O -Mannosyl Phosphorylation of Alpha-Dystroglycan Is Required for Laminin Binding
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- 1 January 2010
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 327 (5961), 88-92
- https://doi.org/10.1126/science.1180512
Abstract
Modifying Protein Modification: Alpha-dystroglycan (α-DG) is a cell-surface receptor that anchors the basal lamina to the sarcolemma by binding proteins containing laminin-G domains. This binding is essential for protecting muscle from contraction-induced injury, and defective binding is thought to cause a subclass of congenital muscular dystrophy (CMD) in humans. Mutations in six (putative) glycosyltransferase genes have been identified in patients with CMD, suggesting that glycosylation of α-DG may confer the ability to bind laminin. Despite extensive efforts for over 20 years, the actual laminin-binding moiety has remained unclear. Now, Yoshida-Moriguchi et al. (p. 88 ) have identified a phosphorylated O -mannosyl glycan on α-DG. This modification occurred in the Golgi via an unidentified kinase and was required for the maturation of α-DG into its laminin-binding form.Keywords
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