Agrin Acts via a MuSK Receptor Complex

  title={Agrin Acts via a MuSK Receptor Complex},
  author={David J. Glass and David C. Bowen and Trevor Stitt and Czeslaw H Radziejewski and Joanne Bruno and Terence E. Ryan and David R. Gies and Sonal Shah and Karen Mattsson and Steven J. Burden and Peter S. Distefano and David M. Valenzuela and Thomas M. Dechiara and George D. Yancopoulos},

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Lrp4 Is a Receptor for Agrin and Forms a Complex with MuSK

Structural basis of agrin-LRP4-MuSK signaling.

It is shown that the tetrameric complex is essential for neuronal agrin-induced acetylcholine receptor (AChR) clustering and represent a novel mechanism for activation of receptor tyrosine kinases.

Induction of multiple signaling loops by MuSK during neuromuscular synapse formation

Agrin activation leads to the establishment of a neuregulin-1-dependent signaling complex that maintains MuSK, ErbB, and AChR expression at the synapse of electrically active muscle fibers.

Distinct Domains of Musk Mediate Its Abilities to Induce and to Associate with Postsynaptic Specializations

The results indicate that the ectodomain of MuSK mediates both agrin- dependent activation of a complex signal transduction pathway and agin-independent association of the kinase with other postsynaptic components.

Tid1 Mediates Agrin and Muscle Specific Kinase Signaling at the Neuromuscular Junction

Tid1 is implicate as a novel NMJ player and a new class of molecules in the agrin/MuSK signaling cascade is defined, which may reveal mechanisms important for the formation and maintenance of synapses.

Formation of the neuromuscular junction. Agrin and its unusual receptors.

  • W. Hoch
  • Biology, Chemistry
    European journal of biochemistry
  • 1999
The picture of the molecular pathway causing the redistribution of synaptic proteins is still incomplete, but many components of the machinery triggering postsynaptic differentiation have now been identified and interactions of the extracellular domain with unknown components are also required.

Signaling complexes for postsynaptic differentiation

Results suggest that MuSK may function as a scaffold tyrosine kinase that forms a multi-molecule complex for AChR clustering.



Defective Neuromuscular Synaptogenesis in Agrin-Deficient Mutant Mice

Building synapses: agrin and dystroglycan stick together

Structural domains of agrin required for clustering of nicotinic acetylcholine receptors.

The data suggest that four domains in the C‐terminal 55 kDa of agrin contribute to its nAChR clustering activity, which is one of the earliest steps in synapse formation.

Dystroglycan binds nerve and muscle agrin

Structure and expression of a rat agrin