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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2019
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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. |
format | Online Article Text |
id | pubmed-7083226 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT milligangraeme gpcrhomooligomerization AT wardrichardj gpcrhomooligomerization AT marsangosara gpcrhomooligomerization |