凋亡抑制蛋白cIAP2作为一种泛素蛋白连接酶发挥作用，并促进半胱天冬酶3和7在体外的单泛素化。
The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7.
作者信息
Huang H k, Joazeiro C A, Bonfoco E, Kamada S, Leverson J D, Hunter T
机构信息
Molecular Biology and Virology Laboratory, The Salk Institute for Biological Studies and the Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA.
出版信息
J Biol Chem. 2000 Sep 1;275(35):26661-4. doi: 10.1074/jbc.C000199200.
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.
凋亡抑制蛋白cIAP2在其C末端含有一个假定的环状结构域。通过体外泛素化实验，我们发现cIAP2单独的环状结构域具有内在的泛素连接酶活性，并能促进不依赖底物的泛素化。它还能促进半胱天冬酶3和7的泛素化，但不能促进半胱天冬酶-1的泛素化。c-Cbl和Apc11的环状结构域不能促进半胱天冬酶-7的泛素化，这表明cIAP2自身的环状结构域参与了底物识别。
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