Journal
NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 13, Issue 9, Pages 549-565Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nrm3414
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Funding
- US National Institutes of Health (NIH) [AI058173, GM097335, HL109920, HL086699, GM068523]
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Stromal interaction molecule (STIM) proteins function in cells as dynamic coordinators of cellular calcium (Ca2+) signals. Spanning the endoplasmic reticulum (ER) membrane, they sense tiny changes in the levels of Ca2+ stored within the ER lumen. As ER Ca2+ is released to generate primary Ca2+ signals, STIM proteins undergo an intricate activation reaction and rapidly translocate into junctions formed between the ER and the plasma membrane. There, STIM proteins tether and activate the highly Ca2+-selective Orai channels to mediate finely controlled Ca2+ signals and to homeostatically balance cellular Ca2+. Details are emerging on the remarkable organization within these STIM-induced junctional microdomains and the identification of new regulators and alternative target proteins for STIM.
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