Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

8.0K
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...
8.0K
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

125.1K
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.
125.1K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

14.1K
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...
14.1K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.1K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.1K
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

2.9K
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,...
2.9K
Rab Proteins01:14

Rab Proteins

4.3K
Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
4.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Cannabinoid and adenosine A<sub>2A</sub> receptor crosstalk regulates postnatal and adult hippocampal neurogenesis.

British journal of pharmacology·2026
Same author

Dopaminergic hypersensitivity of the opioid-responsive striatal-entopeduncular pathway in a rodent model of restless legs syndrome.

Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology·2026
Same author

Ion Channel Nano-Diagnostics for ER+ Breast Cancer.

bioRxiv : the preprint server for biology·2026
Same author

P2Y<sub>14</sub> receptor in the nervous system: Pharmacology, mechanisms, and therapeutic potential.

Pharmacology & therapeutics·2026
Same author

Allosteric coupling between PIP<sub>2</sub> and Ca<sup>2+</sup> binding sites gates TMEM16A channels.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Oligomerization of transmembrane adenylyl cyclase isoforms.

Molecular pharmacology·2026

Related Experiment Video

Updated: Oct 21, 2025

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

3.4K

G protein-coupled receptor-effector macromolecular membrane assemblies (GEMMAs).

Sergi Ferré1, Francisco Ciruela2, Carmen W Dessauer3

  • 1Integrative Neurobiology Section, National Institute on Drug Addiction, Intramural Research Program, NIH, DHHS, Baltimore, MD, USA.

Pharmacology & Therapeutics
|September 4, 2021
PubMed
Summary

G protein-coupled receptors (GPCRs) form pre-assembled complexes called GEMMAs, challenging the traditional collision-coupling model. This new understanding of GPCR signaling assemblies offers novel therapeutic targets.

Keywords:
G protein subnitsG protein-coupled receptorsGPCR allosterismGPCR oligomerizationPlasma membrane effector

More Related Videos

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
07:41

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

9.1K
Construction of Model Lipid Membranes Incorporating G-protein Coupled Receptors GPCRs
09:45

Construction of Model Lipid Membranes Incorporating G-protein Coupled Receptors GPCRs

Published on: February 5, 2022

3.7K

Related Experiment Videos

Last Updated: Oct 21, 2025

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

3.4K
A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
07:41

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

9.1K
Construction of Model Lipid Membranes Incorporating G-protein Coupled Receptors GPCRs
09:45

Construction of Model Lipid Membranes Incorporating G-protein Coupled Receptors GPCRs

Published on: February 5, 2022

3.7K

Area of Science:

  • Cellular Biology
  • Molecular Pharmacology
  • Biochemistry

Background:

  • G protein-coupled receptors (GPCRs) are crucial for cellular signaling and are major drug targets.
  • The canonical GPCR signaling model involves freely mobile components interacting via 'collision coupling'.

Purpose of the Study:

  • To present evidence for GPCR-effector macromolecular membrane assemblies (GEMMAs).
  • To propose GEMMAs as an alternative/complementary model to collision coupling for GPCR signaling.
  • To explore the pharmacological potential of GEMMAs for therapeutic interventions.

Main Methods:

  • Synthesis of existing evidence supporting the GEMMA model.
  • Analysis of GPCR oligomerization and interactions with associated proteins.
  • Exploration of pharmacological characteristics of GEMMAs.

Main Results:

  • GPCRs, G proteins, and effectors can form pre-assembled macromolecular complexes (GEMMAs).
  • GEMMAs undergo rearrangements upon agonist activation.
  • Both collision-coupling and pre-assembled GEMMA mechanisms likely coexist, explaining diverse GPCR signaling.

Conclusions:

  • The GEMMA model provides a framework for understanding efficient and specific GPCR signaling.
  • GEMMAs offer unique pharmacological properties for targeted drug development.
  • Modulating individual GEMMAs presents new therapeutic opportunities for GPCR-related diseases.