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@article{1173918,
author = {Kříž, Vítězslav and Pospíchalová, Vendula and Mašek, Jan and Kilander, Michaela Brita Christina and Slavik, Josef and Tanneberger, Kristina and Schulte, Gunnar and Mchala, Miroslav and Kozubík, Alois and Behrens, Jurgen and Bryja, Vítězslav},
article_location = {Rockville},
article_number = {2},
doi = {http://dx.doi.org/10.1074/jbc.M113.498444},
keywords = {CONVERGENT EXTENSION MOVEMENTS; SIGNALING PATHWAYS; IN-VIVO; CATENIN; ACTIVATION; BETA-ARRESTIN-2; DVL; APC; ENDOCYTOSIS; MECHANISM},
language = {eng},
issn = {0021-9258},
journal = {Journal of Biological Chemistry},
title = {beta-Arrestin Promotes Wnt-induced Low Density Lipoprotein Receptor-related Protein 6 (Lrp6) Phosphorylation via Increased Membrane Recruitment of Amer1 Protein},
url = {https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3887180/},
volume = {289},
year = {2014}
}
TY - JOUR
ID - 1173918
AU - Kříž, Vítězslav - Pospíchalová, Vendula - Mašek, Jan - Kilander, Michaela Brita Christina - Slavik, Josef - Tanneberger, Kristina - Schulte, Gunnar - Mchala, Miroslav - Kozubík, Alois - Behrens, Jurgen - Bryja, Vítězslav
PY - 2014
TI - beta-Arrestin Promotes Wnt-induced Low Density Lipoprotein Receptor-related Protein 6 (Lrp6) Phosphorylation via Increased Membrane Recruitment of Amer1 Protein
JF - Journal of Biological Chemistry
VL - 289
IS - 2
SP - 1128-1141
EP - 1128-1141
PB - The American Society for Biochemistry and Molecular Biology
SN - 00219258
KW - CONVERGENT EXTENSION MOVEMENTS
KW - SIGNALING PATHWAYS
KW - IN-VIVO
KW - CATENIN
KW - ACTIVATION
KW - BETA-ARRESTIN-2
KW - DVL
KW - APC
KW - ENDOCYTOSIS
KW - MECHANISM
UR - https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3887180/
N2 - 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 first time 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. Finally, we show that beta-arrestin interacts with PtdIns kinases PI4KII alpha and PIP5KI beta. Importantly, cells lacking beta-arrestin showed higher steady-state levels of the relevant PtdInsP and were unable to increase levels of these PtdInsP in response to Wnt3a. In summary, our data show that beta-arrestins regulate Wnt3a-induced Lrp6 phosphorylation by the regulation of the membrane dynamics of Amer1. We propose that beta-arrestins via their scaffolding function facilitate Amer1 interaction with PtdIns(4,5)P-2, which is produced locally upon Wnt3a stimulation by beta-arrestin- and Dishevelled-associated kinases.
ER -
KŘÍŽ, Vítězslav, Vendula POSPÍCHALOVÁ, Jan MAŠEK, Michaela Brita Christina KILANDER, Josef SLAVIK, Kristina TANNEBERGER, Gunnar SCHULTE, Miroslav MCHALA, Alois KOZUBÍK, Jurgen BEHRENS a Vítězslav BRYJA. beta-Arrestin Promotes Wnt-induced Low Density Lipoprotein Receptor-related Protein 6 (Lrp6) Phosphorylation via Increased Membrane Recruitment of Amer1 Protein. \textit{Journal of Biological Chemistry}. Rockville: The American Society for Biochemistry and Molecular Biology, roč.~289, č.~2, s.~1128-1141. ISSN~0021-9258. doi:10.1074/jbc.M113.498444. 2014.
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