The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7.
The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7.
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DOI：
10.1074/jbc.c000199200
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发表时间：
2000-09
期刊：
影响因子：
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通讯作者：
Han-kuei Huang;C. Joazeiro;Emanuela Bonfoco;S. Kamada;J. Leverson;T. Hunter
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文献类型：
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作者：
Han-kuei Huang;C. Joazeiro;Emanuela Bonfoco;S. Kamada;J. Leverson;T. Hunter
细胞凋亡抑制因子cIAP2在C末端含有一个可能的Ring Finger基序。利用体外泛素化实验，我们发现cIAP2的Ring Finger单独具有固有的泛素连接酶活性，并促进底物非依赖性泛素化。它还促进caspase 3和7的泛素化，但不促进caspase-1。C-Cb1和Apc11的Ring Finger未能促进caspase-7泛素化，提示CIAP2的Ring Finger本身参与底物识别。
The inhibitor of apoptosis, cIAP2, contains a putative Ring finger motif at the C terminus. Using in vitro ubiquitination assays, we found that the Ring finger of cIAP2 alone possesses intrinsic ubiquitin ligase activity and promotes substrate-independent ubiquitination. It also promotes ubiquitination of caspases 3 and 7 but not caspase-1. The Ring fingers of c-Cbl and Apc11 failed to promote caspase-7 ubiquitination, suggesting that the Ring finger of cIAP2 itself is involved in substrate recognition.