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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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