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Research article summary (published 30 Oct 2005):

The synaptic muscle-specific kinase (MuSK) complex: new partners, new functions.

Full Abstract

The muscle-specific kinase MuSK is part of an agrin receptor complex that stimulates tyrosine phosphorylation and drives clustering of acetylcholine receptors (AChRs) in the postsynaptic membrane at the vertebrate neuromuscular junction (NMJ). MuSK also regulates synaptic gene transcription in subsynaptic nuclei. Over the past few years, decisive progress has been made in the identification of MuSK effectors, helping to understand its function in the formation of the NMJ. Similarly to AChR, MuSK and several of its partners are the target of mutations responsible for diseases of the NMJ, such as congenital myasthenic syndromes. This minireview will focus on the multiple MuSK effectors so far identified that place MuSK at the center of a multifunctional signaling complex involved in the organization of the NMJ and associated disorders. Copyright (c) 2005 Wiley Periodicals, Inc.

 

Author information

Author/s: Strochlic, Laure (L); Cartaud, Annie (A); Cartaud, Jean (J);

Affiliation: Biologie Cellulaire des Membranes, Institut Jacques Monod, Paris, France.

Journal and publication information

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

Journal: BioEssays : news and reviews in molecular, cellular and developmental biology (Bioessays), published in United States. (Language: eng)

Reference: 2005-Nov; vol 27 (issue 11) : pp 1129-35

Dates: Created 2005/10/25; Completed 2006/11/29;

PMID: 16237673, 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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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Associated Chemicals: Receptors, Cholinergic (0) ; Phosphotyrosine (21820-51-9) ; Receptor Protein-Tyrosine Kinases (EC 2.7.1.112)

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