The synaptic muscle-specific kinase (MuSK) complex: new partners, new functions

Bioessays. 2005 Nov;27(11):1129-35. doi: 10.1002/bies.20305.


The muscle-specific kinase MuSK is part of an agrin receptor complex that stimulates tyrosine phosphorylation and drives clustering of acetylcholine receptors (AChRs) in the postsynaptic membrane at the vertebrate neuromuscular junction (NMJ). MuSK also regulates synaptic gene transcription in subsynaptic nuclei. Over the past few years, decisive progress has been made in the identification of MuSK effectors, helping to understand its function in the formation of the NMJ. Similarly to AChR, MuSK and several of its partners are the target of mutations responsible for diseases of the NMJ, such as congenital myasthenic syndromes. This minireview will focus on the multiple MuSK effectors so far identified that place MuSK at the center of a multifunctional signaling complex involved in the organization of the NMJ and associated disorders.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Phosphotyrosine / metabolism
  • Protein Binding
  • Receptor Protein-Tyrosine Kinases / genetics
  • Receptor Protein-Tyrosine Kinases / immunology
  • Receptor Protein-Tyrosine Kinases / metabolism*
  • Receptors, Cholinergic / genetics
  • Receptors, Cholinergic / immunology
  • Receptors, Cholinergic / metabolism*
  • Signal Transduction
  • Synapses / genetics
  • Synapses / immunology
  • Synapses / metabolism*


  • Receptors, Cholinergic
  • Phosphotyrosine
  • Receptor Protein-Tyrosine Kinases