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Issue 6, 2004
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A concept for G proteinactivation by G protein-coupled receptor dimers: the transducin/rhodopsin interface

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Abstract

G protein-coupled receptors (GPCRs) are ubiquitous and essential in modulating virtually all physiological processes. These receptors share a similar structural design consisting of the seven-transmembrane α-helical segments. The active conformations of the receptors are stabilized by an agonist and couple to structurally highly conserved heterotrimeric G proteins. One of the most important unanswered questions is how GPCRs couple to their cognate G proteins. Phototransduction represents an excellent model system for understanding G protein signaling, owing to the high expression of rhodopsin in rod photoreceptors and the multidisciplinary experimental approaches used to study this GPCR. Here, we describe how a G protein (transducin) docks on to an oligomeric GPCR (rhodopsin), revealing structural details of this critical interface in the signal transduction process. This conceptual model takes into account recent structural information on the receptor and G protein, as well as oligomeric states of GPCRs.

Graphical abstract: A concept for G protein activation by G protein-coupled receptor dimers: the transducin/rhodopsin interface

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Article information


Submitted
04 Dec 2003
Accepted
04 Feb 2004
First published
27 Feb 2004

Photochem. Photobiol. Sci., 2004,3, 628-638
Article type
Paper

A concept for G protein activation by G protein-coupled receptor dimers: the transducin/rhodopsin interface

S. Filipek, K. A. Krzysko, D. Fotiadis, Y. Liang, D. A. Saperstein, A. Engel and K. Palczewski, Photochem. Photobiol. Sci., 2004, 3, 628
DOI: 10.1039/B315661C

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