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

Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

3.7K
Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
3.7K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

10.7K
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...
10.7K
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

3.9K
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,...
3.9K
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

131.4K
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.
131.4K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

16.4K
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...
16.4K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.4K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
6.4K

You might also read

Related Articles

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

Sort by
Same author

Investigation and computational prediction of gating pore currents in Na<sub>V</sub>1.2 mutations across clinical phenotypes.

PNAS nexus·2026
Same author

A pore-facing glycan constrains GABA<sub>A</sub> receptor subunit stoichiometry and gating behavior.

Communications biology·2026
Same author

PUFA modulation of ASIC3 involves both specific and lipid solvent-like interactions.

bioRxiv : the preprint server for biology·2026
Same author

Natural Language Processing Methods for the Study of Protein-Ligand Interactions.

Journal of chemical information and modeling·2025
Same author

The differential impacts of equivalent gating-charge mutations in voltage-gated sodium channels.

The Journal of general physiology·2025
Same author

Molecular Insights into Single-Chain Lipid Modulation of Acid-Sensing Ion Channel 3.

The journal of physical chemistry. B·2024

Related Experiment Video

Updated: Jan 10, 2026

Identification and Classification of Position-specific GABAA Receptor Subunit Missense Variants for Their Role In Hippocampal Pyramidal Neurons
08:04

Identification and Classification of Position-specific GABAA Receptor Subunit Missense Variants for Their Role In Hippocampal Pyramidal Neurons

Published on: June 6, 2025

1.3K

A Pore-Facing Glycan Determines GABAA Receptor Subunit Stoichiometry and Gating Behavior.

Jing Li1, Amin Akbari Ahangar1

  • 1University of Mississippi.

Research Square
|November 24, 2025
PubMed
Summary

A conserved N-linked glycan on alpha subunits acts as a gatekeeper, limiting GABA A receptor assembly. This N-glycosylation influences receptor structure and function by controlling subunit incorporation and gating.

Keywords:
GABAA receptorN-glycosylationhetero oligomeric complexesmolecular dynamics simulationneurotransmitterpentameric ligand-gated ion channel

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

17.8K
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

14.2K

Related Experiment Videos

Last Updated: Jan 10, 2026

Identification and Classification of Position-specific GABAA Receptor Subunit Missense Variants for Their Role In Hippocampal Pyramidal Neurons
08:04

Identification and Classification of Position-specific GABAA Receptor Subunit Missense Variants for Their Role In Hippocampal Pyramidal Neurons

Published on: June 6, 2025

1.3K
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

17.8K
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

14.2K

Area of Science:

  • Neuroscience
  • Structural Biology
  • Biochemistry

Background:

  • Gamma-aminobutyric acid type A receptors (GABAARs) are crucial inhibitory neurotransmitter receptors.
  • Their function is regulated by complex hetero-pentameric subunit assembly, but the determinants of this assembly are not fully understood.

Purpose of the Study:

  • To investigate the role of N-linked glycans on alpha subunits in GABAAR assembly and gating.
  • To elucidate the molecular mechanisms by which these glycans influence receptor structure and function.

Main Methods:

  • Utilized extensive molecular dynamics (MD) simulations (28 μs) of native and modified GABAAR assemblies.
  • Analyzed structural changes, interfacial interactions (salt bridges, hydrogen bonds), and conformational dynamics.

Main Results:

  • A conserved N-linked glycan on alpha subunits acts as a steric gatekeeper, limiting alpha subunit incorporation.
  • Introducing additional pore-facing glycans disrupts interfacial networks, reduces loop flexibility, and promotes receptor closure.
  • Native GABAARs with two pore-facing glycans maintain native interfacial networks and pore radius.

Conclusions:

  • N-glycosylation, specifically pore-facing glycans on alpha subunits, is a critical determinant of GABAAR architecture and function.
  • Glycan-mediated steric hindrance regulates receptor assembly and gating dynamics.
  • Findings provide mechanistic insight into evolutionary conservation and structure-function relationships in GABAARs.