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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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Intracerebroventricular Treatment with Resiniferatoxin and Pain Tests in Mice
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Engineering vanilloid-sensitivity into the rat TRPV2 channel.

Feng Zhang1, Sonya M Hanson1,2, Andres Jara-Oseguera1

  • 1Molecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, United States.

Elife
|May 14, 2016
PubMed
Summary

Researchers investigated the Transient Receptor Potential Vanilloid 1 (TRPV1) channel and its related TRPV2 channel. They found that TRPV2

Keywords:
biophysicscapsicingating mechanismneuroscienceratstructural biologytemperature-sensingthermosensing

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Area of Science:

  • Molecular biology and biophysics
  • Ion channel structure and function
  • Sensory neuroscience

Background:

  • The Transient Receptor Potential Vanilloid 1 (TRPV1) channel detects noxious stimuli like heat and chemicals.
  • TRPV2 channel gating mechanisms are poorly understood due to lack of selective ligands and high heat activation threshold.
  • Cryo-EM structures show TRPV1 and TRPV2 share similar structures, with a potential vanilloid binding pocket in TRPV1.

Purpose of the Study:

  • To investigate the resiniferatoxin (RTx) binding site in TRPV1.
  • To explore functional relationships between TRPV1 and TRPV2.
  • To understand TRPV2 channel gating and permeation properties.

Main Methods:

  • Biochemical approaches
  • Electrophysiological approaches
  • Cryo-electron microscopy (Cryo-EM) structure analysis

Main Results:

  • Vanilloids interact with the proposed RTx binding pocket in TRPV1.
  • A tarantula toxin allosterically influences vanilloid binding to TRPV1.
  • Sensitivity to RTx can be engineered into TRPV2, indicating similar gating and permeation properties to TRPV1.

Conclusions:

  • The study elucidates vanilloid binding mechanisms in TRPV1.
  • Functional similarities between TRPV1 and TRPV2 are demonstrated through toxin sensitivity engineering.
  • Findings provide insights into ion channel gating and ligand interactions.