http://purl.uniprot.org/citations/15980432 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15980432 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15980432 | http://www.w3.org/2000/01/rdf-schema#comment | "Ca(2+)-binding protein-1 (CaBP1) and calmodulin (CaM) are highly related Ca(2+)-binding proteins that directly interact with, and yet differentially regulate, voltage-gated Ca(2+) channels. Whereas CaM enhances inactivation of Ca(2+) currents through Ca(v)1.2 (L-type) Ca(2+) channels, CaBP1 completely prevents this process. How CaBP1 and CaM mediate such opposing effects on Ca(v)1.2 inactivation is unknown. Here, we identified molecular determinants in the alpha(1)-subunit of Ca(v)1.2 (alpha(1)1.2) that distinguish the effects of CaBP1 and CaM on inactivation. Although both proteins bind to a well characterized IQ-domain in the cytoplasmic C-terminal domain of alpha(1)1.2, mutations of the IQ-domain that significantly weakened CaM and CaBP1 binding abolished the functional effects of CaM, but not CaBP1. Pulldown binding assays revealed Ca(2+)-independent binding of CaBP1 to the N-terminal domain (NT) of alpha(1)1.2, which was in contrast to Ca(2+)-dependent binding of CaM to this region. Deletion of the NT abolished the effects of CaBP1 in prolonging Ca(v)1.2 Ca(2+) currents, but spared Ca(2+)-dependent inactivation due to CaM. We conclude that the NT and IQ-domains of alpha(1)1.2 mediate functionally distinct interactions with CaBP1 and CaM that promote conformational alterations that either stabilize or inhibit inactivation of Ca(v)1.2."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m504167200"xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m504167200"xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/author | "Lee A."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/author | "Lee A."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/author | "Zhou H."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/author | "Zhou H."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/author | "Yu K."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/author | "Yu K."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/author | "McCoy K.L."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/author | "McCoy K.L."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/pages | "29612-29619"xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/pages | "29612-29619"xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/title | "Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by calmodulin and Ca2+-binding protein-1."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/title | "Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by calmodulin and Ca2+-binding protein-1."xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/volume | "280"xsd:string |
http://purl.uniprot.org/citations/15980432 | http://purl.uniprot.org/core/volume | "280"xsd:string |
http://purl.uniprot.org/citations/15980432 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15980432 |
http://purl.uniprot.org/citations/15980432 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15980432 |