The HECTD3 E3 ubiquitin ligase facilitates cancer cell survival by promoting K63-linked polyubiquitination of caspase-8

被引：51
|
作者：
Li, Y. [1 ,2 ,3 ,4 ]
Kong, Y. [1 ,2 ]
Zhou, Z. [1 ,2 ]
Chen, H. [5 ]
Wang, Z. [1 ,2 ]
Hsieh, Y-C [6 ]
Zhao, D. [6 ]
Zhi, X. [6 ]
Huang, J. [7 ]
Zhang, J. [5 ]
Li, H. [5 ,8 ]
Chen, C. [1 ,2 ]
机构：
[1] Chinese Acad Sci, Key Lab Anim Models & Human Dis Mech, Kunming 650223, Yunnan, Peoples R China
[2] Kunming Inst Zool, Kunming 650223, Yunnan, Peoples R China
[3] Chinese Acad Med Sci, Inst Canc, State Key Lab Mol Oncol, Beijing 100021, Peoples R China
[4] Peking Union Med Coll, Beijing 100021, Peoples R China
[5] New York State Dept Hlth, Wadsworth Ctr, Albany, NY 12208 USA
[6] Albany Med Coll, Ctr Cell Biol & Canc Res, Albany, NY 12208 USA
[7] Med Coll Wisconsin, Dept Pathol, Milwaukee, WI 53226 USA
[8] SUNY Albany, Dept Biomed Sci, Sch Publ Hlth, Albany, NY 12201 USA
来源：
CELL DEATH & DISEASE | 2013年 / 4卷
关键词：
ubiquitination; apoptosis; breast cancer; HECTD3; caspase-8; EXTRINSIC APOPTOSIS; STRUCTURAL BASIS; PROTEIN LIGASE; SYNTAXIN; 8; ACTIVATION; DOMAIN; INHIBITION; RECEPTOR; DEGRADATION; COMPLEX;
D O I：
10.1038/cddis.2013.464
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
Apoptosis resistance is a hurdle for cancer treatment. HECTD3, a new E3 ubiquitin ligase, interacts with caspase-8 death effector domains and ubiquitinates caspase-8 with K63-linked polyubiquitin chains that do not target caspase-8 for degradation but decrease the caspase-8 activation. HECTD3 depletion can sensitize cancer cells to extrinsic apoptotic stimuli. In addition, HECTD3 inhibits TNF-related apoptosis-inducing ligand (TRAIL)-induced caspase-8 cleavage in an E3 ligase activity-dependent manner. Mutation of the caspase-8 ubiquitination site at K215 abolishes the HECTD3 protection from TRAIL-induced cleavage. Finally, HECTD3 is frequently overexpressed in breast carcinomas. These findings suggest that caspase-8 ubiquitination by HECTD3 confers cancer cell survival.
引用
收藏
页码：e935 / e935
页数：11
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