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Related Concept Videos

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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Mechanically-gated Ion Channels01:12

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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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Voltage-gated Ion Channels01:26

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Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
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Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

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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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Ion Channels01:19

Ion Channels

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The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
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Non-gated Ion Channels01:24

Non-gated Ion Channels

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Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
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Related Experiment Video

Updated: Jul 20, 2025

Harvesting Venom Toxins from Assassin Bugs and Other Heteropteran Insects
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Harvesting Venom Toxins from Assassin Bugs and Other Heteropteran Insects

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Human STING is a proton channel.

Bingxu Liu1,2,3, Rebecca J Carlson1,4, Ivan S Pires3

  • 1Broad Institute, Cambridge, MA, USA.

Science (New York, N.Y.)
|August 3, 2023
PubMed
Summary
This summary is machine-generated.

Stimulator of interferon genes (STING) acts as a proton channel, regulating cellular processes. This channel activity is crucial for inflammasome activation and LC3B lipidation, but not interferon induction, offering therapeutic targets.

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Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • Proton leakage from organelles signals noncanonical light chain 3B (LC3B) lipidation and inflammasome activation.
  • These processes are typically induced upon stimulator of interferon genes (STING) activation.

Purpose of the Study:

  • To investigate the hypothesis that human STING functions as a proton channel.
  • To determine the role of STING's potential channel activity in downstream cellular events like LC3B lipidation and inflammasome activation.

Main Methods:

  • Structural analysis to identify STING's putative channel interface.
  • Measuring pH changes in the Golgi upon STING activation.
  • Reconstituting STING in liposomes to assess proton transport.
  • Utilizing Compound 53 (C53), a STING agonist, to inhibit STING activity and proton flux.
  • Evaluating the impact of C53 on STING-induced LC3B lipidation and inflammasome activation.

Main Results:

  • STING activation led to a pH increase in the Golgi, indicating proton efflux.
  • Reconstituted STING demonstrated transmembrane proton transport capabilities in liposomes.
  • Compound 53 (C53) effectively blocked STING-induced proton flux in both cellular models and liposomes.
  • C53 also inhibited STING-induced LC3B lipidation and inflammasome activation, highlighting the necessity of STING's channel function for these pathways.

Conclusions:

  • Human STING functions as a proton channel.
  • STING's proton channel activity is essential for inducing LC3B lipidation and inflammasome activation.
  • The interferon-induction function of STING can be separated from its role in LC3B lipidation and inflammasome activation, suggesting distinct functional mechanisms.