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dc.contributor.authorZhang, Hengtao
dc.contributor.authorBryson, Victoria Graham
dc.contributor.authorWang, Chaojian
dc.contributor.authorLi, TianYu
dc.contributor.authorKerr, Jaclyn P
dc.contributor.authorWilson, Rebecca
dc.contributor.authorMuoio, Deborah M
dc.contributor.authorBloch, Robert J
dc.contributor.authorWard, Christopher
dc.contributor.authorRosenberg, Paul B
dc.date.accessioned2021-09-13T13:50:54Z
dc.date.available2021-09-13T13:50:54Z
dc.date.issued2021-09-08
dc.identifier.urihttp://hdl.handle.net/10713/16586
dc.description.abstractStromal 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.en_US
dc.description.urihttps://doi.org/10.1172/jci.insight.143472en_US
dc.language.isoenen_US
dc.publisherAmerican Society for Clinical Investigationen_US
dc.relation.ispartofJCI Insighten_US
dc.subjectCalcium signalingen_US
dc.subjectMuscle Biologyen_US
dc.titleDesmin interacts with STIM1 and coordinates Ca2+ signaling in skeletal muscleen_US
dc.typeArticleen_US
dc.identifier.doi10.1172/jci.insight.143472
dc.identifier.pmid34494555
dc.source.volume6
dc.source.issue17
dc.source.countryUnited States


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