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SH3 Domain-mediated Interaction of Dystroglycan and Grb2
Journal article   Open access   Peer reviewed

SH3 Domain-mediated Interaction of Dystroglycan and Grb2

Bin Yang, Daniel Jung, David Motto, Jon Meyer, Gary Koretzky and Kevin P Campbell
The Journal of biological chemistry, Vol.270(20), pp.11711-11714
05/19/1995
DOI: 10.1074/jbc.270.20.11711
PMID: 7744812
url
https://doi.org/10.1074/jbc.270.20.11711View
Published (Version of record) Open Access

Abstract

Dystroglycan is a novel laminin receptor that links the extracellular matrix and sarcolemma in skeletal muscle. The dystroglycan complex containing alpha- and beta-dystroglycan also serves as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. beta-Dystroglycan has now been expressed in vitro and shown to directly interact with Grb2, an adapter protein involved in signal transduction and cytoskeletal organization. Protein binding assays with two Grb2 mutants, Grb2/P49L and Grb2/G203R, which correspond to the loss-of-function mutants in the Caenorhabditis elegans sem-5, demonstrated that the dystroglycan-Grb2 association is through beta-dystroglycan C-terminal proline-rich domains and Grb2 Src homology 3 domains. Affinity chromatography has also shown endogenous skeletal muscle Grb2 interacts with beta-dystroglycan. Immunoprecipitation experiments have demonstrated that Grb2 associates with alpha/beta-dystroglycan in vivo in both skeletal muscle and brain. The specific dystroglycan-Grb2 interaction may play an important role in extracellular matrix-mediated signal transduction and/or cytoskeleton organization in skeletal muscle that may be essential for muscle cell viability.

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