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The human TRPA1 intrinsic cold and heat sensitivity involves separate channel structures beyond the N-ARD domain

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F22%3A00563535" target="_blank" >RIV/67985823:_____/22:00563535 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1038/s41467-022-33876-8" target="_blank" >https://doi.org/10.1038/s41467-022-33876-8</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/s41467-022-33876-8" target="_blank" >10.1038/s41467-022-33876-8</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The human TRPA1 intrinsic cold and heat sensitivity involves separate channel structures beyond the N-ARD domain

  • Original language description

    TRP channels sense temperatures ranging from noxious cold to noxious heat. Whether specialized TRP thermosensor modules exist and how they control channel pore gating is unknown. We studied purified human TRPA1 (hTRPA1) truncated proteins to gain insight into the temperature gating of hTRPA1. In patch-clamp bilayer recordings, Delta 1-688 hTRPA1, without the N-terminal ankyrin repeat domain (N-ARD), was more sensitive to cold and heat, whereas Delta 1-854 hTRPA1, also lacking the S1-S4 voltage sensing-like domain (VSLD), gained sensitivity to cold but lost its heat sensitivity. In hTRPA1 intrinsic tryptophan fluorescence studies, cold and heat evoked rearrangement of VSLD and the C-terminus domain distal to the transmembrane pore domain S5-S6 (CTD). In whole-cell electrophysiology experiments, replacement of the CTD located cysteines 1021 and 1025 with alanine modulated hTRPA1 cold responses. It is proposed that hTRPA1 CTD harbors cold and heat sensitive domains allosterically coupled to the S5-S6 pore region and the VSLD, respectively.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30103 - Neurosciences (including psychophysiology)

Result continuities

  • Project

    <a href="/en/project/GA22-13750S" target="_blank" >GA22-13750S: Signaling pathways affecting human TRPC5 receptor function: Prediction of their association with rheumatoid arthritis pain</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2022

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Nature Communications

  • ISSN

    2041-1723

  • e-ISSN

    2041-1723

  • Volume of the periodical

    13

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    15

  • Pages from-to

    6113

  • UT code for WoS article

    000871026900011

  • EID of the result in the Scopus database

    2-s2.0-85139943046