Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

TRP channel activation by reversible covalent modification.

Andrew Hinman1, Huai-Hu Chuang, Diana M Bautista

  • 1Department of Physiology, University of California, San Francisco, CA 94158, USA.

Proceedings of the National Academy of Sciences of the United States of America
|December 14, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Structural energetics of cold sensitivity.

Nature·2026
Same author

Parasites trigger epithelial cell crosstalk to drive gut-brain signalling.

Nature·2026
Same author

Mechanism of Gating and Isoform-Specific Inhibition in Renal CLC Chloride Channels.

bioRxiv : the preprint server for biology·2026
Same author

A cellular basis for heightened gut sensitivity in females.

Science (New York, N.Y.)·2025
Same author

Mitochondrial activity tunes nociceptor resilience to excitotoxicity.

Cell·2025
Same author

The structural basis of cold sensitivity.

bioRxiv : the preprint server for biology·2025

Allyl isothiocyanate activates the TRPA1 pain receptor through direct, reversible covalent modification of cysteine residues. This finding reveals a novel mechanism for natural products activating receptors.

Area of Science:

  • Biochemistry
  • Neuroscience
  • Molecular Pharmacology

Background:

  • Allyl isothiocyanate, found in mustard oils, triggers pain by activating the TRPA1 ion channel.
  • Isothiocyanates are electrophilic and can covalently bind to thiols and amines.

Purpose of the Study:

  • To investigate the mechanism by which isothiocyanates activate the TRPA1 channel.
  • To determine if covalent modification is essential for TRPA1 activation by these compounds.

Main Methods:

  • Utilized thiol-reactive compounds to probe TRPA1 activation.
  • Investigated cysteine residue modification within the TRPA1 channel's N terminus.

Main Results:

  • Diverse thiol-reactive compounds were found to activate TRPA1.

Related Experiment Videos

  • TRPA1 activation by these compounds depends on covalent modification of specific cysteine residues.
  • Modification occurred at the cytoplasmic N terminus of the TRPA1 channel.

    • Conclusions:

    • TRPA1 activation by isothiocyanates involves direct, reversible covalent modification of cysteine residues.
    • This study presents an unconventional mechanism for natural product receptor activation.