XIAP as a ubiquitin ligase in cellular signaling
| Autor: | Stefanie Galbán, Colin S. Duckett |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Cell signaling
biology Ubiquitin-Protein Ligases NF-kappa B Apoptosis X-Linked Inhibitor of Apoptosis Protein Cell Biology Inhibitor of apoptosis Article Inhibitor of Apoptosis Proteins XIAP Cell biology Ubiquitin ligase Ubiquitin biology.protein Cancer research XIAP Deficiency Signal transduction Molecular Biology Caspase Signal Transduction |
| Zdroj: | Cell Death & Differentiation. 17:54-60 |
| ISSN: | 1476-5403 1350-9047 |
| DOI: | 10.1038/cdd.2009.81 |
| Popis: | The ability of the vertebrate X-linked inhibitor of apoptosis (XIAP) protein to directly suppress apoptotic cell death pathways has been the subject of much research. Studies of this broadly expressed protein have largely focused on the unique interactions between XIAP and caspases – proteases that conduct and participate in the ordered disassembly of the cell during apoptosis. However, relatively less attention has been given to the RING domain of XIAP, which functions as an E3 ligase to catalyze the ubiquitination of substrate proteins. Here we discuss the evidence implicating the RING domain of XIAP in the ubiquitin-mediated regulation of three somewhat arbitrarily divided categories of substrate: XIAP itself, XIAP-interacting proteins involved in apoptosis, and other targets whose physiologic roles likely extend beyond cell death. Collectively, these multiple activities of XIAP demonstrate that this enigmatic protein participates in a range of cellular activities beyond apoptotic suppression. |
| Databáze: | OpenAIRE |
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