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First published online January 12, 2006
doi: 10.1242/10.1242/jcs.02814
Commentary |
Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, Department of Internal Medicine, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA
* Author for correspondence (e-mail: kevin-campbell{at}uiowa.edu)
Accepted 29 November 2005
- and ß-dystroglycan constitute a membrane-spanning complex that connects the extracellular matrix to the cytoskeleton. Although a structural role for dystroglycan had been identified, biochemical and genetic discoveries have recently highlighted the significance of posttranslational processing for dystroglycan function. Glycosylation is the crucial modification that modulates the function of dystroglycan as a receptor for extracellular binding partners. It has become clear that perturbation of dystroglycan glycosylation is the central event in the pathogenesis of several complex disorders, and recent advances suggest that glycosylation could be modulated to ameliorate the pathological features. Our increased understanding of the mechanisms of interaction of dystroglycan with its ligands has become an essential tool in deciphering the biological processes related to the human diseases in which the proteins are implicated.
Key words: Dystroglycan, Extracellular matrix, Glycosylation
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