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Monomeric G-Protein-Coupled Receptor as a Functional Unit

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Institut de Pharmacologie Moleculaire et Cellulaire, CNRS and Université de Nice-Sophia-Antipolis, 06560 Valbonne, France, and Département de Biologie Joliot-Curie, CNRS, Université Paris XI and CEA Saclay, 91191 Gif sur Yvette, France
Cite this: Biochemistry 2005, 44, 27, 9395–9403
Publication Date (Web):June 18, 2005
https://doi.org/10.1021/bi050720o
Copyright © 2005 American Chemical Society
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    Abstract

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    Rhodopsin, the first purified G-protein-coupled receptor (GPCR), was characterized as a functional monomer 30 year ago, but dimerization of GPCRs recently became the new paradigm of signal transduction. It has even been claimed, on the basis of recent biophysical and biochemical studies, that this new concept could be extended to higher-order oligomerization. Here this view is challenged. The new studies of rhodopsin and other simple (class 1a) GPCRs solubilized in detergent are re-assessed and are compared to the earlier classical studies of rhodopsin and other membrane proteins solubilized in detergent. The new studies are found to strengthen rather than invalidate the conclusions of the early ones and to support a monomeric model for rhodopsin and other class 1a GPCRs. A molecular model is proposed for the functional coupling of a rhodopsin monomeric unit with a G-protein heterotrimer. This model should be valid even for GPCRs that exist as structural dimers.

    *

     To whom correspondence should be addressed:  CNRS/IPMC, 660 route des lucioles, Sophia-Antipolis, 06560 Valbonne, France. Phone:  33 493957775. Fax:  33 493957710. E-mail:  [email protected].

    ‡

     CNRS and Université de Nice-Sophia-Antipolis.

    §

     Université Paris XI and CEA Saclay.

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