Abstract:
:Neuromuscular junction (NMJ) formation requires agrin, a factor released from motoneurons, and MuSK, a transmembrane tyrosine kinase that is activated by agrin. However, how signal is transduced from agrin to MuSK remains unclear. We report that LRP4, a low-density lipoprotein receptor (LDLR)-related protein, is expressed specifically in myotubes and binds to neuronal agrin. Its expression enables agrin binding and MuSK signaling in cells that otherwise do not respond to agrin. Suppression of LRP4 expression in muscle cells attenuates agrin binding, agrin-induced MuSK tyrosine phosphorylation, and AChR clustering. LRP4 also forms a complex with MuSK in a manner that is stimulated by agrin. Finally, we showed that LRP4 becomes tyrosine-phosphorylated in agrin-stimulated muscle cells. These observations indicate that LRP4 is a coreceptor of agrin that is necessary for MuSK signaling and AChR clustering and identify a potential target protein whose mutation and/or autoimmunization may cause muscular dystrophies.
journal_name
Neuronjournal_title
Neuronauthors
Zhang B,Luo S,Wang Q,Suzuki T,Xiong WC,Mei Ldoi
10.1016/j.neuron.2008.10.006subject
Has Abstractpub_date
2008-10-23 00:00:00pages
285-97issue
2eissn
0896-6273issn
1097-4199pii
S0896-6273(08)00849-0journal_volume
60pub_type
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