期刊
ACTA BIOCHIMICA ET BIOPHYSICA SINICA
卷 37, 期 7, 页码 501-505出版社
OXFORD UNIV PRESS
DOI: 10.1111/j.1745-7270.2005.00069.x
关键词
molecular chaperone; phosphorylation; Hsp90; extracellular signal-regulated protein kinase (ERK); Raf; tau
Extracellular signal-regulated protein kinase (ERK) has been implicated in the pathogenesis of several nerve system diseases. As more and more kinases have been discovered to be the client proteins of the molecular chaperone Hsp90, the use of Hsp90 inhibitors to reduce abnormal kinase activity is a new treatment strategy for nerve system diseases. This study investigated the regulation of the ERK pathway by Hsp90. We showed that Hsp90 inhibitors reduce ERK phosphorylation without affecting the total ERK protein level. Further investigation showed that Raf, the upstream kinase in the Ras-Raf-MEK-ERK pathway, forms a complex with Hsp90 and Hsp70. Treating cells with Hsp90 inhibitors facilitates Raf degradation, thereby down-regulating the activity of ERK.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据