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The human TRPA1 intrinsic cold and heat sensitivity involves separate channel structures beyond the N-ARD domain
L. Moparthi, V. Sinica, VK. Moparthi, M. Kreir, T. Vignane, MR. Filipovic, V. Vlachova, PM. Zygmunt
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
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- MeSH
- alanin MeSH
- ankyrinová repetice * MeSH
- kationtový kanál TRPA1 genetika metabolismus MeSH
- lidé MeSH
- tryptofan MeSH
- vnímání teploty MeSH
- vysoká teplota * MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
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.
Department of Clinical Sciences Malmö Lund University SE 214 28 Malmö Sweden
Wallenberg Centre for Molecular Medicine Linköping University SE 581 83 Linköping Sweden
Citace poskytuje Crossref.org
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- $a Moparthi, Lavanya $u Wallenberg Centre for Molecular Medicine, Linköping University, SE-581 83, Linköping, Sweden. lavanya.moparthi@liu.se $u Department of Biomedical and Clinical Sciences (BKV), Faculty of Health Sciences, Linköping University, SE-581 83, Linköping, Sweden. lavanya.moparthi@liu.se $1 https://orcid.org/0000000260303084
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- $a The human TRPA1 intrinsic cold and heat sensitivity involves separate channel structures beyond the N-ARD domain / $c L. Moparthi, V. Sinica, VK. Moparthi, M. Kreir, T. Vignane, MR. Filipovic, V. Vlachova, PM. Zygmunt
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- $a 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.
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