Intracellular cavity of sensor domain controls allosteric gating of TRPA1 channel

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F18%3A10389195" target="_blank" >RIV/00216208:11320/18:10389195 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67985823:_____/18:00489284

Výsledek na webu

<a href="https://doi.org/10.1126/scisignal.aan8621" target="_blank" >https://doi.org/10.1126/scisignal.aan8621</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1126/scisignal.aan8621" target="_blank" >10.1126/scisignal.aan8621</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Intracellular cavity of sensor domain controls allosteric gating of TRPA1 channel

Popis výsledku v původním jazyce

Transient receptor potential ankyrin 1 (TRPA1) is a temperature-sensitive ion channel activated by various pungent and irritant compounds that can produce pain in humans. Its activation involves an allosteric mechanism whereby electrophilic agonists evoke interactions within cytosolic domains and open the channel pore through an integrated nexus formed by intracellular membrane proximal regions that are densely packed beneath the lower segment of the S1-S4 sensor domain. Studies indicate that this part of the channel may contain residues that form a water-accessible cavity that undergoes changes in solvation during channel gating. We identified conserved polar residues facing the putative lower crevice of the sensor domain that were crucial determinants of the electrophilic, voltage, and calcium sensitivity of the TRPA1 channel. This part of the sensor may also comprise a domain capable of binding to membrane phosphoinositides through which gating of the channel is regulated in a state-dependent manner.

Název v anglickém jazyce

Intracellular cavity of sensor domain controls allosteric gating of TRPA1 channel

Popis výsledku anglicky

Transient receptor potential ankyrin 1 (TRPA1) is a temperature-sensitive ion channel activated by various pungent and irritant compounds that can produce pain in humans. Its activation involves an allosteric mechanism whereby electrophilic agonists evoke interactions within cytosolic domains and open the channel pore through an integrated nexus formed by intracellular membrane proximal regions that are densely packed beneath the lower segment of the S1-S4 sensor domain. Studies indicate that this part of the channel may contain residues that form a water-accessible cavity that undergoes changes in solvation during channel gating. We identified conserved polar residues facing the putative lower crevice of the sensor domain that were crucial determinants of the electrophilic, voltage, and calcium sensitivity of the TRPA1 channel. This part of the sensor may also comprise a domain capable of binding to membrane phosphoinositides through which gating of the channel is regulated in a state-dependent manner.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30105 - Physiology (including cytology)

Projekt

<a href="/cs/project/GA15-15839S" target="_blank" >GA15-15839S: Regulační mechanizmy nociceptivních ‘transient receptor potential’ iontových kanálů</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Science Signaling

ISSN

1945-0877

e-ISSN

—

Svazek periodika

11

Číslo periodika v rámci svazku

514

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

—

Kód UT WoS článku

000423100700003

EID výsledku v databázi Scopus

2-s2.0-85041031781