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http://purl.uniprot.org/citations/17905723http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17905723http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17905723http://www.w3.org/2000/01/rdf-schema#comment"STIM1 and CRACM1 (or Orai1) are essential molecular components mediating store-operated Ca2+ entry (SOCE) and Ca2+ release-activated Ca2+ (CRAC) currents. Although STIM1 acts as a luminal Ca2+ sensor in the endoplasmic reticulum (ER), the function of STIM2 remains unclear. Here we reveal that STIM2 has two distinct modes of activating CRAC channels: a store-operated mode that is activated through depletion of ER Ca2+ stores by inositol 1,4,5-trisphosphate (InsP3) and store-independent activation that is mediated by cell dialysis during whole-cell perfusion. Both modes are regulated by calmodulin (CaM). The store-operated mode is transient in intact cells, possibly reflecting recruitment of CaM, whereas loss of CaM in perfused cells accounts for the persistence of the store-independent mode. The inhibition by CaM can be reversed by 2-aminoethoxydiphenyl borate (2-APB), resulting in rapid, store-independent activation of CRAC channels. The aminoglycoside antibiotic G418 is a highly specific and potent inhibitor of STIM2-dependent CRAC channel activation. The results reveal a novel bimodal control of CRAC channels by STIM2, the store dependence and CaM regulation, which indicates that the STIM2/CRACM1 complex may be under the control of both luminal and cytoplasmic Ca2+ levels."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.org/dc/terms/identifier"doi:10.1096/fj.07-9449com"xsd:string
http://purl.uniprot.org/citations/17905723http://purl.org/dc/terms/identifier"doi:10.1096/fj.07-9449com"xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Beck A."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Beck A."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Parvez S."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Parvez S."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Fleig A."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Fleig A."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Gill D.L."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Gill D.L."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Lis A."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Lis A."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Monteilh-Zoller M."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Monteilh-Zoller M."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Peinelt C."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Peinelt C."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Penner R."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Penner R."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Soboloff J."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/author"Soboloff J."xsd:string
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/17905723http://purl.uniprot.org/core/date"2008"xsd:gYear