An IAP-IAP complex inhibits apoptosis
Department of Cancer Biology and the Cancer Center
Animals; *Apoptosis; Baculoviridae; Caspase 9; Caspases; Cell Death; Cell Line; Cell Line, Tumor; Cysteine Endopeptidases; Dose-Response Relationship, Drug; Fibroblasts; Gene Expression Regulation; Glutathione Transferase; Humans; Immunoblotting; Mice; Mice, Transgenic; Microtubule-Associated Proteins; Multienzyme Complexes; Neoplasm Proteins; Precipitin Tests; Proteasome Endopeptidase Complex; Protein Binding; Proteins; Recombinant Proteins; Time Factors; Transfection; Transgenes; Ubiquitin; X-Linked Inhibitor of Apoptosis Protein
Life Sciences | Medicine and Health Sciences
Regulators of apoptosis are thought to work in concert, but the molecular interactions of this process are not understood. Here, we show that in response to cell death stimulation, survivin, a member of the inhibitor of apoptosis (IAP) gene family, associates with another IAP protein, XIAP, via conserved baculovirus IAP repeats. Formation of a survivin-XIAP complex promotes increased XIAP stability against ubiquitination/proteasomal destruction and synergistic inhibition of apoptosis, which is abolished in XIAP(-/-) cells. Therefore, orchestration of an IAP-IAP complex regulates apoptosis.
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Citation: J Biol Chem. 2004 Aug 13;279(33):34087-90. Epub 2004 Jun 24. Link to article on publisher's site
DOI of Published Version
The Journal of biological chemistry
Dohi, Takehiko; Okada, Kazuya; Xia, Fang; Wilford, Casey E.; Samuel, Temesgen; Welsh, Kate; Marusawa, Hiroyouki; Zou, Hua; Armstrong, Robert; Matsuzawa, Shu-ichi; Salvesen, Guy S.; Reed, John C.; and Altieri, Dario C., "An IAP-IAP complex inhibits apoptosis" (2004). Open Access Articles. 705.