Počet záznamů: 1
The human TRPA1 intrinsic cold and heat sensitivity involves separate channel structures beyond the N-ARD domain
- 1.
SYSNO ASEP 0563535 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název The human TRPA1 intrinsic cold and heat sensitivity involves separate channel structures beyond the N-ARD domain Tvůrce(i) Moparthi, L. (SE)
Sinica, Viktor (FGU-C) RID, ORCID, SAI
Moparthi, V. K. (SE)
Kreir, M. (BE)
Vignane, T. (DE)
Filipovic, M. R. (DE)
Vlachová, Viktorie (FGU-C) RID, ORCID, SAI
Zygmunt, P. M. (SE)Číslo článku 6113 Zdroj.dok. Nature Communications. - : Nature Publishing Group
Roč. 13, č. 1 (2022)Poč.str. 15 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova TRP channel ; structure-function ; thermoTRP Obor OECD Neurosciences (including psychophysiology CEP GA22-13750S GA ČR - Grantová agentura ČR Způsob publikování Open access Institucionální podpora FGU-C - RVO:67985823 UT WOS 000871026900011 EID SCOPUS 85139943046 DOI 10.1038/s41467-022-33876-8 Anotace 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. Pracoviště Fyziologický ústav Kontakt Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Rok sběru 2023 Elektronická adresa https://doi.org/10.1038/s41467-022-33876-8
Počet záznamů: 1