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¹ Torrey Pines Therapeutics, Inc., La Jolla, CA 92037
² Department of Physiology and Biophysics and Center for Immunology, University of California, Irvine, CA 92697

Correspondence to K.A. Stauderman: kstauderman{at}torreypinestherapeutics.com; or M.D. Cahalan: mcahalan{at}uci.edu

Store-operated Ca²⁺ (SOC) channels regulate many cellular processes, but the underlying molecular components are not well defined. Using an RNA interference (RNAi)-based screen to identify genes that alter thapsigargin (TG)-dependent Ca²⁺ entry, we discovered a required and conserved role of Stim in SOC influx. RNAi-mediated knockdown of Stim in Drosophila S2 cells significantly reduced TG-dependent Ca²⁺ entry. Patch-clamp recording revealed nearly complete suppression of the Drosophila Ca²⁺ release-activated Ca²⁺ (CRAC) current that has biophysical characteristics similar to CRAC current in human T cells. Similarly, knockdown of the human homologue STIM1 significantly reduced CRAC channel activity in Jurkat T cells. RNAi-mediated knockdown of STIM1 inhibited TG- or agonist-dependent Ca²⁺ entry in HEK293 or SH-SY5Y cells. Conversely, overexpression of STIM1 in HEK293 cells modestly enhanced TG-induced Ca²⁺ entry. We propose that STIM1, a ubiquitously expressed protein that is conserved from Drosophila to mammalian cells, plays an essential role in SOC influx and may be a common component of SOC and CRAC channels.

A.V. Yeromin and P.J. DiGregorio contributed equally to this work.

Abbreviations used in this paper: [Ca²⁺]_i, intracellular free Ca²⁺ concentration; CRAC, Ca²⁺ release-activated Ca²⁺; dsRNA, double-stranded RNA; iPLA₂, Ca²⁺-independent PLA₂; RFU, relative fluorescence unit; RNAi, RNA interference; SOC, store-operated Ca²⁺; SOCE, SOC entry; TG, thapsigargin.

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