beta-Arrestin Promotes Wnt-induced Low Density Lipoprotein Receptor-related Protein 6 (Lrp6) Phosphorylation via Increased Membrane Recruitment of Amer1 Protein

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F14%3A00073566" target="_blank" >RIV/00216224:14310/14:00073566 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68081707:_____/14:00427976 RIV/68378050:_____/14:00427976 RIV/00027162:_____/14:#0001172

Výsledek na webu

<a href="http://dx.doi.org/10.1074/jbc.M113.498444" target="_blank" >http://dx.doi.org/10.1074/jbc.M113.498444</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.M113.498444" target="_blank" >10.1074/jbc.M113.498444</a>

Jazyk výsledku

angličtina

Název v původním jazyce

beta-Arrestin Promotes Wnt-induced Low Density Lipoprotein Receptor-related Protein 6 (Lrp6) Phosphorylation via Increased Membrane Recruitment of Amer1 Protein

Popis výsledku v původním jazyce

beta-Arrestin is a scaffold protein that regulates signal transduction by seven transmembrane-spanning receptors. Among other functions it is also critically required for Wnt/beta-catenin signal transduction. In the present study we provide for the firsttime a mechanistic basis for the beta-arrestin function in Wnt/beta-catenin signaling. We demonstrate that beta-arrestin is required for efficient Wnt3a-induced Lrp6 phosphorylation, a key event in downstream signaling. beta-Arrestin regulates Lrp6 phosphorylation via a novel interaction with phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P-2)-binding protein Amer1/WTX/Fam123b. Amer1 has been shown very recently to bridge Wnt-induced and Dishevelled-associated PtdIns(4,5)P-2 production to the phosphorylation of Lrp6. Using fluorescence recovery after photobleaching we show here that beta-arrestin is required for the Wnt3a-induced Amer1 membrane dynamics and downstream signaling.

Název v anglickém jazyce

beta-Arrestin Promotes Wnt-induced Low Density Lipoprotein Receptor-related Protein 6 (Lrp6) Phosphorylation via Increased Membrane Recruitment of Amer1 Protein

Popis výsledku anglicky

beta-Arrestin is a scaffold protein that regulates signal transduction by seven transmembrane-spanning receptors. Among other functions it is also critically required for Wnt/beta-catenin signal transduction. In the present study we provide for the firsttime a mechanistic basis for the beta-arrestin function in Wnt/beta-catenin signaling. We demonstrate that beta-arrestin is required for efficient Wnt3a-induced Lrp6 phosphorylation, a key event in downstream signaling. beta-Arrestin regulates Lrp6 phosphorylation via a novel interaction with phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P-2)-binding protein Amer1/WTX/Fam123b. Amer1 has been shown very recently to bridge Wnt-induced and Dishevelled-associated PtdIns(4,5)P-2 production to the phosphorylation of Lrp6. Using fluorescence recovery after photobleaching we show here that beta-arrestin is required for the Wnt3a-induced Amer1 membrane dynamics and downstream signaling.

Druh

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

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

Projekt

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

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

Rok uplatnění

2014

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

289

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

14

Strana od-do

1128-1141

Kód UT WoS článku

000330541200044

EID výsledku v databázi Scopus

—