Desmin interacts with STIM1 and coordinates Ca2+ signaling in skeletal muscle
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 membra...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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American Society for Clinical investigation
2021-09-01
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| Series: | JCI Insight |
| Subjects: | |
| Online Access: | https://doi.org/10.1172/jci.insight.143472 |
| _version_ | 1811227781350031360 |
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| author | Hengtao Zhang Victoria Graham Bryson Chaojian Wang TianYu Li Jaclyn P. Kerr Rebecca Wilson Deborah M. Muoio Robert J. Bloch Christopher Ward Paul B. Rosenberg |
| author_facet | Hengtao Zhang Victoria Graham Bryson Chaojian Wang TianYu Li Jaclyn P. Kerr Rebecca Wilson Deborah M. Muoio Robert J. Bloch Christopher Ward Paul B. Rosenberg |
| author_sort | Hengtao Zhang |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T09:46:34Z |
| format | Article |
| id | doaj.art-4ef5dfde9ee943f784bb8eee0d805e3a |
| institution | Directory Open Access Journal |
| issn | 2379-3708 |
| language | English |
| last_indexed | 2024-04-12T09:46:34Z |
| publishDate | 2021-09-01 |
| publisher | American Society for Clinical investigation |
| record_format | Article |
| series | JCI Insight |
| spelling | doaj.art-4ef5dfde9ee943f784bb8eee0d805e3a2022-12-22T03:37:55ZengAmerican Society for Clinical investigationJCI Insight2379-37082021-09-01617Desmin interacts with STIM1 and coordinates Ca2+ signaling in skeletal muscleHengtao ZhangVictoria Graham BrysonChaojian WangTianYu LiJaclyn P. KerrRebecca WilsonDeborah M. MuoioRobert J. BlochChristopher WardPaul B. RosenbergStromal 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.https://doi.org/10.1172/jci.insight.143472Muscle biology |
| spellingShingle | Hengtao Zhang Victoria Graham Bryson Chaojian Wang TianYu Li Jaclyn P. Kerr Rebecca Wilson Deborah M. Muoio Robert J. Bloch Christopher Ward Paul B. Rosenberg Desmin interacts with STIM1 and coordinates Ca2+ signaling in skeletal muscle JCI Insight Muscle biology |
| title | Desmin interacts with STIM1 and coordinates Ca2+ signaling in skeletal muscle |
| title_full | Desmin interacts with STIM1 and coordinates Ca2+ signaling in skeletal muscle |
| title_fullStr | Desmin interacts with STIM1 and coordinates Ca2+ signaling in skeletal muscle |
| title_full_unstemmed | Desmin interacts with STIM1 and coordinates Ca2+ signaling in skeletal muscle |
| title_short | Desmin interacts with STIM1 and coordinates Ca2+ signaling in skeletal muscle |
| title_sort | desmin interacts with stim1 and coordinates ca2 signaling in skeletal muscle |
| topic | Muscle biology |
| url | https://doi.org/10.1172/jci.insight.143472 |
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