STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx

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Ca2+ signaling in nonexcitable cells is typically initiated by receptor-triggered production of inositol-1,4,5-tris-phosphate and the release of Ca2+ from intracellular stores [1]. An elusive signaling process senses the Ca2+ store depletion and triggers the opening of plasma membrane Ca2+ channels [2-5]. The resulting sustained Ca2+ signals are required for many physiological responses, such as T cell activation and differentiation [6]. Here, we monitored receptor-triggered Ca2+ signals in cells transfected with siRNAs against 2,304 human signaling proteins, and we identified two proteins required for Ca2+-store-depletion-mediated Ca2+ influx, STIM1 and STIM2 [7-9]. These proteins have a single transmembrane region with a putative Ca2+ binding domain in the lumen of the endoplasmic reticulum. Ca2+ store depletion led to a rapid translocation of STIM1 into puncta that accumulated near the plasma membrane. Introducing a point mutation in the STIM1 Ca2+ binding domain resulted in prelocalization of the protein in puncta, and this mutant failed to respond to store depletion. Our study suggests that STIM proteins function as Ca2+ store sensors in the signaling pathway connecting Ca2+ store depletion to Ca2+ influx.
Publisher
CELL PRESS
Issue Date
2005-07
Language
English
Article Type
Article
Keywords

CALCIUM-ENTRY; HELA-CELLS; GENE; IDENTIFICATION; MECHANISMS; PROTEINS

Citation

CURRENT BIOLOGY, v.15, no.13, pp.1235 - 1241

ISSN
0960-9822
DOI
10.1016/j.cub.2005.05.055
URI
http://hdl.handle.net/10203/90421
Appears in Collection
BS-Journal Papers(저널논문)
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