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@article{1504861,
author = {Straková, Kateřina and KowalskiandJahn, M. and Gybeľ, Tomáš and Valnohová, Jana and Dhople, V.M. and Harnoš, Jakub and Bernatík, Ondřej and Ganji, Sri Ranjani and Zdráhal, Zbyněk and Mulder, J. and Lindskog, C. and Bryja, Vítězslav and Schulte, G.},
article_location = {Bethesda, USA},
article_number = {48},
doi = {http://dx.doi.org/10.1074/jbc.RA118.004656},
keywords = {DEP DOMAIN; FUNCTIONAL-ANALYSIS; PLANAR POLARITY; BETA-ARRESTINS; DIX DOMAIN; I-EPSILON; RECEPTOR; RECRUITMENT; COMPLEX; GROWTH},
language = {eng},
issn = {0021-9258},
journal = {Journal of Biological Chemistry},
title = {Dishevelled enables casein kinase 1-mediated phosphorylation of Frizzled 6 required for cell membrane localization},
volume = {293},
year = {2018}
}
TY - JOUR
ID - 1504861
AU - Straková, Kateřina - Kowalski-Jahn, M. - Gybeľ, Tomáš - Valnohová, Jana - Dhople, V.M. - Harnoš, Jakub - Bernatík, Ondřej - Ganji, Sri Ranjani - Zdráhal, Zbyněk - Mulder, J. - Lindskog, C. - Bryja, Vítězslav - Schulte, G.
PY - 2018
TI - Dishevelled enables casein kinase 1-mediated phosphorylation of Frizzled 6 required for cell membrane localization
JF - Journal of Biological Chemistry
VL - 293
IS - 48
SP - 18477-18493
EP - 18477-18493
PB - Amer. Soc. Biochem. Mol. Biol.
SN - 00219258
KW - DEP DOMAIN
KW - FUNCTIONAL-ANALYSIS
KW - PLANAR POLARITY
KW - BETA-ARRESTINS
KW - DIX DOMAIN
KW - I-EPSILON
KW - RECEPTOR
KW - RECRUITMENT
KW - COMPLEX
KW - GROWTH
N2 - Frizzleds (FZDs) are receptors for secreted lipoglycoproteins of the Wingless/Int-1(WNT) family, initiating an important signal transduction network in multicellular organisms. FZDs are G protein-coupled receptors (GPCRs), which are well known to be regulated by phosphorylation, leading to specific downstream signaling or receptor desensitization. The role and underlying mechanisms of FZD phosphorylation remain largely unexplored. Here, we investigated the phosphorylation of human FZD(6). Using MS analysis and a phospho-state- and -site-specific antibody, we found that Ser-648, located in the FZD(6) C terminus, is efficiently phosphorylated by casein kinase 1 is an element of (CK1 is an element of) and that this phosphorylation requires the scaffolding protein Dishevelled (DVL). In an overexpression system, DVL1, -2, and -3 promoted CK1-mediated FZD(6) phosphorylation on Ser-648. This DVL activity required an intact DEP domain and FZD-mediated recruitment of this domain to the cell membrane. Substitution of the CK1 is an element of-targeted phosphomo-tif reduced FZD(6) surface expression, suggesting that Ser-648 phosphorylation controls membrane trafficking of FZD(6). Phos-pho-Ser-648 FZD(6) immunoreactivity in human fallopian tube epithelium was predominantly apical, associated with cilia in a subset of epithelial cells, compared with the total FZD(6) protein expression, suggesting that FZD(6) phosphorylation contributes to asymmetric localization of receptor function within the cell and to epithelial polarity. Given the key role of FZD(6) in planar cell polarity, our results raise the possibility that asymmetric phosphorylation of FZD(6) rather than asymmetric protein distribution accounts for polarized receptor signaling.
ER -
STRAKOVÁ, Kateřina, M. KOWALSKI-JAHN, Tomáš GYBEĽ, Jana VALNOHOVÁ, V.M. DHOPLE, Jakub HARNOŠ, Ondřej BERNATÍK, Sri Ranjani GANJI, Zbyněk ZDRÁHAL, J. MULDER, C. LINDSKOG, Vítězslav BRYJA and G. SCHULTE. Dishevelled enables casein kinase 1-mediated phosphorylation of Frizzled 6 required for cell membrane localization. \textit{Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2018, vol.~293, No~48, p.~18477-18493. ISSN~0021-9258. Available from: https://dx.doi.org/10.1074/jbc.RA118.004656.
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