Number of the records: 1
Transient receptor potential ankyrin 1 channel: an evolutionarily tuned thermosensor
- 1.0544563 - FGÚ 2022 RIV CZ eng J - Journal Article
Sinica, Viktor - Vlachová, Viktorie
Transient receptor potential ankyrin 1 channel: an evolutionarily tuned thermosensor.
Physiological Research. Roč. 70, č. 3 (2021), s. 363-381. ISSN 0862-8408. E-ISSN 1802-9973
R&D Projects: GA ČR(CZ) GA19-03777S
Institutional support: RVO:67985823
Keywords : Transient Receptor Potential Ankyrin 1 * structure-function * noxious heat * functional diversity * gating models
OECD category: Neurosciences (including psychophysiology
Impact factor: 2.139, year: 2021
Method of publishing: Open access
https://www.biomed.cas.cz/physiolres/pdf/2021/70_363.pdf
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.
Permanent Link: http://hdl.handle.net/11104/0321410
Number of the records: 1