RIP3, a Novel Apoptosis-inducing Kinase
| Autor: | Daryl T. Baldwin, Xiaoqing Sun, Tony A. Navas, Timothy A. Stewart, Vishva M. Dixit, James Lee |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
endocrine system
Molecular Sequence Data Apoptosis Plasma protein binding Protein Serine-Threonine Kinases Biology Biochemistry Receptors Tumor Necrosis Factor Antigens CD Receptor-Interacting Protein Serine-Threonine Kinase 2 Humans Amino Acid Sequence Cloning Molecular Molecular Biology Death domain Sequence Homology Amino Acid Kinase C-terminus NF-kappa B Proteins Cell Biology Molecular biology Recombinant Proteins Protein kinase domain Receptors Tumor Necrosis Factor Type I Caspases Receptor-Interacting Protein Serine-Threonine Kinases Tumor necrosis factor alpha Signal transduction Protein Kinases Sequence Analysis Protein Binding Signal Transduction |
| Zdroj: | Journal of Biological Chemistry. 274:16871-16875 |
| ISSN: | 0021-9258 |
| Popis: | RIP3 is a novel gene product containing a N-terminal kinase domain that shares extensive homology with the corresponding domain in RIP (receptor-interacting protein) and RIP2. Unlike RIP, which has a C-terminal death domain, and RIP2, which has a C-terminal caspase activation and recruitment domain, RIP3 has a unique C terminus. RIP3 binds RIP through its unique C-terminal segment and by virtue of this interaction is recruited to the tumor necrosis factor (TNF) receptor-1 signaling complex. Previous studies have shown that RIP mediates TNF-induced activation of the anti-apoptotic NF-kappaB pathway. RIP3, however, attenuates both RIP and TNF receptor-1-induced NF-kappaB activation. Overexpression studies revealed RIP3 to be a potent inducer of apoptosis, capable of selectively binding to large prodomain initiator caspases. |
| Databáze: | OpenAIRE |
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