胞信号传导过程至关重要。因此，了解调节Hsp90活性的分子基础是一项重要的生物学奋进。令人兴奋的新结果表明，至少对于核受体活性，Hsp90的功能直接受组蛋白去乙酰化酶6（HDAC6）调节。这些观察结果对各种生物学过程具有影响，并对癌症治疗的发展具有潜在的重要意义。
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.