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A division of labor: asymmetric roles for GPCR subunits in receptor dimers

Nature Chemical Biology volume 5, pages 608–609 (2009)Cite this article

The functional architecture of dimeric or oligomeric GPCR signaling remains incompletely understood. Using a clever combination of receptor–G protein fusions and various receptor mutations, new research provides a glimpse into how oligomers might be arranged with respect to the G proteins they interact with.

The functional consequences of G protein–coupled receptor (GPCR) homo- and hetero-oligomerization, while broadly accepted as a structural feature of many such receptors, have been difficult to understand at the molecular level. It is clear that some GPCRs, such as the GABA-B receptor, function mainly as obligate heterodimers, where one subunit is responsible for membrane targeting and the other for ligand binding1,2. It is also clear that GPCRs can productively interact with G proteins as monomers, although so far this has only been shown in artificial environments3,4. There has been a longstanding need for a system to evaluate the functional necessity for either homo- or hetero-oligomerization of receptors. Now the successful development of such a system provides an increased understanding of the asymmetric function of receptor equivalents in a GPCR oligomer with respect to G protein coupling5.

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Figure 1: Asymmetry of receptor subunits in dimeric GPCRs.

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  1. Peter Zylbergold and Terence E. Hébert are in the Department of Pharmacology and Therapeutics, McGill University, Montreal, Canada.,

    Peter Zylbergold & Terence E Hébert

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  1. Peter Zylbergold
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  2. Terence E Hébert
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Correspondence to Terence E Hébert.

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Zylbergold, P., Hébert, T. A division of labor: asymmetric roles for GPCR subunits in receptor dimers. Nat Chem Biol 5, 608–609 (2009). https://doi.org/10.1038/nchembio0909-608

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