Research article summary (published 30 Jan 2002):

Clustering of nicotinic acetylcholine receptors: from the neuromuscular junction to interneuronal synapses.

Full Abstract

Fast and accurate synaptic transmission requires high-density accumulation of neurotransmitter receptors in the postsynaptic membrane. During development of the neuromuscular junction, clustering of acetylcholine receptors (AChR) is one of the first signs of postsynaptic specialization and is induced by nerve-released agrin. Recent studies have revealed that different mechanisms regulate assembly vs stabilization of AChR clusters and of the postsynaptic apparatus. MuSK, a receptor tyrosine kinase and component of the agrin receptor, and rapsyn, an AChR-associated anchoring protein, play crucial roles in the postsynaptic assembly. Once formed, AChR clusters and the postsynaptic membrane are stabilized by components of the dystrophin/utrophin glycoprotein complex, some of which also direct aspects of synaptic maturation such as formation of postjunctional folds. Nicotinic receptors are also expressed across the peripheral and central nervous system (PNS/CNS). These receptors are localized not only at the pre- but also at the postsynaptic sites where they carry out major synaptic transmission. In neurons, they are found as clusters at synaptic or extrasynaptic sites, suggesting that different mechanisms might underlie this specific localization of nicotinic receptors. This review summarizes the current knowledge about formation and stabilization of the postsynaptic apparatus at the neuromuscular junction and extends this to explore the synaptic structures of interneuronal cholinergic synapses.

Author information

Author/s: Huh, Kyung-Hye (KH); Fuhrer, Christian (C);

Affiliation: Department of Neurochemistry, Brain Research Institute, University of Zürich, Switzerland.

Journal and publication information

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

Journal: Molecular neurobiology (Mol Neurobiol), published in United States. (Language: eng)

Reference: 2002-Feb; vol 25 (issue 1) : pp 79-112

Dates: Created 2002/03/13; Completed 2003/05/01; Revised 2006/11/15;

PMID: 11890459, 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.

Agrin - secretion Animals Cholinergic Fibers - physiology Cytoskeletal Proteins - physiology Dystrophin - physiology Humans Interneurons Laminin - physiology Macromolecular Substances Membrane Proteins - physiology Mice Mice, Neurologic Mutants Models, Neurological Muscle Proteins - physiology

Muscle Proteins - physiology Nerve Tissue Proteins - analysis; chemistry; physiology Neuromuscular Junction - physiology; ultrastructure Neurons - physiology Oligosaccharides - physiology Receptor Protein-Tyrosine Kinases - physiology Receptors, Cholinergic - physiology Receptors, Growth Factor - physiology Receptors, Nicotinic - analysis; chemistry; physiology Signal Transduction Synapses - physiology; ultrastructure Synaptic Transmission Utrophin src-Family Kinases - physiology

Associated Chemicals: Agrin (0) ; Cytoskeletal Proteins (0) ; Dystrophin (0) ; Laminin (0) ; Macromolecular Substances (0) ; Membrane Proteins (0) ; Muscle Proteins (0) ; Nerve Tissue Proteins (0) ; Oligosaccharides (0) ; Receptors, Cholinergic (0) ; Receptors, Growth Factor (0) ; Receptors, Nicotinic (0) ; Utrn protein, mouse (0) ; Utrophin (0) ; agrin receptor (0) ; peripheral membrane protein 43K (0) ; Receptor Protein-Tyrosine Kinases (EC 2.7.1.112) ; src-Family Kinases (EC 2.7.1.112) ; MUSK protein, human (EC 2.7.10.1)

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