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GPCR homo-oligomerization

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 h...

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Detalles Bibliográficos
Autores principales: Milligan, Graeme, Ward, Richard J, Marsango, Sara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7083226/
https://www.ncbi.nlm.nih.gov/pubmed/30453145
http://dx.doi.org/10.1016/j.ceb.2018.10.007
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author Milligan, Graeme
Ward, Richard J
Marsango, Sara
author_facet Milligan, Graeme
Ward, Richard J
Marsango, Sara
author_sort Milligan, Graeme
collection PubMed
description 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.
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spelling pubmed-70832262020-03-24 GPCR homo-oligomerization Milligan, Graeme Ward, Richard J Marsango, Sara Curr Opin Cell Biol Article 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. Elsevier 2019-04 /pmc/articles/PMC7083226/ /pubmed/30453145 http://dx.doi.org/10.1016/j.ceb.2018.10.007 Text en © 2018 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Milligan, Graeme
Ward, Richard J
Marsango, Sara
GPCR homo-oligomerization
title GPCR homo-oligomerization
title_full GPCR homo-oligomerization
title_fullStr GPCR homo-oligomerization
title_full_unstemmed GPCR homo-oligomerization
title_short GPCR homo-oligomerization
title_sort gpcr homo-oligomerization
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7083226/
https://www.ncbi.nlm.nih.gov/pubmed/30453145
http://dx.doi.org/10.1016/j.ceb.2018.10.007
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