Agrin acts via a MuSK receptor complex

被引:566
作者
Glass, DJ [1 ]
Bowen, DC [1 ]
Stitt, TN [1 ]
Radziejewski, C [1 ]
Bruno, J [1 ]
Ryan, TE [1 ]
Gies, DR [1 ]
Shah, S [1 ]
Mattsson, K [1 ]
Burden, SJ [1 ]
DiStefano, PS [1 ]
Valenzuela, DM [1 ]
DeChiara, TM [1 ]
Yancopoulos, GD [1 ]
机构
[1] NYU,MED CTR,SKIRBALL INST,MOL NEUROBIOL PROGRAM,NEW YORK,NY 10016
关键词
D O I
10.1016/S0092-8674(00)81252-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Formation of the 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 induce 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.
引用
收藏
页码:513 / 523
页数:11
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