中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Cyclodepsipeptide toxin promotes the degradation of Hsp90 client proteins through chaperone-mediated autophagy

文献类型:期刊论文

作者Shen, Shensi ; Zhang PT(张澎涛) ; Lovchik, Martin A. ; Li, Ying ; Tang, Liuya ; Chen, Zhimin ; Zeng, Rong ; Ma DW(马大为) ; Yuan JY(袁钧英) ; Yu Q(俞强)
刊名J. Cell Biol.
出版日期2009
卷号185期号:4页码:629-639
ISSN号0021-9525
其他题名环酯肽毒素通过分子伴侣介导的自吞噬作用促进Hsp90事件蛋白降解
通讯作者马大为 ; 袁钧英 ; 俞强
英文摘要Promoting the degradation of Hsp90 client proteins by inhibiting Hsp90, an important protein chaperone, has been shown to be a promising new anticancer strategy. In this study, we show that an oxazoline analogue of apratoxin A (oz-apraA), a cyclodepsipeptide isolated from a marine cyanobacterium, promotes the degradation of Hsp90 clients through chaperone-mediated autophagy (CMA). We identify a KFERQ-like motif as a conserved pentapeptide sequence in the kinase domain of epidermal growth factor receptor (EGFR) necessary for recognition as a CMA substrate. Mutation of this motif prevents EGFR degradation by CMA and promotes the degradation of EGFR through the proteasomal pathway in oz-apraA-treated cells. Oz-apraA binds to Hsc70/Hsp70. We propose that apratoxin A inhibits Hsp90 function by stabilizing the interaction of Hsp90 client proteins with Hsc70/Hsp70 and thus prevents their interactions with Hsp90. Our study provides the first examples for the ability of CMA to mediate degradation of membrane receptors and cross talks of CMA and proteasomal degradation mechanisms.
学科主题生命有机化学
收录类别SCI
原文出处http://dx.doi.org/10.1083/jcb.200810183
语种英语
WOS记录号WOS:000266279900009
公开日期2013-02-19
源URL[http://202.127.28.38/handle/331003/15611]  
专题上海有机化学研究所_生命有机化学国家重点实验室
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Shen, Shensi,Zhang PT,Lovchik, Martin A.,et al. Cyclodepsipeptide toxin promotes the degradation of Hsp90 client proteins through chaperone-mediated autophagy[J]. J. Cell Biol.,2009,185(4):629-639.
APA Shen, Shensi.,张澎涛.,Lovchik, Martin A..,Li, Ying.,Tang, Liuya.,...&俞强.(2009).Cyclodepsipeptide toxin promotes the degradation of Hsp90 client proteins through chaperone-mediated autophagy.J. Cell Biol.,185(4),629-639.
MLA Shen, Shensi,et al."Cyclodepsipeptide toxin promotes the degradation of Hsp90 client proteins through chaperone-mediated autophagy".J. Cell Biol. 185.4(2009):629-639.

入库方式: OAI收割

来源:上海有机化学研究所

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