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STIM1L traps and gates Orai1 channels without remodeling the cortical ER

Published inJournal of cell science, vol. 128, no. 8, p. 1568-1579
Publication date2015
Abstract

STIM proteins populate and expand cortical ER sheets to mediate store-operated Ca(2+) entry (SOCE) by trapping and gating Orai channels in ER-PM clusters. A longer splice variant, STIM1L, forms permanent ER-PM clusters and mediates rapid influx in muscle. Here, we used electron microscopy, TIRF, and Ca(2+) imaging to establish the trafficking and signaling properties of the two STIM1 isoforms in Stim1(-/-)/Stim2(-/-) fibroblasts. Unlike STIM1, STIM1L was poorly recruited into ER-PM clusters and did not mediate store-dependent expansion of cortical ER cisternae. Removal of the STIM1 lysine-rich tail prevented store-dependent cluster enlargement, while inhibition of cytosolic Ca(2+) elevations or removal of the STIM1L actin binding domain had no impact on cluster expansion. Finally, STIM1L restored robust, but not accelerated SOCE and clustered with Orai1 channels more slowly than STIM1 following store depletion. These results indicate that STIM1L does not mediate rapid SOCE but can trap and gate Orai1 channels efficiently without remodeling cortical ER cisternae. The ability of STIM proteins to induce cortical ER formation is dispensable for SOCE and requires the lysine-rich tail of STIM1 involved in binding to phosphoinositides.

Citation (ISO format)
SAUC, Sophie et al. STIM1L traps and gates Orai1 channels without remodeling the cortical ER. In: Journal of cell science, 2015, vol. 128, n° 8, p. 1568–1579. doi: 10.1242/jcs.164228
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ISSN of the journal0021-9533
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