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    Desmin interacts with STIM1 and coordinates Ca2+ signaling in skeletal muscle

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    Author
    Zhang, Hengtao
    Bryson, Victoria Graham
    Wang, Chaojian
    Li, TianYu
    Kerr, Jaclyn P
    Wilson, Rebecca
    Muoio, Deborah M
    Bloch, Robert J
    Ward, Christopher
    Rosenberg, Paul B
    Date
    2021-09-08
    Journal
    JCI Insight
    Publisher
    American Society for Clinical Investigation
    Type
    Article
    
    Metadata
    Show full item record
    See at
    https://doi.org/10.1172/jci.insight.143472
    Abstract
    Stromal interaction molecule 1 (STIM1), the sarcoplasmic reticulum (SR) transmembrane protein, activates store-operated Ca2+ entry (SOCE) in skeletal muscle and, thereby, coordinates Ca2+ homeostasis, Ca2+-dependent gene expression, and contractility. STIM1 occupies space in the junctional SR membrane of the triads and the longitudinal SR at the Z-line. How STIM1 is organized and is retained in these specific subdomains of the SR is unclear. Here, we identified desmin, the major type III intermediate filament protein in muscle, as a binding partner for STIM1 based on a yeast 2-hybrid screen. Validation of the desmin-STIM1 interaction by immunoprecipitation and immunolocalization confirmed that the CC1-SOAR domains of STIM1 interact with desmin to enhance STIM1 oligomerization yet limit SOCE. Based on our studies of desmin-KO mice, we developed a model wherein desmin connected STIM1 at the Z-line in order to regulate the efficiency of Ca2+ refilling of the SR. Taken together, these studies showed that desmin-STIM1 assembles a cytoskeletal-SR connection that is important for Ca2+ signaling in skeletal muscle.
    Keyword
    Calcium signaling
    Muscle Biology
    Identifier to cite or link to this item
    http://hdl.handle.net/10713/16586
    ae974a485f413a2113503eed53cd6c53
    10.1172/jci.insight.143472
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