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

Rab Proteins01:14

Rab Proteins

5.5K
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...
5.5K
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

134.6K
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.
134.6K
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

7.2K
7.2K
Rab Cascades01:25

Rab Cascades

3.8K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
3.8K
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

8.6K
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,...
8.6K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

12.6K
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...
12.6K

You might also read

Related Articles

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

Sort by
Same author

A prefrontal cortex-lateral hypothalamus circuit controls stress-driven increased food intake.

Nature communications·2026
Same author

Longitudinal analysis of arterial pressure and its impact on outcomes in patients with thrombotic thrombocytopenic purpura.

Intensive care medicine·2025
Same author

Uneasiness in interdisciplinary research and the importance of metaphors: A case story on building an interdisciplinary chronic pain research team.

PEC innovation·2024
Same author

Cytomegalovirus infection in intensive care unit patients with hematological malignancies: Characteristics and clinical outcomes.

Journal of critical care·2024
Same author

Validation of an LC-MS/MS method for the quantification IOA-289 in human plasma and its application in a first-in-human clinical trial.

Journal of pharmaceutical and biomedical analysis·2022
Same author

Herpesvirus reactivation during severe COVID-19 and high rate of immune defect.

Infectious diseases now·2021

Related Experiment Video

Updated: Apr 11, 2026

Using an α-Bungarotoxin Binding Site Tag to Study GABA A Receptor Membrane Localization and Trafficking
11:57

Using an α-Bungarotoxin Binding Site Tag to Study GABA A Receptor Membrane Localization and Trafficking

Published on: March 28, 2014

16.4K

GABAB receptor cell-surface export is controlled by an endoplasmic reticulum gatekeeper.

S Doly1,2,3, H Shirvani1,2,3, G Gäta1,2,3,4

  • 1INSERM, U1016, Institut Cochin, Paris, France.

Molecular Psychiatry
|June 3, 2015
PubMed
Summary

A novel ER gatekeeper, PRAF2, controls the cell-surface expression of gamma-aminobutyric acid (GABA)B receptors. Modulating PRAF2 impacts GABAB function and may offer therapeutic potential for neurological disorders.

More Related Videos

Inhibitory Synapse Formation in a Co-culture Model Incorporating GABAergic Medium Spiny Neurons and HEK293 Cells Stably Expressing GABAA Receptors
07:51

Inhibitory Synapse Formation in a Co-culture Model Incorporating GABAergic Medium Spiny Neurons and HEK293 Cells Stably Expressing GABAA Receptors

Published on: November 14, 2014

18.0K
Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission
07:16

Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission

Published on: August 16, 2018

14.4K

Related Experiment Videos

Last Updated: Apr 11, 2026

Using an α-Bungarotoxin Binding Site Tag to Study GABA A Receptor Membrane Localization and Trafficking
11:57

Using an α-Bungarotoxin Binding Site Tag to Study GABA A Receptor Membrane Localization and Trafficking

Published on: March 28, 2014

16.4K
Inhibitory Synapse Formation in a Co-culture Model Incorporating GABAergic Medium Spiny Neurons and HEK293 Cells Stably Expressing GABAA Receptors
07:51

Inhibitory Synapse Formation in a Co-culture Model Incorporating GABAergic Medium Spiny Neurons and HEK293 Cells Stably Expressing GABAA Receptors

Published on: November 14, 2014

18.0K
Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission
07:16

Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission

Published on: August 16, 2018

14.4K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Cell-surface export of G protein-coupled receptors (GPCRs), including gamma-aminobutyric acid (GABA)B receptors, is tightly regulated.
  • The ligand-binding GB1 subunit of GABA-B receptors is retained in the endoplasmic reticulum (ER) until it heterodimerizes with the GB2 subunit.

Purpose of the Study:

  • To identify the mechanisms regulating GABA-B receptor GB1 subunit retention in the ER.
  • To investigate the role of specific ER-resident proteins in controlling GABA-B receptor cell-surface expression and function.

Main Methods:

  • Co-immunoprecipitation assays to study protein interactions.
  • Cell surface biotinylation and Western blotting to assess receptor trafficking.
  • In vivo studies in mice to evaluate the physiological impact of PRAF2 manipulation.

Main Results:

  • PRAF2, an ER-resident transmembrane protein, directly binds to the GB1 subunit, retaining it in the ER.
  • GB1 release from PRAF2 occurs upon binding of the GB2 subunit, enabling receptor maturation and export.
  • Altering PRAF2 levels in vivo significantly impacts GABA-B receptor function and leads to hyperactivity in mice.

Conclusions:

  • PRAF2 acts as a critical gatekeeper controlling GABA-B receptor cell-surface expression.
  • PRAF2 levels precisely regulate neuronal GABA-B receptor function.
  • PRAF2 represents a potential therapeutic target for psychiatric and neurological diseases associated with GABA-B signaling dysfunction.