Glycobiology of the neuromuscular junction.
Most molecules that are present at synapses are glycosylated with carbohydrates, and some carbohydrate structures are themselves uniquely synaptic in their localization. Thus, proteins or lipids at the synapse may bear distinct carbohydrates that alter their localization or function. Here, I will review the evidence that there are unique synaptic carbohydrates at the neuromuscular junction. Then, I will review the evidence that such carbohydrates can affect the function of synaptic proteins, with particular attention to agrin, dystroglycan, and the neural cell adhesion molecule (NCAM). Finally, I will review recent data that demonstrates a role for one carbohydrate structure, the cytotoxic T cell (CT) antigen, in neuromuscular development. These studies suggest that glycosylation is an important modification to consider in studies of synapse formation and function.
Martin
Paul T
PT
Department of Neuroscience, Glycobiology Research and Training Center, University of California-San Diego, School of Medicine, 9500 Gilman Drive, La Jolla, CA 92093-0691, USA. pmartin@ucsd.edu
D000818:Animals; D006031:Glycosylation; D006801:Humans; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D009469:Neuromuscular Junction / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure
D008562:Membrane Glycoproteins