Signaling complexes for postsynaptic differentiation.

Full Abstract

The receptor tyrosine kinase MuSK is activated by agrin, an extracellular matrix protein believed to be utilized by motoneurons to regulate the formation or maintenance of the neuromuscular junction (NMJ). Recent studies have shed light on intracellular signaling mechanisms downstream of MuSK. Agrin enhances the activity of Rho GTPases and PAK, which is required for AChR clustering. Activation of these enzymes requires not only the kinase activity of MuSK, but also its interaction with proteins such as Dishevelled. These results suggest that MuSK may function as a scaffold tyrosine kinase that forms a multi-molecule complex for AChR clustering.

Author information

Author/s: Luo, Zhenge (Z); Wang, Qiang (Q); Dobbins, G Clement (GC); Levy, Shoshanah (S); Xiong, Wen C (WC); Mei, Lin (L);

Affiliation: Departments of Neurobiology, Pathology, and Physical Medicine and Rehabilitation, Civitan International Research Center, University of Alabama at Birmingham, Birmingham, AL 35294, USA.

Grants: AR 48120 (Agency:NIAMS NIH HHS) ; GM 63861 (Agency:NIGMS NIH HHS) ; NS 40480 (Agency:NINDS NIH HHS) ; NS 44521 (Agency:NINDS NIH HHS) ; NS 46848 (Agency:NINDS NIH HHS)

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review

Journal: Journal of neurocytology (J Neurocytol), published in United States. (Language: eng)

Reference: -2003 Jun-Sep; vol 32 (issue 5-8) : pp 697-708

Dates: Created 2004/03/22; Completed 2004/07/02; Revised 2007/11/14;

PMID: 15034262, 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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