title: The inside and out of dystroglycan post-translational modification.
abstract: 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.
authors: Department of Biomedical Science, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK. chris.moore@sheffield.ac.uk
authors: Chris J
authors: CJ
authors: Moore
authors: Steve J
authors: SJ
authors: Winder
mesh_terms: D000818:Animals; D049030:Dystroglycans / Q000235:genetics / Q000378:metabolism*; D016189:Dystrophin / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007797:Laminin / Q000235:genetics / Q000378:metabolism; D009154:Mutation / Q000235:genetics; D017351:N-Acetylglucosaminyltransferases / Q000235:genetics / Q000378:metabolism; D011499:Protein Processing, Post-Translational
chemical_list: D016189:Dystrophin; D007797:Laminin; D049030:Dystroglycans; C117674:LARGE1 protein, human; D017351:N-Acetylglucosaminyltransferases