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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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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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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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Activation and Inactivation of G Proteins01:22

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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...
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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.
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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.
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Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4
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TRPV1 Opening is Stabilized Equally by Its Four Subunits.

Shisheng Li, Phuong Tran Nguyen, Simon Vu

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    Resiniferatoxin (RTX) binding to the capsaicin receptor TRPV1 sequentially opens the channel. Each RTX molecule binding contributes equally to activation energy, primarily by destabilizing the closed state.

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    Area of Science:

    • Molecular biology
    • Ion channel biophysics
    • Pain signaling

    Background:

    • The capsaicin receptor TRPV1 is a key sensor for noxious stimuli.
    • Understanding how TRPV1 gating is regulated by vanilloid molecules like RTX is crucial for pain research.

    Approach:

    • Developed a method to control RTX binding stoichiometry (0-4 molecules) to mouse TRPV1.
    • Performed equilibrium measurements at macroscopic and single-molecule levels.

    Key Points:

    • Each RTX binding event contributes approximately 1.86 kcal/mol to TRPV1 activation.
    • RTX binding predominantly destabilizes the closed conformation of TRPV1.
    • Sequential RTX binding increases channel open probability without changing single-channel conductance.

    Conclusions:

    • RTX binding leads to a single open-pore conformation of TRPV1.
    • This study provides quantitative energetic insights into TRPV1 channel gating by vanilloids.