Literature DB >> 22914293

STIM proteins: dynamic calcium signal transducers.

Jonathan Soboloff1, Brad S Rothberg, Muniswamy Madesh, Donald L Gill.   

Abstract

Stromal interaction molecule (STIM) proteins function in cells as dynamic coordinators of cellular calcium (Ca(2+)) signals. Spanning the endoplasmic reticulum (ER) membrane, they sense tiny changes in the levels of Ca(2+) stored within the ER lumen. As ER Ca(2+) is released to generate primary Ca(2+) 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 Ca(2+)-selective Orai channels to mediate finely controlled Ca(2+) signals and to homeostatically balance cellular Ca(2+). 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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Year:  2012        PMID: 22914293      PMCID: PMC3458427          DOI: 10.1038/nrm3414

Source DB:  PubMed          Journal:  Nat Rev Mol Cell Biol        ISSN: 1471-0072            Impact factor:   94.444


  199 in total

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Journal:  Mol Cell       Date:  2008-11-07       Impact factor: 17.970

7.  S-glutathionylation activates STIM1 and alters mitochondrial homeostasis.

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Journal:  J Biol Chem       Date:  2008-07-17       Impact factor: 5.157

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Review 5.  Ca2+ and lipid signals hold hands at endoplasmic reticulum-plasma membrane contact sites.

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6.  Junctional membrane Ca2+ dynamics in human muscle fibers are altered by malignant hyperthermia causative RyR mutation.

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Review 7.  Sterol hindrance of Orai activation.

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