Identification and subcellular localization of molecular complexes of Gq/11? protein in HEK293 cells

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10123868" target="_blank" >RIV/00216208:11310/12:10123868 - isvavai.cz</a>

Výsledek na webu

<a href="http://abbs.oxfordjournals.org/" target="_blank" >http://abbs.oxfordjournals.org/</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/abbs/gms050" target="_blank" >10.1093/abbs/gms050</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Identification and subcellular localization of molecular complexes of Gq/11? protein in HEK293 cells

Popis výsledku v původním jazyce

Heterotrimeric G-proteins localized in the plasma membrane convey the signals from G-protein-coupled receptors (GPCRs) to different effectors. At least some types of G-protein ? subunits have been shown to be partly released from plasma membranes and tomove into the cytosol after receptor activation by the agonists. However, the mechanism underlying subcellular redistribution of trimeric G-proteins is not well understood and no definitive conclusions have been reached regarding the translocation of G?subunits between membranes and cytosol. Here we used subcellular fractionation and clear-native polyacrylamide gel electrophoresis to identify molecular complexes of G(q/11)? protein and to determine their localization in isolated fractions and stabilityin na?ve and thyrotropin-releasing hormone (TRH)-treated HEK293 cells expressing high levels of TRH receptor and G(11)? protein. We identified two high-molecular-weight complexes of 300 and 140 kDa in size comprising the G(q/11) protein,

Název v anglickém jazyce

Identification and subcellular localization of molecular complexes of Gq/11? protein in HEK293 cells

Popis výsledku anglicky

Heterotrimeric G-proteins localized in the plasma membrane convey the signals from G-protein-coupled receptors (GPCRs) to different effectors. At least some types of G-protein ? subunits have been shown to be partly released from plasma membranes and tomove into the cytosol after receptor activation by the agonists. However, the mechanism underlying subcellular redistribution of trimeric G-proteins is not well understood and no definitive conclusions have been reached regarding the translocation of G?subunits between membranes and cytosol. Here we used subcellular fractionation and clear-native polyacrylamide gel electrophoresis to identify molecular complexes of G(q/11)? protein and to determine their localization in isolated fractions and stabilityin na?ve and thyrotropin-releasing hormone (TRH)-treated HEK293 cells expressing high levels of TRH receptor and G(11)? protein. We identified two high-molecular-weight complexes of 300 and 140 kDa in size comprising the G(q/11) protein,

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

ED - Fyziologie

OECD FORD obor

—

Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Acta Biochimica et Biophysica Sinica

ISSN

1672-9145

e-ISSN

—

Svazek periodika

44

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

CN - Čínská lidová republika

Počet stran výsledku

9

Strana od-do

641-649

Kód UT WoS článku

000306922800003

EID výsledku v databázi Scopus

—