IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v445y2007i7127d10.1038_nature05544.html
   My bibliography  Save this article

Noxious compounds activate TRPA1 ion channels through covalent modification of cysteines

Author

Listed:
  • Lindsey J. Macpherson

    (The Scripps Research Institute)

  • Adrienne E. Dubin

    (The Scripps Research Institute
    The Scripps Research Institute)

  • Michael J. Evans

    (The Scripps Research Institute)

  • Felix Marr

    (The Scripps Research Institute
    Westfälische Wilhelms-Universität Münster)

  • Peter G. Schultz

    (The Scripps Research Institute
    Genomics Institute of the Novartis Research Foundation)

  • Benjamin F. Cravatt

    (The Scripps Research Institute
    The Scripps Research Institute)

  • Ardem Patapoutian

    (The Scripps Research Institute
    Genomics Institute of the Novartis Research Foundation)

Abstract

Sensing danger The TRPA1 ion channel, found in neurons associated with sensing pain, responds to noxious and pungent compounds and also to cold. Gene knockout experiments in mice confirm that TRPA1 is a physiologicallyrequired pain sensor. How such diverse stimuli activate TRPA1 was not known but Macpherson et al. show that that TRPA1 is activated by covalent modification of its cysteine residues. It is not unusual for proteins to be modified by cysteine reactive agents, but this is the first ion channel known to be activated by this method. The role of TRPA1 activation in response to electrophile toxicity and oxidative stress may be to warn the organism of potential tissue damage.

Suggested Citation

  • Lindsey J. Macpherson & Adrienne E. Dubin & Michael J. Evans & Felix Marr & Peter G. Schultz & Benjamin F. Cravatt & Ardem Patapoutian, 2007. "Noxious compounds activate TRPA1 ion channels through covalent modification of cysteines," Nature, Nature, vol. 445(7127), pages 541-545, February.
    • Handle: RePEc:nat:nature:v:445:y:2007:i:7127:d:10.1038_nature05544
    DOI: 10.1038/nature05544
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature05544
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature05544?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Yi-Yu Lin & Yan Lu & Chun-Yun Li & Xue-Fei Ma & Miao-Qing Shao & Yu-Hao Gao & Yu-Qing Zhang & Hai-Ning Jiang & Yan Liu & Yang Yang & Li-Dong Huang & Peng Cao & Heng-Shan Wang & Jin Wang & Ye Yu, 2024. "Finely ordered intracellular domain harbors an allosteric site to modulate physiopathological function of P2X3 receptors," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Xiaoning Wang & Yangyang Sun & Qian Wang & Fengying Liu & Weijie Yang & Xin Sui & Jun Yang & Minmin Zhang & Shuai Wang & Zhenyu Xiao & Yuan Luo & Yongan Wang & Tong Zhu, 2022. "Potential Common Mechanisms of Cytotoxicity Induced by Amide Herbicides via TRPA1 Channel Activation," IJERPH, MDPI, vol. 19(13), pages 1-18, June.
    3. A. Catalina Vélez-Ortega & Ruben Stepanyan & Stephanie E. Edelmann & Sara Torres-Gallego & Channy Park & Desislava A. Marinkova & Joshua S. Nowacki & Ghanshyam P. Sinha & Gregory I. Frolenkov, 2023. "TRPA1 activation in non-sensory supporting cells contributes to regulation of cochlear sensitivity after acoustic trauma," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    4. Avnika Bali & Samantha P. Schaefer & Isabelle Trier & Alice L. Zhang & Lilian Kabeche & Candice E. Paulsen, 2023. "Molecular mechanism of hyperactivation conferred by a truncation of TRPA1," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:445:y:2007:i:7127:d:10.1038_nature05544. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.