Sequential inter- and intrasubunit rearrangements during activation of dimeric metabotropic glutamate receptor 1

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F12%3A00381622" target="_blank" >RIV/68378050:_____/12:00381622 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1126/scisignal.2002720" target="_blank" >http://dx.doi.org/10.1126/scisignal.2002720</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1126/scisignal.2002720" target="_blank" >10.1126/scisignal.2002720</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Sequential inter- and intrasubunit rearrangements during activation of dimeric metabotropic glutamate receptor 1

Popis výsledku v původním jazyce

The metabotropic glutamate receptor 1 (mGluR1), a class C member of the heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor family, is a constitutive dimer that regulates excitatory neurotransmission. We investigated the role of homodimer formation in mGluR1 activation by examining activation-dependent inter-and intrasubunit conformational changes by fluorescence resonance energy transfer (FRET). We inserted yellow and cyan fluorescent proteins in the second intracellular loopand at the carboxyl terminus of mGluR1 to act as FRET sensors and expressed these proteins in human embryonic kidney 293 cells. Agonist-dependent activation of these mGluR1 chimeras rapidly increased the intersubunit FRET, suggesting rapid movement of the subunits relative to each other. After intersubunit movement, the intrasubunit FRET decreased, reflecting conformational changes within a subunit. Cotransfection of chimeric receptor subunits that were capable or incapable of G protein

Název v anglickém jazyce

Sequential inter- and intrasubunit rearrangements during activation of dimeric metabotropic glutamate receptor 1

Popis výsledku anglicky

The metabotropic glutamate receptor 1 (mGluR1), a class C member of the heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor family, is a constitutive dimer that regulates excitatory neurotransmission. We investigated the role of homodimer formation in mGluR1 activation by examining activation-dependent inter-and intrasubunit conformational changes by fluorescence resonance energy transfer (FRET). We inserted yellow and cyan fluorescent proteins in the second intracellular loopand at the carboxyl terminus of mGluR1 to act as FRET sensors and expressed these proteins in human embryonic kidney 293 cells. Agonist-dependent activation of these mGluR1 chimeras rapidly increased the intersubunit FRET, suggesting rapid movement of the subunits relative to each other. After intersubunit movement, the intrasubunit FRET decreased, reflecting conformational changes within a subunit. Cotransfection of chimeric receptor subunits that were capable or incapable of G protein

Druh

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

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Science Signaling

ISSN

1937-9145

e-ISSN

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Svazek periodika

5

Číslo periodika v rámci svazku

237

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

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Kód UT WoS článku

000307885200002

EID výsledku v databázi Scopus

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