New dogs in the dogma: Lrp4 and Tid1 in neuromuscular synapse formation

Neuron. 2008 Nov 26;60(4):526-8. doi: 10.1016/j.neuron.2008.11.003.


Two recent papers reported identification of a long-sought agrin coreceptor, Lrp4 (Kim et al. in Cell and Zhang et al. in Neuron). In this issue of Neuron, Linnoila et al. report the identification of a new player in the agrin-MuSK pathway, Tid1, which directly interacts with MuSK and is responsible for transducing signals from MuSK activation to AChR clustering, culminating in cross-linking to the subsynaptic cytoskeleton. These papers substantially reshape the agrin-MuSK-ACh hypothesis of neuromuscular synaptogenesis.

Publication types

  • Review
  • Comment

MeSH terms

  • Agrin / metabolism*
  • Animals
  • HSP40 Heat-Shock Proteins / metabolism*
  • Humans
  • LDL-Receptor Related Proteins
  • Mice
  • Neuromuscular Junction / embryology*
  • Neuromuscular Junction / metabolism*
  • Neuromuscular Junction / ultrastructure
  • Receptor Aggregation / physiology
  • Receptor Protein-Tyrosine Kinases / metabolism
  • Receptors, Cholinergic / metabolism
  • Receptors, LDL / metabolism*
  • Signal Transduction / physiology
  • Synapses / metabolism*
  • Synapses / ultrastructure


  • Agrin
  • Dnaja3 protein, mouse
  • HSP40 Heat-Shock Proteins
  • LDL-Receptor Related Proteins
  • Lrp4 protein, mouse
  • Receptors, Cholinergic
  • Receptors, LDL
  • MuSK protein, mouse
  • Receptor Protein-Tyrosine Kinases