Journal
EMBO JOURNAL
Volume 22, Issue 11, Pages 2729-2740Publisher
OXFORD UNIV PRESS
DOI: 10.1093/emboj/cdg263
Keywords
apoptosis; caspase; hepatitis B virus; hepatitis B X-interacting protein; survivin
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Funding
- NIA NIH HHS [AG15393-05, R01 AG015393] Funding Source: Medline
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Survivin is an anti-apoptotic protein that is overexpressed in most human cancers. We show that survivin forms complexes with a cellular protein, hepatitis B X-interacting protein (HBXIP), which was originally recognized for its association with the X protein of hepatitis B virus (HBX). Survivin-HBXIP complexes, but neither survivin nor HBXIP individually, bind pro-caspase-9, preventing its recruitment to Apaf1, and thereby selectively suppressing apoptosis initiated via the mitochondria/cytochrome c pathway. Viral HBX protein also interacts with the survivin- HBXIP complex and suppresses caspase activation in a survivin-dependent manner. Thus, HBXIP functions as a cofactor for survivin, and serves as a link between the cellular apoptosis machinery and a viral pathogen involved in hepatocellular carcinogenesis.
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