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Cyclodepsipeptide toxin promotes the degradation of Hsp90 client proteins through chaperone-mediated autophagy

文献类型：期刊论文

作者Shen, Shensi2; Zhang, Pengtao3; Lovchik, Martin A.3; Li, Ying3; Tang, Liuya4; Chen, Zhimin2; Zeng, Rong4; Ma, Dawei3; Yuan, Junying1; Yu, Qiang2
刊名JOURNAL OF CELL BIOLOGY
出版日期2009-05-18
卷号185期号:4页码:629-639
ISSN号0021-9525
DOI10.1083/jcb.200810183
文献子类Article
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.
WOS关键词HEAT-SHOCK RESPONSE ; MOLECULAR CHAPERONE ; GENE-EXPRESSION ; APRATOXIN-A ; OXIDATIVE STRESS ; CANCER ; COMPLEX ; RECOGNIZES ; MECHANISMS ; COMPONENTS
资助项目China National Science and Technology[2004CB518903] ; China National Natural Science Foundation[30672481] ; China National Natural Science Foundation[30771097] ; China National Science Foundation[20632050] ; China National Science Foundation[20621062] ; U.S. National Institute on Aging[00000000] ; National Basic Research Program of China[2006CB910700] ; PROTEOMAGE Project[FP6] ; European Union[00000000]
WOS研究方向Cell Biology
语种英语
WOS记录号WOS:000266279900009
出版者ROCKEFELLER UNIV PRESS
源URL[http://119.78.100.183/handle/2S10ELR8/279235]  
专题药理学第一研究室
通讯作者Ma, Dawei
作者单位1.Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
2.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China;
3.Chinese Acad Sci, Shanghai Inst Organ Chem, State Key Lab Bioorgan & Nat Prod Chem, Shanghai 201203, Peoples R China;
4.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Key Lab Syst Biol, Shanghai 201203, Peoples R China;
推荐引用方式
GB/T 7714		 Shen, Shensi,Zhang, Pengtao,Lovchik, Martin A.,et al. Cyclodepsipeptide toxin promotes the degradation of Hsp90 client proteins through chaperone-mediated autophagy[J]. JOURNAL OF CELL BIOLOGY,2009,185(4):629-639.
APA Shen, Shensi.,Zhang, Pengtao.,Lovchik, Martin A..,Li, Ying.,Tang, Liuya.,...&Yu, Qiang.(2009).Cyclodepsipeptide toxin promotes the degradation of Hsp90 client proteins through chaperone-mediated autophagy.JOURNAL OF CELL BIOLOGY,185(4),629-639.
MLA Shen, Shensi,et al."Cyclodepsipeptide toxin promotes the degradation of Hsp90 client proteins through chaperone-mediated autophagy".JOURNAL OF CELL BIOLOGY 185.4(2009):629-639.

入库方式： OAI收割

来源：上海药物研究所

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