Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F12%3A10124478" target="_blank" >RIV/00216208:11320/12:10124478 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67985823:_____/12:00388343 RIV/61388971:_____/12:00388343 RIV/00216208:11310/12:10124478

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.bpj.2012.09.021" target="_blank" >http://dx.doi.org/10.1016/j.bpj.2012.09.021</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bpj.2012.09.021" target="_blank" >10.1016/j.bpj.2012.09.021</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding

Popis výsledku v původním jazyce

Phosducin (Pdc), a highly conserved phosphoprotein, plays an important role in the regulation of G protein signaling, transcriptional control, and modulation of blood pressure. Pdc is negatively regulated by phosphorylation followed by binding to the 14-3-3 protein, whose role is still unclear. To gain insight into the role of 14-3-3 in the regulation of Pdc function, we studied structural changes of Pdc induced by phosphorylation and 14-3-3 protein binding using time-resolved fluorescence spectroscopy.Our data show that the phosphorylation of the N-terminal domain of Pdc at Ser-54 and Ser-73 affects the structure of the whole Pdc molecule. Complex formation with 14-3-3 reduces the flexibility of both the N- and C-terminal domains of phosphorylated Pdc, as determined by time-resolved tryptophan and dansyl fluorescence

Název v anglickém jazyce

Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding

Popis výsledku anglicky

Phosducin (Pdc), a highly conserved phosphoprotein, plays an important role in the regulation of G protein signaling, transcriptional control, and modulation of blood pressure. Pdc is negatively regulated by phosphorylation followed by binding to the 14-3-3 protein, whose role is still unclear. To gain insight into the role of 14-3-3 in the regulation of Pdc function, we studied structural changes of Pdc induced by phosphorylation and 14-3-3 protein binding using time-resolved fluorescence spectroscopy.Our data show that the phosphorylation of the N-terminal domain of Pdc at Ser-54 and Ser-73 affects the structure of the whole Pdc molecule. Complex formation with 14-3-3 reduces the flexibility of both the N- and C-terminal domains of phosphorylated Pdc, as determined by time-resolved tryptophan and dansyl fluorescence

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GAP305%2F11%2F0708" target="_blank" >GAP305/11/0708: Úloha proteinu 14-3-3 na regulaci funkce fosducinu</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Biophysical Journal

ISSN

0006-3495

e-ISSN

—

Svazek periodika

103

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

1960-1969

Kód UT WoS článku

000310785300023

EID výsledku v databázi Scopus

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