In neuromuscular systems dystroglycan provides a vital link between laminin in the extracellular matrix and dystrophin in the membrane cytoskeleton. The integrity of this link is maintained and regulated by post-translational modifications of dystroglycan that have effects both inside and outside the cell. Glycosylation of α-dystroglycan is crucial for its link to laminin and phosphorylation of β-dystroglycan on tyrosine regulates its association with intracellular binding partners. This short review focuses on some of the recent developments in our understanding of the role of these post-translational modification in regulating dystroglycan function, and how new knowledge of signalling through the laminin-dystroglycan axis is leading to hope for treatment for some neuromuscular diseases associated with this adhesion complex.
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