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2010
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info:eu-repo/semantics/altIdentifier/doi/10.1126/science.1180512
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info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_5B98B675F5702
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Muscular dystrophiesCiter ce document
Takako Yoshida-Moriguchi et al., « O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding. », Serveur académique Lausannois, ID : 10.1126/science.1180512
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Alpha-dystroglycan (alpha-DG) is a cell-surface glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains and certain arenaviruses. Receptor binding is thought to be mediated by a posttranslational modification, and defective binding with laminin underlies a subclass of congenital muscular dystrophy. Using mass spectrometry- and nuclear magnetic resonance (NMR)-based structural analyses, we identified a phosphorylated O-mannosyl glycan on the mucin-like domain of recombinant alpha-DG, which was required for laminin binding. We demonstrated that patients with muscle-eye-brain disease and Fukuyama congenital muscular dystrophy, as well as mice with myodystrophy, commonly have defects in a postphosphoryl modification of this phosphorylated O-linked mannose, and that this modification is mediated by the like-acetylglucosaminyltransferase (LARGE) protein. These findings expand our understanding of the mechanisms that underlie congenital muscular dystrophy.