| http://purl.uniprot.org/citations/16537481 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16537481 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16537481 | http://www.w3.org/2000/01/rdf-schema#comment | "Receptor-induced Ca(2+) signals are key to the function of all cells and involve release of Ca(2+) from endoplasmic reticulum (ER) stores, triggering Ca(2+) entry through plasma membrane (PM) "store-operated channels" (SOCs). The identity of SOCs and their coupling to store depletion remain molecular and mechanistic mysteries. The single transmembrane-spanning Ca(2+)-binding protein, STIM1, is necessary in this coupling process and is proposed to function as an ER Ca(2+) sensor to provide the trigger for SOC activation. Here we reveal that, in addition to being an ER Ca(2+) sensor, STIM1 functions within the PM to control operation of the Ca(2+) entry channel itself. Increased expression levels of STIM1 correlate with a gain in function of Ca(2+) release-activated Ca(2+) (CRAC) channel activity. Point mutation of the N-terminal EF hand transforms the CRAC channel current (I(CRAC)) into a constitutively active, Ca(2+) store-independent mode. Mutants in the EF hand and cytoplasmic C terminus of STIM1 alter operational parameters of CRAC channels, including pharmacological profile and inactivation properties. Last, Ab externally applied to the STIM1 N-terminal EF hand blocks both I(CRAC) in hematopoietic cells and SOC-mediated Ca(2+) entry in HEK293 cells, revealing that STIM1 has an important functional presence within the PM. The results reveal that, in addition to being an ER Ca(2+) sensor, STIM1 functions within the PM to exert control over the operation of SOCs. As a cell surface signaling protein, STIM1 represents a key pharmacological target to control fundamental Ca(2+)-regulated processes including secretion, contraction, metabolism, cell division, and apoptosis."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0510050103"xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0510050103"xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "Xu W."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "Xu W."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "Dziadek M.A."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "Dziadek M.A."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "Gill D.L."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "Gill D.L."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "Soboloff J."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "Soboloff J."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "Spassova M.A."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "Spassova M.A."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "He L.-P."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/author | "He L.-P."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/pages | "4040-4045"xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/pages | "4040-4045"xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/title | "STIM1 has a plasma membrane role in the activation of store-operated Ca(2+) channels."xsd:string |
| http://purl.uniprot.org/citations/16537481 | http://purl.uniprot.org/core/title | "STIM1 has a plasma membrane role in the activation of store-operated Ca(2+) channels."xsd:string |