title: Signaling mechanisms mediating synapse formation.
abstract: Recent experiments have begun to decipher the molecular dialog that mediates differentiation at sites of synaptic contact between neurons and their targets. It had been hypothesized that the protein agrin is released by axon terminals at embryonic neuromuscular junctions and binds to a receptor on the myofiber surface to trigger postsynaptic differentiation. Now a genetic 'knockout' experiment has confirmed the essential role of agrin in signaling between developing nerve and muscle. A second 'knockout' has shown that the muscle-specific receptor tyrosine kinase MuSK is a critical element in the agrin-induced signaling cascade. Additional results suggest that MuSK may comprise a portion of the agrin receptor.
authors.affiliation: University of Colorado Health Sciences Center, Dept of Physiology, Denver 80262, USA.
authors.forename: B G
authors.initials: BG
authors.lastname: Wallace
mesh_terms: D018171:Agrin / Q000235:genetics / Q000502:physiology; D000818:Animals; D051379:Mice; D018345:Mice, Knockout; D008959:Models, Neurological; D009469:Neuromuscular Junction / Q000502:physiology; D020794:Receptor Protein-Tyrosine Kinases / Q000502:physiology; D011950:Receptors, Cholinergic; D017978:Receptors, Growth Factor / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology; D013569:Synapses / Q000502:physiology*
chemical_list: D018171:Agrin; D011950:Receptors, Cholinergic; D017978:Receptors, Growth Factor; C080030:agrin receptor; C095714:MUSK protein, human; D020794:Receptor Protein-Tyrosine Kinases