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Transient receptor potential ankyrin 1 channel: an evolutionarily tuned thermosensor
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SYSNO ASEP 0544563 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Transient receptor potential ankyrin 1 channel: an evolutionarily tuned thermosensor Author(s) Sinica, Viktor (FGU-C) RID, ORCID, SAI
Vlachová, Viktorie (FGU-C) RID, ORCID, SAISource Title Physiological Research. - : Fyziologický ústav AV ČR, v. v. i. - ISSN 0862-8408
Roč. 70, č. 3 (2021), s. 363-381Number of pages 19 s. Language eng - English Country CZ - Czech Republic Keywords Transient Receptor Potential Ankyrin 1 ; structure-function ; noxious heat ; functional diversity ; gating models Subject RIV FH - Neurology OECD category Neurosciences (including psychophysiology R&D Projects GA19-03777S GA ČR - Czech Science Foundation (CSF) Method of publishing Open access Institutional support FGU-C - RVO:67985823 UT WOS 000675528500005 EID SCOPUS 85112123925 DOI 10.33549/physiolres.934697 Annotation The discovery of the role of the transient receptor potential ankyrin 1 (TRPA1) channel as a polymodal detector of cold and pain-producing stimuli almost two decades ago catalyzed the consequent identification of various vertebrate and invertebrate orthologues. In different species, the role of TRPA1 has been implicated in numerous physiological functions, indicating that the molecular structure of the channel exhibits evolutionary flexibility. Until very recently, information about the critical elements of the temperature-sensing molecular machinery of thermosensitive ion channels such as TRPA1 had lagged far behind information obtained from mutational and functional analysis. Current developments in single-particle cryo-electron microscopy are revealing precisely how the thermosensitive channels operate, how they might be targeted with drugs, and at which sites they can be critically regulated by membrane lipids. This means that it is now possible to resolve a huge number of very important pharmacological, biophysical and physiological questions in a way we have never had before. In this review, we aim at providing some of the recent knowledge on the molecular mechanisms underlying the temperature sensitivity of TRPA1. We also demonstrate how the search for differences in temperature and chemical sensitivity between human and mouse TRPA1 orthologues can be a useful approach to identifying important domains with a key role in channel activation. Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2022 Electronic address https://www.biomed.cas.cz/physiolres/pdf/2021/70_363.pdf
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