Research article summary (published 29 Apr 1994):

Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: a heteromeric complex related to the dystroglycans.

Full Abstract

The selective concentration of neurotransmitter receptors at the postsynaptic membrane is an essential aspect of synaptic differentiation and function. Agrin is an extracellular matrix protein that is likely to direct the accumulation of acetylcholine receptors and several other postsynaptic elements at developing and regenerating neuromuscular junctions. How agrin interacts with the membrane to bring about these changes is unknown. We now report the identification and purification of a protein complex from Torpedo electric organ postsynaptic membranes that is likely to serve as an agrin receptor. The native receptor is a heteromeric complex of two membrane glycoproteins of 190 kDa and 50 kDa. The 190 kDa subunit is sufficient to bind ligand. Peptide sequence analysis revealed that the 190 kDa and 50 kDa subunits are related to the dystrophin-associated glycoproteins alpha- and beta-dystroglycan, respectively. No other candidate agrin receptors were detected. The identification of the agrin receptor opens new avenues toward a mechanistic understanding of synapse differentiation.

Author information

Author/s: Bowe, M A (MA); Deyst, K A (KA); Leszyk, J D (JD); Fallon, J R (JR);

Affiliation: Neurobiology Group, Worcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545.

Journal and publication information

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

Journal: Neuron (Neuron), published in UNITED STATES. (Language: eng)

Reference: 1994-May; vol 12 (issue 5) : pp 1173-80

Dates: Created 1994/06/23; Completed 1994/06/23; Revised 2006/11/15;

PMID: 8185951, 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 - metabolism Amino Acid Sequence Animals Antibodies, Monoclonal Cell Membrane - metabolism Chromatography, Affinity Chromatography, Gel Cytoskeletal Proteins - chemistry Dystroglycans Dystrophin - chemistry Electric Organ - metabolism Electrophoresis, Polyacrylamide Gel Humans

Humans Immunoblotting Membrane Glycoproteins - chemistry Mice - immunology Molecular Sequence Data Molecular Weight Neurons - metabolism Peptide Fragments - chemistry; isolation & purification Peptide Mapping Receptors, Growth Factor - chemistry; isolation & purification; metabolism Sequence Homology, Amino Acid Synapses Torpedo

Associated Chemicals: Agrin (0) ; Antibodies, Monoclonal (0) ; Cytoskeletal Proteins (0) ; DAG1 protein, human (0) ; Dystrophin (0) ; Membrane Glycoproteins (0) ; Peptide Fragments (0) ; Receptors, Growth Factor (0) ; agrin receptor (0) ; Dystroglycans (146888-27-9)

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