Research article summary (published 26 May 2001):

MAGI-1c: a synaptic MAGUK interacting with muSK at the vertebrate neuromuscular junction.

Full Abstract

The muscle-specific receptor tyrosine kinase (MuSK) forms part of a receptor complex, activated by nerve-derived agrin, that orchestrates the differentiation of the neuromuscular junction (NMJ). The molecular events linking MuSK activation with postsynaptic differentiation are not fully understood. In an attempt to identify partners and/or effectors of MuSK, cross-linking and immunopurification experiments were performed in purified postsynaptic membranes from the Torpedo electrocyte, a model system for the NMJ. Matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis was conducted on both cross-link products, and on the major peptide coimmunopurified with MuSK; this analysis identified a polypeptide corresponding to the COOH-terminal fragment of membrane-associated guanylate kinase (MAGUK) with inverted domain organization (MAGI)-1c. A bona fide MAGI-1c (150 kD) was detected by Western blotting in the postsynaptic membrane of Torpedo electrocytes, and in a high molecular mass cross-link product of MuSK. Immunofluorescence experiments showed that MAGI-1c is localized specifically at the adult rat NMJ, but is absent from agrin-induced acetylcholine receptor clusters in myotubes in vitro. In the central nervous system, MAGUKs play a primary role as scaffolding proteins that organize cytoskeletal signaling complexes at excitatory synapses. Our data suggest that a protein from the MAGUK family is involved in the MuSK signaling pathway at the vertebrate NMJ.

Author information

Author/s: Strochlic, L (L); Cartaud, A (A); Labas, V (V); Hoch, W (W); Rossier, J (J); Cartaud, J (J);

Affiliation: Biologie Cellulaire des Membranes, Institut Jacques Monod, UMR 7592 CNRS, Universités Paris 6 et Paris 7, 75251 Paris, France.

Journal and publication information

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

Journal: The Journal of cell biology (J Cell Biol), published in United States. (Language: eng)

Reference: 2001-May; vol 153 (issue 5) : pp 1127-32

Dates: Created 2001/05/30; Completed 2001/06/28; Revised 2008/11/20;

PMID: 11381096, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: 18 Feb 2009 00:00:00)

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.

Agrin - metabolism Animals Cell Membrane - enzymology; metabolism Cross-Linking Reagents - metabolism Fluorescent Antibody Technique, Indirect Guanylate Kinase Molecular Weight Neuromuscular Junction - cytology; enzymology; metabolism Nucleoside-Phosphate Kinase - chemistry; metabolism Protein Binding

Protein Binding Protein Isoforms - chemistry; metabolism Protein Structure, Tertiary Rats Receptor Protein-Tyrosine Kinases - chemistry; metabolism Receptors, Cholinergic - metabolism Signal Transduction Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Synapses - enzymology; metabolism Torpedo - metabolism

Associated Chemicals: Agrin (0) ; Cross-Linking Reagents (0) ; Protein Isoforms (0) ; Receptors, Cholinergic (0) ; Receptor Protein-Tyrosine Kinases (EC 2.7.1.112) ; MUSK protein, human (EC 2.7.10.1) ; Nucleoside-Phosphate Kinase (EC 2.7.4.4) ; Guanylate Kinase (EC 2.7.4.8)

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