Regulators of IAP function: coming to grips with the grim reaper |
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Authors: | Bergmann Andreas Yang Amy Yi-Pei Srivastava Mayank |
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Affiliation: | The University of Texas MD Anderson Cancer Center, Department of Biochemistry & Molecular Biology, Unit 117, 1515 Holcombe Blvd, Houston, TX 77030, USA. andreas@bergman.net |
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Abstract: | Inhibitor of apoptosis proteins (IAPs) are a conserved class of proteins that control apoptosis in both vertebrates and invertebrates. They exert their anti-apoptotic function through inhibition of caspases, the principal executioners of apoptotic cell death. Recent advances in vertebrates and Drosophila have demonstrated that IAPs use ubiquitin conjugation to control the stability, and thus the activity, of select target proteins. The Drosophila IAP1 gene is an instructive example: it employs at least two distinct ubiquitin-dependent mechanisms of protein destruction. The apoptosis-inducing genes grim, reaper and hid modulate these mechanisms, and determine the outcome. |
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Keywords: | Abbreviations: BIR, baculovirus IAP repeat DIAP1, Drosophila inhibitor of apoptosis protein 1 GMR, glass-multimer reporter IAP, inhibitor of apoptosis protein RHG, reaper, hid and grim RING, really interesting new gene UBC, ubiquitin conjugating XIAP, X-linked IAP |
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