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Related Concept Videos

Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

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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...
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Regulation of Transpiration by Stomata02:04

Regulation of Transpiration by Stomata

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During photosynthesis, plants acquire the necessary carbon dioxide and release the produced oxygen back into the atmosphere. Openings in the epidermis of plant leaves is the site of this exchange of gasses. A single opening is called a stoma—derived from the Greek word for “mouth.” Stomata open and close in response to a variety of environmental cues.
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Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

7.5K
Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
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G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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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...
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Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

13.8K
Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...
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GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

7.1K
Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of...
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Related Experiment Video

Updated: Dec 28, 2025

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers
09:54

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers

Published on: November 19, 2015

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How stomatin stops ASIC3 gating.

Ben Short

    The Journal of General Physiology
    |February 19, 2020
    PubMed
    Summary

    Stomatin protein may trap acid-sensing ion channel 3 (ASIC3) in a desensitized state, according to a JGP study. This finding offers new insights into ion channel regulation.

    Area of Science:

    • Molecular biology
    • Neuroscience
    • Physiology

    Background:

    • Acid-sensing ion channels (ASICs) are crucial for neuronal function and pain perception.
    • ASIC3, specifically, is implicated in various physiological processes, including mechanotransduction and pain signaling.
    • Understanding the regulation of ASIC3 activity is vital for developing targeted therapies.

    Discussion:

    • The JGP study proposes a novel mechanism where stomatin interacts with ASIC3.
    • This interaction may stabilize ASIC3 in a desensitized conformation, reducing its ion channel activity.
    • This trapping mechanism could represent a new regulatory pathway for ASIC3 function.

    Key Insights:

    • Stomatin acts as a potential regulator of ASIC3 channel gating.
    • The study provides evidence for stomatin's role in maintaining ASIC3 desensitization.

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  • This interaction could influence cellular responses to acidic environments.
  • Outlook:

    • Further research is needed to elucidate the precise structural basis of the stomatin-ASIC3 interaction.
    • Investigating this mechanism could reveal new therapeutic targets for pain and other ASIC3-related disorders.
    • Exploring stomatin's role in other ion channel functions may uncover broader regulatory principles.