The human TRPA1 intrinsic cold and heat sensitivity involves separate channel structures beyond the N-ARD domain.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
17 10 2022
17 10 2022
Historique:
received:
08
10
2021
accepted:
04
10
2022
entrez:
17
10
2022
pubmed:
18
10
2022
medline:
20
10
2022
Statut:
epublish
Résumé
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, ∆1-688 hTRPA1, without the N-terminal ankyrin repeat domain (N-ARD), was more sensitive to cold and heat, whereas ∆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.
Identifiants
pubmed: 36253390
doi: 10.1038/s41467-022-33876-8
pii: 10.1038/s41467-022-33876-8
pmc: PMC9576766
doi:
Substances chimiques
TRPA1 Cation Channel
0
TRPA1 protein, human
0
Tryptophan
8DUH1N11BX
Alanine
OF5P57N2ZX
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
6113Informations de copyright
© 2022. The Author(s).
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