Putative interaction site for membrane phospholipids controls activation of TRPA1 channel at physiological membrane potentials

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F19%3A00510413" target="_blank" >RIV/67985823:_____/19:00510413 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/19:10396661

Result on the web

<a href="https://doi.org/10.1111/febs.14931" target="_blank" >https://doi.org/10.1111/febs.14931</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/febs.14931" target="_blank" >10.1111/febs.14931</a>

Result language

angličtina

Original language name

Putative interaction site for membrane phospholipids controls activation of TRPA1 channel at physiological membrane potentials

Original language description

The transient receptor potential ankyrin 1 (TRPA1) channel is a polymodal sensor of environmental irritant compounds, endogenous proalgesic agents, and cold. Upon activation, TRPA1 channels increase cellular calcium levels via direct permeation and trigger signaling pathways that hydrolyze phosphatidylinositol-4,5-bisphosphate (PIP2) in the inner membrane leaflet. Our objective was to determine the extent to which a putative PIP2-interaction site (Y1006-Q1031) is involved in TRPA1 regulation. The interactions of two specific peptides (L992-N1008 and T1003-P1034) with model lipid membranes were characterized by biophysical approaches to obtain information about affinity, peptide secondary structure, and peptide effect in the lipid organization. The results indicate that the two peptides interact with lipid membranes only if PIP2 is present and their affinities depend on the presence of calcium. Using whole-cell electrophysiology, we demonstrate that mutation at F1020 produced channels with faster activation kinetics and with a rightward shifted voltage-dependent activation curve by altering the allosteric constant that couples voltage sensing to pore opening. We assert that the presence of PIP2 is essential for the interaction of the two peptide sequences with the lipid membrane. The putative phosphoinositide-interacting domain comprising the highly conserved F1020 contributes to the stabilization of the TRPA1 channel gate.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

30103 - Neurosciences (including psychophysiology)

Project

<a href="/en/project/GA19-03777S" target="_blank" >GA19-03777S: Molecular Basis of Thermosensitive TRP Ion Channel Regulation in Nociceptive Neurons</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2019

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

FEBS Journal

ISSN

1742-464X

e-ISSN

—

Volume of the periodical

286

Issue of the periodical within the volume

18

Country of publishing house

GB - UNITED KINGDOM

Number of pages

20

Pages from-to

3664-3683

UT code for WoS article

000486201000010

EID of the result in the Scopus database

2-s2.0-85067398939