| http://purl.uniprot.org/citations/35065666 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/35065666 | http://www.w3.org/2000/01/rdf-schema#comment | "BackgroundThe sarcoglycan complex (SC) is part of a network that links the striated muscle cytoskeleton to the basal lamina across the sarcolemma. The SC coordinates changes in phosphorylation and Ca++-flux during mechanical deformation, and these processes are disrupted with loss-of-function mutations in gamma-sarcoglycan (Sgcg) that cause Limb girdle muscular dystrophy 2C/R5.MethodsTo gain insight into how the SC mediates mechano-signaling in muscle, we utilized LC-MS/MS proteomics of SC-associated proteins in immunoprecipitates from enriched sarcolemmal fractions. Criteria for inclusion were co-immunoprecipitation with anti-Sgcg from C57BL/6 control muscle and under-representation in parallel experiments with Sgcg-null muscle and with non-specific IgG. Validation of interaction was performed in co-expression experiments in human RH30 rhabdomyosarcoma cells.ResultsWe identified 19 candidates as direct or indirect interactors for Sgcg, including the other 3 SC proteins. Novel potential interactors included protein-phosphatase-1-catalytic-subunit-beta (Ppp1cb, PP1b) and Na+-K+-Cl--co-transporter NKCC1 (SLC12A2). NKCC1 co-localized with Sgcg after co-expression in human RH30 rhabdomyosarcoma cells, and its cytosolic domains depleted Sgcg from cell lysates upon immunoprecipitation and co-localized with Sgcg after detergent permeabilization. NKCC1 localized in proximity to the dystrophin complex at costameres in vivo. Bumetanide inhibition of NKCC1 cotransporter activity in isolated muscles reduced SC-dependent, strain-induced increases in phosphorylation of extracellular signal-regulated kinases 1 and 2 (ERK1/2). In silico analysis suggests that candidate SC interactors may cross-talk with survival signaling pathways, including p53, estrogen receptor, and TRIM25.ConclusionsResults support that NKCC1 is a new SC-associated signaling protein. Moreover, the identities of other candidate SC interactors suggest ways by which the SC and NKCC1, along with other Sgcg interactors such as the membrane-cytoskeleton linker archvillin, may regulate kinase- and Ca++-mediated survival signaling in skeletal muscle."xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.org/dc/terms/identifier | "doi:10.1186/s13395-021-00285-2"xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/author | "Smith T.C."xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/author | "Shaffer S.A."xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/author | "Luna E.J."xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/author | "Chou C.H."xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/author | "Barton E.R."xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/author | "Puglise J.M."xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/author | "Vasilakos G."xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/date | "2022"xsd:gYear |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/name | "Skelet Muscle"xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/pages | "2"xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/title | "Novel gamma-sarcoglycan interactors in murine muscle membranes."xsd:string |
| http://purl.uniprot.org/citations/35065666 | http://purl.uniprot.org/core/volume | "12"xsd:string |
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