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http://purl.uniprot.org/citations/14685260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14685260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14685260http://www.w3.org/2000/01/rdf-schema#comment"Inositol 1,4,5-trisphosphate receptors (InsP(3)Rs) were recently demonstrated to be activated independently of InsP(3) by a family of calmodulin (CaM)-like neuronal Ca(2+)-binding proteins (CaBPs). We investigated the interaction of both naturally occurring long and short CaBP1 isoforms with InsP(3)Rs, and their functional effects on InsP(3)R-evoked Ca(2+) signals. Using several experimental paradigms, including transient expression in COS cells, acute injection of recombinant protein into Xenopus oocytes and (45)Ca(2+) flux from permeabilised COS cells, we demonstrated that CaBPs decrease the sensitivity of InsP(3)-induced Ca(2+) release (IICR). In addition, we found a Ca(2+)-independent interaction between CaBP1 and the NH(2)-terminal 159 amino acids of the type 1 InsP(3)R. This interaction resulted in decreased InsP(3) binding to the receptor reminiscent of that observed for CaM. Unlike CaM, however, CaBPs do not inhibit ryanodine receptors, have a higher affinity for InsP(3)Rs and more potently inhibited IICR. We also show that phosphorylation of CaBP1 at a casein kinase 2 consensus site regulates its inhibition of IICR. Our data suggest that CaBPs are endogenous regulators of InsP(3)Rs tuning the sensitivity of cells to InsP(3)."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7600037"xsd:string
http://purl.uniprot.org/citations/14685260http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7600037"xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Holmes A.B."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Holmes A.B."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Conway S.J."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Conway S.J."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Missiaen L."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Missiaen L."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Bultynck G."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Bultynck G."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"De Smedt H."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"De Smedt H."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Parys J.B."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Parys J.B."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Berridge M.J."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Berridge M.J."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Bootman M.D."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Bootman M.D."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Holmes A.M."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Holmes A.M."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Kasri N.N."xsd:string
http://purl.uniprot.org/citations/14685260http://purl.uniprot.org/core/author"Kasri N.N."xsd:string