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A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors

There is accumulating evidence that membrane-bound receptors interact with many intracellular proteins. Multiprotein complexes associated with ionotropic receptors have been extensively characterized, but the identification of proteins interacting with G protein-coupled receptors (GPCRs) has so far...

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Detalles Bibliográficos
Autores principales: Bécamel, Carine, Galéotti, Nathalie, Poncet, Joël, Jouin, Patrick, Dumuis, Aline, Bockaert, Joël, Marin, Philippe
Formato: Texto
Lenguaje:English
Publicado: Biological Procedures Online 2002
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC145562/
https://www.ncbi.nlm.nih.gov/pubmed/12734563
http://dx.doi.org/10.1251/bpo39
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author Bécamel, Carine
Galéotti, Nathalie
Poncet, Joël
Jouin, Patrick
Dumuis, Aline
Bockaert, Joël
Marin, Philippe
author_facet Bécamel, Carine
Galéotti, Nathalie
Poncet, Joël
Jouin, Patrick
Dumuis, Aline
Bockaert, Joël
Marin, Philippe
author_sort Bécamel, Carine
collection PubMed
description There is accumulating evidence that membrane-bound receptors interact with many intracellular proteins. Multiprotein complexes associated with ionotropic receptors have been extensively characterized, but the identification of proteins interacting with G protein-coupled receptors (GPCRs) has so far only been achieved in a piecemeal fashion, focusing on one or two protein species. We describe a method based on peptide affinity chromatography, two-dimensional electrophoresis, mass spectrometry and immunoblotting to identify the components of multiprotein complexes interacting directly or indirectly with intracellular domains of GPCRs or, more generally, any other membrane-bound receptor. Using this global approach, we have characterized multiprotein complexes that bind to the carboxy-terminal tail of the 5-hydroxytryptamine type 2C receptor and are important for its subcellular localization in CNS cells (Bécamel et al., EMBO J., 21(10): 2332, 2002).
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spelling pubmed-1455622003-04-15 A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors Bécamel, Carine Galéotti, Nathalie Poncet, Joël Jouin, Patrick Dumuis, Aline Bockaert, Joël Marin, Philippe Biol Proced Online Research Article There is accumulating evidence that membrane-bound receptors interact with many intracellular proteins. Multiprotein complexes associated with ionotropic receptors have been extensively characterized, but the identification of proteins interacting with G protein-coupled receptors (GPCRs) has so far only been achieved in a piecemeal fashion, focusing on one or two protein species. We describe a method based on peptide affinity chromatography, two-dimensional electrophoresis, mass spectrometry and immunoblotting to identify the components of multiprotein complexes interacting directly or indirectly with intracellular domains of GPCRs or, more generally, any other membrane-bound receptor. Using this global approach, we have characterized multiprotein complexes that bind to the carboxy-terminal tail of the 5-hydroxytryptamine type 2C receptor and are important for its subcellular localization in CNS cells (Bécamel et al., EMBO J., 21(10): 2332, 2002). Biological Procedures Online 2002-12-09 /pmc/articles/PMC145562/ /pubmed/12734563 http://dx.doi.org/10.1251/bpo39 Text en Copyright © December 12, 2002, C Bécamel et al. Published in Biological Procedures Online under license from the authors. Copying, printing, redistribution and storage permitted.
spellingShingle Research Article
Bécamel, Carine
Galéotti, Nathalie
Poncet, Joël
Jouin, Patrick
Dumuis, Aline
Bockaert, Joël
Marin, Philippe
A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors
title A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors
title_full A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors
title_fullStr A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors
title_full_unstemmed A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors
title_short A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors
title_sort proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC145562/
https://www.ncbi.nlm.nih.gov/pubmed/12734563
http://dx.doi.org/10.1251/bpo39
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