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| Research article summary (published 15 May 1996): |
Agrin acts via a MuSK receptor complex.
Full Abstract
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.
Author information
Author/s: Glass, D J (DJ); Bowen, D C (DC); Stitt, T N (TN); Radziejewski, C (C); Bruno, J (J); Ryan, T E (TE); Gies, D R (DR); Shah, S (S); Mattsson, K (K); Burden, S J (SJ); DiStefano, P S (PS); Valenzuela, D M (DM); DeChiara, T M (TM); Yancopoulos, G D (GD);
Affiliation: Regeneron Pharmaceuticals, Inc., Tarrytown, New York 10591, USA.
Journal and publication information
Publication Type: Journal Article
Journal: Cell (Cell), published in UNITED STATES. (Language: eng)
Reference: 1996-May; vol 85 (issue 4) : pp 513-23
Dates: Created 1996/07/26; Completed 1996/07/26; Revised 2008/11/21;
PMID: 8653787, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )
Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.
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