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Related Concept Videos

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...
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...
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.
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

Updated: Jul 14, 2026

BRET-based G Protein Biosensors for Measuring G Protein-Coupled Receptor Activity in Live Cells
09:21

BRET-based G Protein Biosensors for Measuring G Protein-Coupled Receptor Activity in Live Cells

Published on: November 7, 2025

Live cell analysis of G protein beta5 complex formation, function, and targeting.

Evan A Yost1, Stacy M Mervine, Jonathan L Sabo

  • 1Weis Center for Research, Geisinger Clinic, 100 North Academy Avenue, Danville, PA 17822-2623, USA.

Molecular Pharmacology
|June 29, 2007
PubMed
Summary

G protein beta(5) subunit interactions were studied in vivo. Beta(5) preferentially binds gamma(2) and RGS7, with localization influenced by alpha subunits, suggesting functional G protein signaling complexes.

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Imaging G-protein Coupled Receptor (GPCR)-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum
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G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay
09:12

G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay

Published on: September 10, 2016

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Last Updated: Jul 14, 2026

BRET-based G Protein Biosensors for Measuring G Protein-Coupled Receptor Activity in Live Cells
09:21

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Published on: November 7, 2025

Imaging G-protein Coupled Receptor (GPCR)-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum
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G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay
09:12

G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay

Published on: September 10, 2016

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The G protein beta(5) subunit exhibits unique sequence and localization compared to other beta subunits.
  • While beta(5)gamma(2) complexes modulate effectors, beta(5) associates with RGS7 proteins in tissues.
  • Understanding beta(5) complex formation in vivo is crucial for elucidating G protein signaling pathways.

Purpose of the Study:

  • To investigate in vivo interactions of the G protein beta(5) subunit with various gamma subunits and RGS7.
  • To compare the competitive binding affinities of gamma subunits and RGS7 for beta(5).
  • To determine the impact of alpha subunits on beta(5) complex localization and function.

Main Methods:

  • Utilized multicolor bimolecular fluorescence complementation in human embryonic kidney 293 cells.
  • Assessed interactions between beta(5) and seven gamma subunits, and RGS7.
  • Observed subcellular localization of beta(5) complexes using fluorescent tagging and coexpression with alpha subunits.

Main Results:

  • Beta(5) preferentially interacted with gamma(2) over other gamma subunits and RGS7, with R7BP influencing this preference.
  • Gamma(2) showed a stronger interaction with beta(1) than beta(5).
  • Alpha subunits (alpha(o) and alpha(q)) targeted beta(5) complexes to the plasma membrane, with differential effects observed for an alpha(o) mutant.

Conclusions:

  • Beta(5) complex formation in vivo is influenced by the presence of multiple coexpressed proteins.
  • Functional beta(5)gamma(2) complexes can form in cells and mediate signaling via G protein-coupled receptors.
  • Alpha subunit interactions modulate the localization and potentially the function of beta(5) complexes.