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- W2124304575 abstract "Store-operated calcium entry (SOCE) regulates a wide variety of essential cellular functions. SOCE is mediated by STIM1 and STIM2, which sense depletion of ER Ca(2+) stores and activate Orai channels in the plasma membrane. Although the amplitude and dynamics of SOCE are considered important determinants of Ca(2+)-dependent responses, the underlying modulatory mechanisms are unclear. In this paper, we identify STIM2β, a highly conserved alternatively spliced isoform of STIM2, which, in contrast to all known STIM isoforms, is a potent inhibitor of SOCE. Although STIM2β does not by itself strongly bind Orai1, it is recruited to Orai1 channels by forming heterodimers with other STIM isoforms. Analysis of STIM2β mutants and Orai1-STIM2β chimeras suggested that it actively inhibits SOCE through a sequence-specific allosteric interaction with Orai1. Our results reveal a previously unrecognized functional flexibility in the STIM protein family by which alternative splicing creates negative and positive regulators of SOCE to shape the amplitude and dynamics of Ca(2+) signals." @default.
- W2124304575 created "2016-06-24" @default.
- W2124304575 creator A5004406457 @default.
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- W2124304575 creator A5079895950 @default.
- W2124304575 creator A5084286497 @default.
- W2124304575 date "2015-06-01" @default.
- W2124304575 modified "2023-10-15" @default.
- W2124304575 title "Alternative splicing converts STIM2 from an activator to an inhibitor of store-operated calcium channels" @default.
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- W2124304575 doi "https://doi.org/10.1083/jcb.201412060" @default.
- W2124304575 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4460148" @default.
- W2124304575 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26033257" @default.
- W2124304575 hasPublicationYear "2015" @default.
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