Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 303, Issue 1, Pages 69-73Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0006-291X(03)00309-7
Keywords
ASC; Nod protein family; caspase-recruitment domain; NF-kappa B; Ipaf; caspase-8; apoptosis
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Funding
- NCI NIH HHS [CA-64556] Funding Source: Medline
- NICHD NIH HHS [T32-HD07505] Funding Source: Medline
- NIDDK NIH HHS [DK-61707] Funding Source: Medline
- NIGMS NIH HHS [GM-60421] Funding Source: Medline
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ASC is a pro-apoptotic protein containing a pyrin domain (PD) and a caspase-recruitment domain (CARD). A previous study suggests that ASC interacts with Ipaf, a member of the Apaf-l/Nodl protein family. However, the functional relevance of the interaction has not been determined. Here, we report that co-expression of ASC with Ipaf or oligomerization of ASC induces both apoptosis and NF-kappaB activation. Apoptosis induced through ASC was inhibited by a mutant form of Caspase-8 but not by that of Caspase-1. The PD of ASC physically interacted with Caspase-8 as well as with pyrin, the familial Mediterranean fever gene product. Caspase-8 deficiency rescued mouse fibroblasts from apoptosis induced by ASC oligomerization. Pyrin disrupted the interaction between ASC and Caspase-8, and inhibited both apoptosis and NF-kappaB activation induced by ASC. These findings suggest that ASC is a mediator of NF-kappaB activation and Caspase-8-dependent apoptosis in an Ipaf signaling pathway. (C) 2003 Elsevier Science (USA). All rights reserved.
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