Proteomics

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Sarcoglycan interactions in murine muscle membranes


ABSTRACT: The 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. To gain insight into how the SC mediates mechano-signaling in muscle, we utilized LC-MS/MS proteomics to identify SC-associated proteins in immunoprecipitates from enriched sarcolemmal fractions. Criteria for inclusion were selective co-immunoprecipitation with anti-Sgcg from C57BL/6 control muscle, but under-representation in parallel experiments with Sgcg-null muscle or with non-specific IgG. Co-immunoprecipitation from archvillin-deleted muscle (Svil-null) was also evaluated.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Plasma Membrane, Muscle Fibre, Gastrocnemius

DISEASE(S): Autosomal Recessive Limb-girdle Muscular Dystrophy Type 2c

SUBMITTER: Scott Shaffer  

LAB HEAD: Elizabeth J. Luna

PROVIDER: PXD028584 | Pride | 2022-02-16

REPOSITORIES: Pride

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Novel γ-sarcoglycan interactors in murine muscle membranes.

Smith Tara C TC   Vasilakos Georgios G   Shaffer Scott A SA   Puglise Jason M JM   Chou Chih-Hsuan CH   Barton Elisabeth R ER   Luna Elizabeth J EJ  

Skeletal muscle 20220122 1


<h4>Background</h4>The 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<sup>++</sup>-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.<h4>Methods</h4>To gain insight into how the SC mediates mechano-signaling in muscle, we utilized LC  ...[more]

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