Agrin acts via a MuSK receptor complex
Agrin acts via a MuSK receptor complex
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DOI：
10.1016/s0092-8674(00)81252-0
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发表时间：
1996-05-17
期刊：
影响因子：
64.5
通讯作者：
Yancopoulos, GD
中科院分区：
文献类型：
--
作者：
Glass, DJ;Bowen, DC;Yancopoulos, GD
神经肌肉接头的形成取决于发育中的神经和肌肉之间的相互诱导相互作用，导致分化的神经末梢与肌肉膜上高度特化的补丁（称为运动终板）精确并列。聚集蛋白是一种神经源性因子，可以诱导运动终板的分子重组，但其作用机制仍知之甚少。MuSK是一种定位于运动终板的受体酪氨酸激酶，似乎很好地定位于接收关键的神经源性信号。最近已经产生了缺乏聚集蛋白或MUSK的小鼠，并且在它们的神经肌肉接头中表现出类似的严重缺陷。在这里，我们表明，聚集蛋白的行为通过一个受体复合物，包括MuSK以及肌管特异性配件。
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.