Related Experiment Video
Updated: May 9, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 10, 2010
Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor
S H Gee1, F Montanaro, M H Lindenbaum
1Centre for Research in Neuroscience, McGill University, Montreal General Hospital Research Institute, Quebec, Canada.
Abstract:
Aggregation of acetylcholine receptors (AChRs) on skeletal muscle fibers is thought to be mediated by the basal lamina protein agrin. Structural similarities shared by agrin and laminin suggested that the laminin receptor dystroglycan-alpha, part of a dystrophin-receptor complex, might also bind agrin. We show here that dystroglycan-alpha and dystrophin-related protein (DRP/utrophin) are concentrated within AChR aggregates in cultures of C2 myotubes and that agrin binds specifically to dystroglycan-alpha in in vitro assays. This binding is calcium dependent and is inhibited by monoclonal antibody (MAb) IIH6 against dystroglycan-alpha, heparin, and laminin, but not by fibronectin. In S27 cells, which do not aggregate AChRs spontaneously, agrin and laminin binding to dystroglycan-alpha are dramatically decreased. Moreover, MAb IIH6 significantly inhibits agrin-induced AChR aggregation on C2 cells. We conclude that dystroglycan-alpha is an agrin-binding protein and part of a dystrophin-receptor complex involved in AChR aggregation.
More Related Videos
Related Concept Videos
Cytoskeletal Linker Proteins - Plakins
Cytoskeletal Accessory Proteins
Proteoglycans
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Activation and Inactivation of G Proteins
Desmosomes

