Title
An IAP-IAP complex inhibits apoptosis
UMMS Affiliation
Department of Cancer Biology and the Cancer Center
Publication Date
2004-06-26
Document Type
Article
Subjects
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
Disciplines
Life Sciences | Medicine and Health Sciences
Abstract
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.
DOI of Published Version
10.1074/jbc.C400236200
Source
J Biol Chem. 2004 Aug 13;279(33):34087-90. Epub 2004 Jun 24. Link to article on publisher's site
Journal/Book/Conference Title
The Journal of biological chemistry
Related Resources
PubMed ID
15218035
Repository Citation
Dohi T, Okada K, Xia F, Wilford CE, Samuel T, Welsh K, Marusawa H, Zou H, Armstrong R, Matsuzawa S, Salvesen GS, Reed JC, Altieri DC. (2004). An IAP-IAP complex inhibits apoptosis. Open Access Publications by UMMS Authors. https://doi.org/10.1074/jbc.C400236200. Retrieved from https://escholarship.umassmed.edu/oapubs/705