A calcium-accumulating region, CAR, in the channel Orai1 enhances Ca2+ permeation and SOCE-induced gene transcription
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F15%3A43890218" target="_blank" >RIV/60076658:12310/15:43890218 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/15:00463207
Result on the web
<a href="http://stke.sciencemag.org/content/8/408/ra131" target="_blank" >http://stke.sciencemag.org/content/8/408/ra131</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1126/scisignal.aab1901" target="_blank" >10.1126/scisignal.aab1901</a>
Alternative languages
Result language
angličtina
Original language name
A calcium-accumulating region, CAR, in the channel Orai1 enhances Ca2+ permeation and SOCE-induced gene transcription
Original language description
The Ca2+ release-activated Ca2+ channel mediates Ca2+ influx in a plethora of cell types, thereby controlling diverse cellular functions. The channel complex is composed of stromal interaction molecule 1 (STIM1), an endoplasmic reticulum Ca2+-sensing protein, and Orai1, a plasma membrane Ca2+ channel. Channels composed of STIM1 and Orai1 mediate Ca2+ influx even at low extracellular Ca2+ concentrations. We investigated whether the activity of Orai1 adapted to different environmental Ca2+ concentrations.We used homology modeling and molecular dynamics simulations to predict the presence of an extracellular Ca2+-accumulating region (CAR) at the pore entrance of Orai1. Furthermore, simulations of Orai1 proteins with mutations in CAR, along with live-cellexperiments, or simulations and electrophysiological recordings of the channel with transient, electrostatic loop3 interacting with loop1 (the site of CAR) determined that CAR enhanced Ca2+ permeation most efficiently at low external Ca2
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GA13-21053S" target="_blank" >GA13-21053S: Investigating the Symmetric Allosteric Mechanism of Hexameric Escherichia coli Arginine Repressor using Computational Simulations</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Science Signaling
ISSN
1945-0877
e-ISSN
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Volume of the periodical
8
Issue of the periodical within the volume
408
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
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UT code for WoS article
000367102600004
EID of the result in the Scopus database
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