RGD Reference Report - Agrin acts via a MuSK receptor complex. - Rat Genome Database

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Agrin acts via a MuSK receptor complex.

Authors: Glass, DJ  Bowen, DC  Stitt, TN  Radziejewski, C  Bruno, J  Ryan, TE  Gies, DR  Shah, S  Mattsson, K  Burden, SJ  DiStefano, PS  Valenzuela, DM  DeChiara, TM  Yancopoulos, GD 
Citation: Glass DJ, etal., Cell 1996 May 17;85(4):513-23.
RGD ID: 1300271
Pubmed: PMID:8653787   (View Abstract at PubMed)

Formation of th neuromuscular junction depends upon reciprocal inductive interactions between the developing nerve and muscle, resulting in the precise juxtaposition of a differentiated nerve terminal with a highly specialized patch on the muscle membrane, termed the motor endplate. Agrin is a nerve-derived factor that can induced molecular reorganizations at the motor endplate, but the mechanism of action of agrin remains poorly understood. MuSK is a receptor tyrosine kinase localized to the motor endplate, seemingly well positioned to receive a key nerve-derived signal. Mice lacking either agrin or MuSK have recently been generated and exhibit similarly profound defects in their neuromuscular junctions. Here we demonstrate that agrin acts via a receptor complex that includes MuSK as well as a myotube-specific accessory component.

Objects referenced in this article
Gene Musk muscle, skeletal, receptor tyrosine kinase Mus musculus
Gene Agrn agrin Rattus norvegicus

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