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Related Concept Videos

Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

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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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Thermosensation01:43

Thermosensation

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Peripheral thermosensation is the perception of external temperature. A change in temperature (on the surface of the skin and other tissues) is detected by a family of temperature-sensitive ion channels called Transient Receptor Potential, or TRP, receptors. These receptors are located on free nerve endings. Those detecting cold temperatures are closer to the surface of the skin than the nerve endings detecting warmth. These thermoTRP channels, while temperature selective, have relatively...
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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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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.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism....
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Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

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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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Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

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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.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several...
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Related Experiment Video

Updated: Sep 25, 2025

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4
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Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

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Structural insights into TRPV2 activation by small molecules.

Ruth A Pumroy1, Anna D Protopopova1, Tabea C Fricke2

  • 1Department of Systems Pharmacology and Translational Therapeutics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, United States.

Nature Communications
|April 28, 2022
PubMed
Summary
This summary is machine-generated.

Cryo-EM structures reveal how 2-aminoethoxydiphenyl borate (2-APB) activates Transient Receptor Potential Vanilloid 2 (TRPV2) channels. This provides a framework for developing new TRPV2-targeting drugs.

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Area of Science:

  • Structural Biology
  • Molecular Pharmacology
  • Ion Channel Physiology

Background:

  • Transient Receptor Potential Vanilloid 2 (TRPV2) channels are implicated in crucial physiological and pathophysiological functions.
  • TRPV2 represents a significant therapeutic target due to its involvement in various disease processes.
  • Understanding the molecular mechanisms of TRPV2 activation is essential for drug development.

Purpose of the Study:

  • To elucidate the structural basis of TRPV2 activation by small molecules.
  • To identify specific binding sites for activators like 2-aminoethoxydiphenyl borate (2-APB).
  • To provide a structural foundation for designing novel TRPV2 modulators.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine high-resolution structures of rat TRPV2.
  • Lipid nanodiscs were used to maintain the channel in a native-like membrane environment.
  • In silico docking and electrophysiological studies were performed to validate findings.

Main Results:

  • Novel cryo-EM structures of TRPV2 in activated states were obtained.
  • A specific binding site for 2-APB was identified at the interface of S5 and the S4-S5 linker.
  • Key residues (His521 and Arg539) were confirmed to be critical for 2-APB-mediated activation.
  • Synergistic activation of TRPV2 by 2-APB and cannabidiol was observed, with both binding simultaneously.

Conclusions:

  • The study provides unprecedented structural insights into TRPV2 activation by small molecules.
  • The identified binding site and key residues offer a target for rational drug design.
  • The findings pave the way for developing specific activators for therapeutic applications.