title: Molecular dissection of neuromuscular junction formation.
abstract: The muscle-specific kinase (MuSK) is the key component that mediates the synapse-inducing role of motoneuron-derived agrin at the neuromuscular junction. Recent reverse-genetics approaches have shed new light on the events triggered inside myotubes by activation of this kinase. Mice in which most of the intracellular domain of MuSK is replaced by a related kinase are viable. Analysis of the imperfect postsynaptic specializations of these mice has provided new insights into the complex postsynaptic differentiation process.
authors.affiliation: University of Houston, Science and Research Building 2, Houston, TX 77204-5001, USA. whoch@uh.edu
authors.forename: Werner
authors.initials: W
authors.lastname: Hoch
mesh_terms: D018171:Agrin / Q000378:metabolism*; D000818:Animals; D009046:Motor Neurons / Q000378:metabolism; D018485:Muscle Fibers, Skeletal / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000254:growth & development* / Q000378:metabolism; D009469:Neuromuscular Junction / Q000254:growth & development* / Q000378:metabolism; D020794:Receptor Protein-Tyrosine Kinases / Q000378:metabolism*; D011950:Receptors, Cholinergic / Q000378:metabolism*
chemical_list: D018171:Agrin; D011950:Receptors, Cholinergic; C095714:MUSK protein, human; D020794:Receptor Protein-Tyrosine Kinases