RIP5 is a RIP-homologous inducer of cell death.
Members of the RIP serine/threonine kinase family are involved in activation of NF-kappaB, JNK, and p38, and induction of apoptosis. Here we report the identification of a novel RIP-homologous protein designated as RIP5. The C-terminus of RIP5 contains a kinase domain, which is mostly homologous with the kinase domain of RIP. RIP5 also contains a large unconserved N-terminal domain. Overexpression of RIP5 induces cell death with characteristic apoptotic morphology. Overexpression of RIP5 also induces DNA fragmentation and this is blocked by the caspase inhibitor crmA. However, RIP5-induced apoptotic morphology is not blocked by crmA. These findings suggest that RIP5 may induce both caspase-dependent apoptosis and caspase-independent cell death.
Zha
Jikun
J
Department of Cell Biology and Genetics, College of Life Sciences, Peking University, Beijing 100871, China.
Zhou
Qianhe
Q
Xu
Liang-Guo
LG
Chen
Danying
D
Li
Lixia
L
Zhai
Zhonghe
Z
Shu
Hong-Bing
HB
D000595:Amino Acid Sequence; D017209:Apoptosis / Q000502:physiology*; D020169:Caspases / Q000378:metabolism; D003001:Cloning, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D016296:Mutagenesis; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D053422:Receptor-Interacting Protein Serine-Threonine Kinases; D017386:Sequence Homology, Amino Acid
D017346:Protein Serine-Threonine Kinases; D053422:Receptor-Interacting Protein Serine-Threonine Kinases; C487805:DSTYK protein, human; D020169:Caspases