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Serotonin Type 4 Receptor Dimers

Numerous class A G protein-coupled receptors and especially biogenic amine receptors have been reported to form homodimers. Indeed, the dimerization process might occur for all the metabotropic serotonergic receptors. Moreover, dimerization appears to be essential for the function of serotonin type... Full description

Journal Title: Methods in Cell Biology 2013, Vol.117, p.123-139
Main Author: Claeysen, Sylvie
Other Authors: Donneger, Romain , Giannoni, Patrizia , Gaven, Florence , Pellissier, Lucie P
Format: Electronic Article Electronic Article
Language: English
Subjects:
Publisher: United States: Elsevier Science & Technology
ID: ISSN: 0091-679X
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recordid: cdi_hal_primary_oai_HAL_hal_01792387v1
title: Serotonin Type 4 Receptor Dimers
format: Article
creator:
  • Claeysen, Sylvie
  • Donneger, Romain
  • Giannoni, Patrizia
  • Gaven, Florence
  • Pellissier, Lucie P
subjects:
  • Animals
  • Biochemistry
  • Biochemistry, Molecular Biology
  • Blotting, Western
  • Cell Membrane - chemistry
  • Cell Membrane - metabolism
  • Cercopithecus aethiops
  • Cognition
  • Cognitive science
  • COS Cells
  • Dimer visualization
  • Dimerization
  • Fluorescence Resonance Energy Transfer
  • Gene Expression
  • GPCR
  • HEK293 Cells
  • Humans
  • Immunoprecipitation
  • Life Sciences
  • Ligands
  • Mice
  • Molecular Biology
  • Molecular Imaging - methods
  • Mutation
  • Neurobiology
  • Neurons
  • Neurons and Cognition
  • Neuroscience
  • Oligomerization
  • Protein Multimerization
  • Receptors, Serotonin, 5-HT4 - chemistry
  • Receptors, Serotonin, 5-HT4 - genetics
  • Receptors, Serotonin, 5-HT4 - metabolism
  • Recombinant Proteins - chemistry
  • Recombinant Proteins - genetics
  • Recombinant Proteins - metabolism
  • Serotonin receptor
ispartof: Methods in Cell Biology, 2013, Vol.117, p.123-139
description: Numerous class A G protein-coupled receptors and especially biogenic amine receptors have been reported to form homodimers. Indeed, the dimerization process might occur for all the metabotropic serotonergic receptors. Moreover, dimerization appears to be essential for the function of serotonin type 2C (5-HT2C) and type 4 (5-HT4) receptors and required to obtain full receptor activity. Several techniques have been developed to analyze dimer formation and properties. Due to our involvement in deciphering 5-HT4R transduction mechanisms, we improved and set up new procedures to study 5-HT4R dimers, by classical methods or modern tools. This chapter presents detailed protocols to detect 5-HT4R dimers by Western blotting and coimmunoprecipitation, including the optimizations that we routinely carry out. We developed an innovative method to achieve functional visualization of 5-HT4R dimers by immunofluorescence, taking advantage of the 5-HT4-RASSL (receptor activated solely by synthetic ligand) mutant that was engineered in the laboratory. Finally, we adapted the powerful time-resolved FRET technology to assess a relative quantification of dimer formation and affinity.
language: eng
source:
identifier: ISSN: 0091-679X
fulltext: no_fulltext
issn:
  • 0091-679X
url: Link


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creatorClaeysen, Sylvie ; Donneger, Romain ; Giannoni, Patrizia ; Gaven, Florence ; Pellissier, Lucie P
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descriptionNumerous class A G protein-coupled receptors and especially biogenic amine receptors have been reported to form homodimers. Indeed, the dimerization process might occur for all the metabotropic serotonergic receptors. Moreover, dimerization appears to be essential for the function of serotonin type 2C (5-HT2C) and type 4 (5-HT4) receptors and required to obtain full receptor activity. Several techniques have been developed to analyze dimer formation and properties. Due to our involvement in deciphering 5-HT4R transduction mechanisms, we improved and set up new procedures to study 5-HT4R dimers, by classical methods or modern tools. This chapter presents detailed protocols to detect 5-HT4R dimers by Western blotting and coimmunoprecipitation, including the optimizations that we routinely carry out. We developed an innovative method to achieve functional visualization of 5-HT4R dimers by immunofluorescence, taking advantage of the 5-HT4-RASSL (receptor activated solely by synthetic ligand) mutant that was engineered in the laboratory. Finally, we adapted the powerful time-resolved FRET technology to assess a relative quantification of dimer formation and affinity.
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languageeng
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subjectAnimals ; Biochemistry ; Biochemistry, Molecular Biology ; Blotting, Western ; Cell Membrane - chemistry ; Cell Membrane - metabolism ; Cercopithecus aethiops ; Cognition ; Cognitive science ; COS Cells ; Dimer visualization ; Dimerization ; Fluorescence Resonance Energy Transfer ; Gene Expression ; GPCR ; HEK293 Cells ; Humans ; Immunoprecipitation ; Life Sciences ; Ligands ; Mice ; Molecular Biology ; Molecular Imaging - methods ; Mutation ; Neurobiology ; Neurons ; Neurons and Cognition ; Neuroscience ; Oligomerization ; Protein Multimerization ; Receptors, Serotonin, 5-HT4 - chemistry ; Receptors, Serotonin, 5-HT4 - genetics ; Receptors, Serotonin, 5-HT4 - metabolism ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Serotonin receptor
ispartofMethods in Cell Biology, 2013, Vol.117, p.123-139
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descriptionNumerous class A G protein-coupled receptors and especially biogenic amine receptors have been reported to form homodimers. Indeed, the dimerization process might occur for all the metabotropic serotonergic receptors. Moreover, dimerization appears to be essential for the function of serotonin type 2C (5-HT2C) and type 4 (5-HT4) receptors and required to obtain full receptor activity. Several techniques have been developed to analyze dimer formation and properties. Due to our involvement in deciphering 5-HT4R transduction mechanisms, we improved and set up new procedures to study 5-HT4R dimers, by classical methods or modern tools. This chapter presents detailed protocols to detect 5-HT4R dimers by Western blotting and coimmunoprecipitation, including the optimizations that we routinely carry out. We developed an innovative method to achieve functional visualization of 5-HT4R dimers by immunofluorescence, taking advantage of the 5-HT4-RASSL (receptor activated solely by synthetic ligand) mutant that was engineered in the laboratory. Finally, we adapted the powerful time-resolved FRET technology to assess a relative quantification of dimer formation and affinity.
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1Biochemistry
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4Cell Membrane - chemistry
5Cell Membrane - metabolism
6Cercopithecus aethiops
7Cognition
8Cognitive science
9COS Cells
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11Dimerization
12Fluorescence Resonance Energy Transfer
13Gene Expression
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16Humans
17Immunoprecipitation
18Life Sciences
19Ligands
20Mice
21Molecular Biology
22Molecular Imaging - methods
23Mutation
24Neurobiology
25Neurons
26Neurons and Cognition
27Neuroscience
28Oligomerization
29Protein Multimerization
30Receptors, Serotonin, 5-HT4 - chemistry
31Receptors, Serotonin, 5-HT4 - genetics
32Receptors, Serotonin, 5-HT4 - metabolism
33Recombinant Proteins - chemistry
34Recombinant Proteins - genetics
35Recombinant Proteins - metabolism
36Serotonin receptor
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32Receptors, Serotonin, 5-HT4 - metabolism
33Recombinant Proteins - chemistry
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35Recombinant Proteins - metabolism
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abstractNumerous class A G protein-coupled receptors and especially biogenic amine receptors have been reported to form homodimers. Indeed, the dimerization process might occur for all the metabotropic serotonergic receptors. Moreover, dimerization appears to be essential for the function of serotonin type 2C (5-HT2C) and type 4 (5-HT4) receptors and required to obtain full receptor activity. Several techniques have been developed to analyze dimer formation and properties. Due to our involvement in deciphering 5-HT4R transduction mechanisms, we improved and set up new procedures to study 5-HT4R dimers, by classical methods or modern tools. This chapter presents detailed protocols to detect 5-HT4R dimers by Western blotting and coimmunoprecipitation, including the optimizations that we routinely carry out. We developed an innovative method to achieve functional visualization of 5-HT4R dimers by immunofluorescence, taking advantage of the 5-HT4-RASSL (receptor activated solely by synthetic ligand) mutant that was engineered in the laboratory. Finally, we adapted the powerful time-resolved FRET technology to assess a relative quantification of dimer formation and affinity.
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