Direct interaction of beta-dystroglycan with F-actin

Chen, Y.J., Spence, H.J., Cameron, J.M., Jess, T., Ilsley, J.L. and Winder, S.J. (2003) Direct interaction of beta-dystroglycan with F-actin. Biochemical Journal, 375, pp. 329-337.

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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.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Spence, Dr Heather
Authors: Chen, Y.J., Spence, H.J., Cameron, J.M., Jess, T., Ilsley, J.L., and Winder, S.J.
College/School:College of Medical Veterinary and Life Sciences
Journal Name:Biochemical Journal
Publisher:Portland Press Ltd.
ISSN (Online):1470-8728

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