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Related Concept Videos

Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

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...
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 Receptors01:21

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.
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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.
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G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory organs,...

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Related Experiment Video

Updated: Jul 19, 2026

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

GABA(A) receptor function is regulated by lipid bilayer elasticity.

Rikke Søgaard1, Thomas M Werge, Camilla Bertelsen

  • 1Research Institute of Biological Psychiatry, Sct. Hans Hospital, Boserupvej 2, DK-4000 Roskilde, Denmark.

Biochemistry
|October 25, 2006
PubMed
Summary

Polyunsaturated fatty acids like DHA and other amphiphiles regulate GABA(A) receptor function by altering lipid bilayer elasticity. This research reveals a novel mechanism for membrane protein regulation by membrane physical properties.

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Single Molecule Methods for Monitoring Changes in Bilayer Elastic Properties
12:20

Single Molecule Methods for Monitoring Changes in Bilayer Elastic Properties

Published on: November 3, 2008

Related Experiment Videos

Last Updated: Jul 19, 2026

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

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

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Single Molecule Methods for Monitoring Changes in Bilayer Elastic Properties
12:20

Single Molecule Methods for Monitoring Changes in Bilayer Elastic Properties

Published on: November 3, 2008

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Docosahexaenoic acid (DHA) and polyunsaturated fatty acids (PUFAs) influence GABA(A) receptor function, but the mechanisms are unclear.
  • Amphiphiles, like Triton X-100, also affect GABA(A) receptor binding, suggesting a role for membrane properties.

Purpose of the Study:

  • To investigate the role of lipid bilayer elasticity in regulating GABA(A) receptor function.
  • To determine if amphiphile-induced changes in membrane elasticity affect GABA(A) receptor binding and function.

Main Methods:

  • Measurement of lipid bilayer stiffness using gramicidin channels.
  • Assessing GABA(A) receptor [(3)H]-muscimol binding in mammalian cells.
  • Whole-cell voltage-clamp experiments to measure GABA-induced currents.

Main Results:

  • Four structurally unrelated amphiphiles (Triton X-100, octyl-beta-glucoside, capsaicin, DHA) decreased bilayer stiffness and promoted GABA(A) receptor binding.
  • A correlation was observed between decreased bilayer stiffness and increased GABA(A) receptor binding capacity.
  • Amphiphiles reduced GABA-induced current amplitude and accelerated receptor desensitization.

Conclusions:

  • GABA(A) receptor function is modulated by lipid bilayer elasticity.
  • PUFAs may regulate membrane protein function broadly by altering the physical properties of the lipid bilayer.