The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligaseand promotes in vitro monoubiquitination of caspases 3 and 7

Citation
Hk. Huang et al., The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligaseand promotes in vitro monoubiquitination of caspases 3 and 7, J BIOL CHEM, 275(35), 2000, pp. 26661-26664
Citations number
37
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
00219258 → ACNP
Volume
275
Issue
35
Year of publication
2000
Pages
26661 - 26664
Database
ISI
SICI code
0021-9258(20000901)275:35<26661:TIOACF>2.0.ZU;2-Q
Abstract
The inhibitor of apoptosis, cIAP2, contains a putative Ring finger motif at the C terminus. Using in vitro ubiquitination assays, we found that the Ri ng finger of cIAP2 alone possesses intrinsic ubiquitin ligase activity and promotes substrate-independent ubiquitination. It also promotes ubiquitinat ion of caspases 3 and 7 but not caspase-1. The Ring fingers of c-Cbl and Ap c11 failed to promote caspase-7 ubiquitination, suggesting that the Ring fi nger of cIAP2 itself is involved in substrate recognition.