GPCR homo-oligomerization

https://doi.org/10.1016/j.ceb.2018.10.007Get rights and content
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G protein-coupled receptors (GPCRs) are an extensive class of trans-plasma membrane proteins that function to regulate a wide range of physiological functions. Despite a general perception that GPCRs exist as monomers an extensive literature has examined whether GPCRs can also form dimers and even higher-order oligomers, and if such organization influences various aspects of GPCR function, including cellular trafficking, ligand binding, G protein coupling and signalling. Here we focus on recent studies that employ approaches ranging from computational methods to single molecule tracking and both quantal brightness and fluorescence fluctuation measurements to assess the organization, stability and potential functional significance of dimers and oligomers within the class A, rhodopsin-like GPCR family.

Graphical abstract

Cartoon depictions of (a) Dynamic interchange between receptor monomers, (homo, orange GPCR1, and hetero, orange GPCR1 and green GPCR2) dimers and oligomers which may be ligand regulated (orange sphere). (b) Signalling cross-talk between protomers of a dimer. Left: ligand (orange sphere) binds to one protomer and the conformational change transmitted to the second protomer results in signalling through activation of a Gα subunit (blue). Right: ligand (green sphere) binding to the second protomer may modulate signalling (large or small yellow flash).

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