Communication between N terminus and loop2 tunes Orai activation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F18%3A00489833" target="_blank" >RIV/61388971:_____/18:00489833 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.saa.2017.12.021" target="_blank" >http://dx.doi.org/10.1016/j.saa.2017.12.021</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.saa.2017.12.021" target="_blank" >10.1016/j.saa.2017.12.021</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Communication between N terminus and loop2 tunes Orai activation

Popis výsledku v původním jazyce

The CRAC channel gating involves the binding of STIM1 C-terminus to cytosolic N- and C-termini of Orai. The C-termini of Orai is the main binding partner however N-termini also have been found necessary for Orai channel function. Despite a highly conserved ETON region Orai1 and Orai3 differ in length of the ETON region. Our aim here was to study the reasons for different behavior of these two isoforms and to find the differences in structural requirement for gating and function. While there is no interaction between the N-terminus and loop2 in Orai3, we predict that interactions between loop2 and Orai1 N-terminus results into masking the STIM1 coupling sites which are located either at N-terminus or loop2 or both, thus loop2 either directly or allosterically affects the STIM1-Orai coupling in an isoform specific manner. Thus along with the requirement of conserved ETON region a fine tuning between N-termini and loop2 conformations has an essential role in maintaining permissive conformation of channel and store-operated function of Orai channel.nn

Název v anglickém jazyce

Communication between N terminus and loop2 tunes Orai activation

Popis výsledku anglicky

The CRAC channel gating involves the binding of STIM1 C-terminus to cytosolic N- and C-termini of Orai. The C-termini of Orai is the main binding partner however N-termini also have been found necessary for Orai channel function. Despite a highly conserved ETON region Orai1 and Orai3 differ in length of the ETON region. Our aim here was to study the reasons for different behavior of these two isoforms and to find the differences in structural requirement for gating and function. While there is no interaction between the N-terminus and loop2 in Orai3, we predict that interactions between loop2 and Orai1 N-terminus results into masking the STIM1 coupling sites which are located either at N-terminus or loop2 or both, thus loop2 either directly or allosterically affects the STIM1-Orai coupling in an isoform specific manner. Thus along with the requirement of conserved ETON region a fine tuning between N-termini and loop2 conformations has an essential role in maintaining permissive conformation of channel and store-operated function of Orai channel.nn

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

<a href="/cs/project/LTC17069" target="_blank" >LTC17069: Pochopení různých aspektů struktury a funkce systémů translokujících kationty</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

—

Svazek periodika

293

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

15

Strana od-do

1271-1285

Kód UT WoS článku

000423515000014

EID výsledku v databázi Scopus

2-s2.0-85041209005