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):

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