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.