Phospho-Mimetic Mutation at Ser602 Inactivates Human TRPA1 Channel
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F20%3A00535243" target="_blank" >RIV/67985823:_____/20:00535243 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11320/20:10423320
Result on the web
<a href="https://www.mdpi.com/1422-0067/21/21/7995" target="_blank" >https://www.mdpi.com/1422-0067/21/21/7995</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms21217995" target="_blank" >10.3390/ijms21217995</a>
Alternative languages
Result language
angličtina
Original language name
Phospho-Mimetic Mutation at Ser602 Inactivates Human TRPA1 Channel
Original language description
The Transient Receptor Potential Ankyrin 1 (TRPA1) channel is an integrative molecular sensor for detecting environmental irritant compounds, endogenous proalgesic and inflammatory agents, pressure, and temperature. Different post-translational modifications participate in the discrimination of the essential functions of TRPA1 in its physiological environment, but the underlying structural bases are poorly understood. Here, we explored the role of the cytosolic N-terminal residue Ser602 located near a functionally important allosteric coupling domain as a potential target of phosphorylation. The phosphomimetic mutation S602D completely abrogated channel activation, whereas the phosphonull mutations S602G and S602N produced a fully functional channel. Using mutagenesis, electrophysiology, and molecular simulations, we investigated the possible structural impact of a modification (mutation or phosphorylation) of Ser602 and found that this residue represents an important regulatory site through which the intracellular signaling cascades may act to reversibly restrict or “dampen” the conformational space of the TRPA1 channel and promote its transitions to the closed state.
Czech name
—
Czech description
—
Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
30103 - Neurosciences (including psychophysiology)
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International Journal of Molecular Sciences
ISSN
1422-0067
e-ISSN
—
Volume of the periodical
21
Issue of the periodical within the volume
21
Country of publishing house
CH - SWITZERLAND
Number of pages
14
Pages from-to
7995
UT code for WoS article
000588921200001
EID of the result in the Scopus database
2-s2.0-85094974414