The Ig1/2 domain of MuSK binds to muscle surface and is involved in acetylcholine receptor clustering

Qiang Wang, Bin Zhang, Ye Elaine Wang, Wen Cheng Xiong, Lin Mei

Research output: Contribution to journalArticlepeer-review

Abstract

The neuromuscular junction, the synapse between motor neurons and muscle cells, serves as an excellent model for studying synapse formation. Agrin is believed to be released by motor neurons to induce postsynaptic differentiation at the neuromuscular junction. MuSK, a receptor tyrosine kinase, appears to be a key component of the agrin receptor complex. However, how agrin activates MuSK remains unclear. To address this question, we characterized the binding of the MuSK extracellular region to the muscle cell surface. The MuSK ectodomain was found to bind to muscle cells in a manner dependent on stimulation with neural agrin. Moreover, the binding was myotube specific and appeared to be mediated by two regions in the MuSK: one region containing the first and second immunoglobin domains and the other containing the cysteine-rich domain. Importantly, recombinant proteins containing the binding activity can block full-length MuSK binding to muscle cells and agrin-induced AChR clustering. These results suggest that the Ig1/2 domain of MuSK is involved in AChR clustering by binding to the muscle surface.

Original languageEnglish (US)
Pages (from-to)246-253
Number of pages8
JournalNeuroSignals
Volume16
Issue number2-3
DOIs
StatePublished - Feb 2008

Keywords

  • Acetylcholine receptor
  • Agrin
  • Binding
  • Ectodomain
  • MuSK
  • Neuromuscular junction

ASJC Scopus subject areas

  • Neurology
  • Developmental Neuroscience
  • Cellular and Molecular Neuroscience

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