西亚试剂：The HECTD3 E3 ubiquitin ligase facilitates cancer cell surv

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

Y Li1，2，7， Y Kong1，7， Z Zhou1， H Chen3， Z Wang1， Y-C Hsieh4， D Zhao4， X Zhi4， J Huang5， J Zhang3， H Li3，6 and C Chen1

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.

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