Destabilizing influences in apoptosis: sowing the seeds of IAP destruction.
Inhibitor of apoptosis proteins (IAPs) can block apoptosis through interactions with members of the caspase family of cysteine proteases. Recent developments suggest that ubiquitin-proteasome mediated destruction of the Drosophila IAP, DIAP1, is a key event during the initiation of programmed cell death in the fly.
Martin
Seamus J
SJ
Molecular Cell Biology Laboratory, Department of Genetics, Trinity College, Dublin 2, Ireland. martinsj@tcd.ie
D000818:Animals; D017209:Apoptosis; D020169:Caspases / Q000378:metabolism; D003574:Cytochrome c Group / Q000378:metabolism; D004330:Drosophila / Q000166:cytology* / Q000201:enzymology / Q000378:metabolism; D029721:Drosophila Proteins / Q000378:metabolism*; D051034:Inhibitor of Apoptosis Proteins; D009479:Neuropeptides / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D025801:Ubiquitin / Q000378:metabolism
D003574:Cytochrome c Group; C111891:DIAP1 protein, Drosophila; D029721:Drosophila Proteins; C108880:HID protein, Drosophila; D051034:Inhibitor of Apoptosis Proteins; D009479:Neuropeptides; D010455:Peptides; D025801:Ubiquitin; C108881:grim protein, Drosophila; C086973:rpr protein, Drosophila; D020169:Caspases