Title

An IAP-IAP complex inhibits apoptosis

UMMS Affiliation

Department of Cancer Biology and the Cancer Center

Publication Date

6-26-2004

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.

Rights and Permissions

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

10.1074/jbc.C400236200

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

The Journal of biological chemistry

PubMed ID

15218035