Authors
Dohi, TakehikoOkada, 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.
Altieri, Dario C.
UMass Chan Affiliations
Department of Cancer Biology and the Cancer CenterDocument Type
Journal ArticlePublication Date
2004-06-26Keywords
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
Metadata
Show full item recordAbstract
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.Source
J Biol Chem. 2004 Aug 13;279(33):34087-90. Epub 2004 Jun 24. Link to article on publisher's siteDOI
10.1074/jbc.C400236200Permanent Link to this Item
http://hdl.handle.net/20.500.14038/42348PubMed ID
15218035Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1074/jbc.C400236200
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