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. 2003 Oct 15;375(Pt 2):329–337. doi: 10.1042/BJ20030808

Direct interaction of beta-dystroglycan with F-actin.

Yun-Ju Chen 1, Heather J Spence 1, Jacqueline M Cameron 1, Thomas Jess 1, Jane L Ilsley 1, Steven J Winder 1
PMCID: PMC1223702  PMID: 12892561

Abstract

Dystroglycans are essential transmembrane adhesion receptors for laminin. Alpha-dystroglycan is a highly glycosylated extracellular protein that interacts with laminin in the extracellular matrix and the transmembrane region of beta-dystroglycan. Beta-dystroglycan, via its cytoplasmic tail, interacts with dystrophin and utrophin and also with the actin cytoskeleton. As a part of the dystrophin-glycoprotein complex of muscles, dystroglycan is also important in maintaining sarcolemmal integrity. Mutations in dystrophin that lead to Duchenne muscular dystrophy also lead to a loss of dystroglycan from the sarcolemma, and chimaeric mice lacking muscle dystroglycan exhibit a severe muscular dystrophy phenotype. Using yeast two-hybrid analysis and biochemical and cell biological studies, we show, in the present study, that the cytoplasmic tail of beta-dystroglycan interacts directly with F-actin and, furthermore, that it bundles actin filaments and induces an aberrant actin phenotype when overexpressed in cells.

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Selected References

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