Agrin acts via a MuSK receptor complex

Cell. 1996 May 17;85(4):513-23. doi: 10.1016/s0092-8674(00)81252-0.


Formation of th neuromuscular junction depends upon reciprocal inductive interactions between the developing nerve and muscle, resulting in the precise juxtaposition of a differentiated nerve terminal with a highly specialized patch on the muscle membrane, termed the motor endplate. Agrin is a nerve-derived factor that can induced molecular reorganizations at the motor endplate, but the mechanism of action of agrin remains poorly understood. MuSK is a receptor tyrosine kinase localized to the motor endplate, seemingly well positioned to receive a key nerve-derived signal. Mice lacking either agrin or MuSK have recently been generated and exhibit similarly profound defects in their neuromuscular junctions. Here we demonstrate that agrin acts via a receptor complex that includes MuSK as well as a myotube-specific accessory component.

MeSH terms

  • Agrin / genetics*
  • Agrin / metabolism
  • Animals
  • Gene Deletion
  • Gene Expression / physiology
  • Mice
  • Mice, Knockout
  • Muscle Fibers, Skeletal / physiology
  • Muscle Fibers, Skeletal / ultrastructure
  • Muscle, Skeletal / cytology
  • Muscle, Skeletal / embryology
  • Muscle, Skeletal / physiology
  • Neuromuscular Junction / chemistry
  • Neuromuscular Junction / embryology
  • Neuromuscular Junction / physiology
  • Phosphorylation
  • Protein Structure, Tertiary
  • Receptor Protein-Tyrosine Kinases / chemistry
  • Receptor Protein-Tyrosine Kinases / genetics*
  • Receptor Protein-Tyrosine Kinases / metabolism
  • Receptors, Cholinergic / physiology
  • Signal Transduction / physiology*
  • Tyrosine / metabolism


  • Agrin
  • Receptors, Cholinergic
  • Tyrosine
  • MUSK protein, human
  • Receptor Protein-Tyrosine Kinases