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Park, Chan Young
Calcium Dynamics Lab
Research Interests
  • Calcium Signaling, calcium Channels, immune, neuroscience, drug Development

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Alternative splicing converts STIM2 from an activator to an inhibitor of store-operated calcium channels

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Title
Alternative splicing converts STIM2 from an activator to an inhibitor of store-operated calcium channels
Author
Park, Chan YoungDolmetsch, Ricardo E.Lewis, Richard S.Rana, AnshulYen, MichelleSadaghiani, Amir MasoudMalmersjo, Seth
Issue Date
2015-06
Publisher
ROCKEFELLER UNIV PRESS
Citation
JOURNAL OF CELL BIOLOGY, v.209, no.5, pp.653 - 670
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 Ca2+ stores and activate Orai channels in the plasma membrane. Although the amplitude and dynamics of SOCE are considered important determinants of Ca2+-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 Ca2+ signals.
URI
https://scholarworks.unist.ac.kr/handle/201301/11806
URL
http://jcb.rupress.org/content/209/5/653.abstract
DOI
10.1083/jcb.201412060
ISSN
0021-9525
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