Glycobiology Advance Access originally published online on May 7, 2003
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Glycobiology, 2003, Vol. 13, No. 8 55R-66R
© 2003 Oxford University Press
REVIEW |
Dystroglycan glycosylation and its role in matrix binding in skeletal muscle
Department of Neuroscience, Glycobiology Research and Training Center, University of California, San Diego, School of Medicine, La Jolla, CA 92093-0691
accepted on April 24, 2003
Dystroglycan is an essential component of the dystrophin–glycoprotein complex. Three glycan sequencing studies have identified O-linked mannose chains, including NeuAc
2, 3Galß1,4GlcNAcß1,2Man-O, on dystroglycan. Chemical deglycosylation of dystroglycan, antibody blocking studies, and glycan blocking studies all suggest that the O-linked glycans on dystroglycan mediate the binding of extracellular matrix proteins in skeletal muscle. Structural data on laminin G domains and agrin-binding studies also suggest this is the case. Dystroglycan, however, is able to bind proteins via mechanisms that do not involve O-linked glycans. Moreover, laminin and other matrix proteins can bind cell adhesion molecules via their glycan chains. Thus although complex and sometimes not overly convincing, these data suggest that glycosylation plays an important role in dystroglycan binding and function in skeletal muscle.
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