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Related Concept Videos

G-protein Coupled Receptors01:21

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical, 7TM, or...

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Related Experiment Video

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function.

Stephane Angers1, Ali Salahpour, Michel Bouvier

  • 1Department of Biochemistry and Groupe de Recherche sur le Système Nerveux Autonome, Université de Montréal, Montréal, H3C 3J7, Canada. stephane.angers@umontreal.ca

Annual Review of Pharmacology and Toxicology
|January 25, 2002
PubMed
Summary

G protein-coupled receptors (GPCRs) are now understood to form dimers and oligomers, challenging the monomeric view. This discovery impacts receptor function, biogenesis, and drug development strategies.

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Last Updated: Jul 12, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay
11:49

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay

Published on: July 28, 2014

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
10:59

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Published on: August 17, 2022

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Traditionally, G protein-coupled receptors (GPCRs) were viewed as monomeric proteins.
  • Recent studies challenge this paradigm, suggesting GPCRs exist as dimers or oligomers.
  • This oligomerization is increasingly supported by biophysical evidence in living cells.

Purpose of the Study:

  • To review the emerging evidence for GPCR oligomerization.
  • To discuss the potential roles of GPCR dimerization in receptor biogenesis and function.
  • To explore the implications of GPCR homo- and heterodimerization for pharmacology and drug discovery.

Main Methods:

  • Biophysical techniques, including luminescence and fluorescence energy transfer (FRET).
  • Observation of oligomeric complexes in living cells.
  • Analysis of existing literature on GPCR structure and function.

Main Results:

  • Confirmation of GPCR oligomeric complexes in living cells using advanced biophysical methods.
  • Evidence for both constitutive dimerization during biosynthesis and ligand-promoted dimerization at the cell surface.
  • Identification of receptor subtype heterodimerization, adding complexity to GPCR signaling.

Conclusions:

  • GPCRs likely function as dimers or oligomers, not just monomers.
  • Receptor dimerization plays roles in GPCR biogenesis, cell surface function, and signaling complexity.
  • Understanding GPCR oligomerization is crucial for advancing drug development and screening.