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Molecular Pharmacology Fast Forward
First published on August 19, 2004; DOI: 10.1124/mol.104.006320


0026-895X/04/6605-1077-1082$20.00
Mol Pharmacol 66:1077-1082, 2004

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Perspective

The Ants Go Marching Two by Two: Oligomeric Structure of G-Protein-Coupled Receptors

Jonathan A. Javitch

Center for Molecular Recognition, Departments of Psychiatry and Pharmacology, Columbia University College of Physicians and Surgeons, New York, New York

A number of class C G-protein coupled receptors (GPCRs) have been shown to form dimers in the plasma membrane, and mounting evidence supports the hypothesis that many, if not all, class A rhodopsin-like receptors also form dimers or higher-order oligomers. Evidence for this hypothesis has come from SDS-polyacrylamide gel electrophoresis, coimmunoprecipitation, resonance energy transfer, atomic force microscopy, and cross-linking studies, approaches that are reviewed in this article. Like any method, each has its strengths and limitations, and these must be kept in mind when interpreting the data for oligomerization. Recent experimental evidence supports the hypothesis that class A receptors may exist as higher-order oligomers, or even as arrays, with distinct symmetrical interfaces in both the first and fourth transmembrane segments.


Received August 9, 2004; accepted August 18, 2004

Address correspondence to: Dr. Jonathan A. Javitch, Center for Molecular Recognition, Columbia University, P&S 11-401, 630 W. 168th Street, New York, NY 10032. E-mail: jaj2{at}columbia.edu




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