Digital.CSIC > Biología y Biomedicina > Instituto de Biomedicina de Valencia (IBV) > (IBV) Artículos >




Open Access item Polypeptide modulators of caspase recruitment domain (CARD)-CARD-mediated protein-protein interactions

Authors:Palacios-Rodríguez, Yadira
García-Laínez, Guillermo
Sancho, Mónica
Gortat, Anna
Orzáez, Mar
Pérez-Payá, Enrique
Keywords:Apaf-1, apoptosis, apoptosome, caspase-1, caspase-9, CARD, inflammasome, inhibitors, NLRP-1, NOD, ASC, peptides, procaspase-1, procaspase-9, protein-protein
Issue Date:7-Nov-2011
Publisher:American Society for Biochemistry and Molecular Biology
Citation:Journal of Biological Chemistry 286(52):44457-66 (2011 Dec 30)
Abstract:The caspase recruitment domain (CARD) is present in a large number of proteins. Initially, the CARD was recognized as part of the caspase activation machinery. CARD-CARD interactions play a role in apoptosis and are responsible for the Apaf-1-mediated activation of procaspase-9 in the apoptosome. CARD-containing proteins mediate the inflammasome-dependent activation of proinflammatory caspase-1. More recently, new roles for CARD-containing proteins have been reported in signaling pathways associated with immune responses. The functional role of CARD-containing proteins and CARDs in coordinating apoptosis and inflammatory and immune responses is not completely understood. We have explored the putative cross-talk between apoptosis and inflammation by analyzing the modulatory activity on both the Apaf-1/procaspase-9 interaction and the inflammasome-mediated procaspase-1 activation of CARD-derived polypeptides. To this end, we analyzed the activity of individual recombinant CARDs, rationally designed CARD-derived peptides, and peptides derived from phage display.
Description:10 páginas, 7 figuras, 3 tablas. PMID:22065589[PubMed] PMCID:PMC3247988[Available on 2012/12/30]
Publisher version (URL):http://dx.doi.org/10.1074/jbc.M111.255364
E-ISSNmetadata.dc.identifier.doi = DOI:1083-351X
Appears in Collections:(IBV) Artículos

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.