Regulators of IAP function: coming to grips with the grim reaper

Regulators of IAP function: coming to grips with the grim reaper 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in Cell Biology Elsevier

Regulators of IAP function: coming to grips with the grim reaper

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Publisher
Elsevier
Copyright
Copyright © 2003 Elsevier Ltd
ISSN
0955-0674
D.O.I.
10.1016/j.ceb.2003.10.002
Publisher site
See Article on Publisher Site

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.

Journal

Current Opinion in Cell BiologyElsevier

Published: Dec 1, 2003

References

  • The damage-responsive Drosophila gene sickle encodes a novel IAP binding protein similar to but distinct from reaper , grim , and hid
    Christich, A.; Kauppila, S.; Chen, P.; Sogame, N.; Ho, S.I.; Abrams, J.M.
  • Sickle , a novel Drosophila death gene in the reaper / hid / grim region, encodes an IAP-inhibitory protein
    Srinivasula, S.M.; Datta, P.; Kobayashi, M.; Wu, J.W.; Fujioka, M.; Hegde, R.; Zhang, Z.; Mukattash, R.; Fernandes-Alnemri, T.; Shi, Y.
  • Drosophila sickle is a novel grim - reaper cell death activator
    Wing, J.P.; Karres, J.S.; Ogdahl, J.L.; Zhou, L.; Schwartz, L.M.; Nambu, J.R.
  • Jafrac2 is an IAP antagonist that promotes cell death by liberating Dronc from DIAP1
    Tenev, T.; Zachariou, A.; Wilson, R.; Paul, A.; Meier, P.
  • Cell killing by Drosophila reaper
    White, K.; Tahaoglu, E.; Steller, H.
  • Induction of apoptosis by Drosophila reaper , hid and grim through inhibition of IAP function
    Goyal, L.; McCall, K.; Agapite, J.; Hartwieg, E.; Steller, H.
  • Diverse domains of THREAD/DIAP1 are required to inhibit apoptosis induced by REAPER and HID in Drosophila
    Lisi, S.; Mazzon, I.; White, K.
  • IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases
    Deveraux, Q.L.; Roy, N.; Stennicke, H.R.; Van Arsdale, T.; Zhou, Q.; Srinivasula, S.M.; Alnemri, E.S.; Salvesen, G.S.; Reed, J.C.
  • The Drosophila caspase DRONC is regulated by DIAP1
    Meier, P.; Silke, J.; Leevers, S.J.; Evan, G.I.
  • Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases
    Deveraux, Q.L.; Leo, E.; Stennicke, H.R.; Welsh, K.; Salvesen, G.S.; Reed, J.C.
  • Drosophila Bruce can potently suppress Rpr- and grim-dependent but not hid-dependent cell death
    Vernooy, S.Y.; Chow, V.; Su, J.; Verbrugghe, K.; Yang, J.; Cole, S.; Olson, M.R.; Hay, B.A.
  • Scythe: a novel reaper-binding apoptotic regulator
    Thress, K.; Henzel, W.; Shillinglaw, W.; Kornbluth, S.

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