| STRAKOVÁ, Kateřina, Pierre MATRICON, Chika YOKOTA, Elisa ARTHOFER, Ondřej BERNATÍK, David RODRIGUEZ, Ernesto ARENAS CASES, Jens CARLSSON, Vítězslav BRYJA a Gunnar SCHULTE. The tyrosine Y250 2.39 in Frizzled 4 defines a conserved motif important for structural integrity of the receptor and recruitment of Disheveled. Cellular Signalling. New York: ELSEVIER SCIENCE, 2017, roč. 38, October, s. 85-96. ISSN 0898-6568. Dostupné z: https://dx.doi.org/10.1016/j.cellsig.2017.06.018. |
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@article{1402056,
author = {Straková, Kateřina and Matricon, Pierre and Yokota, Chika and Arthofer, Elisa and Bernatík, Ondřej and Rodriguez, David and Arenas Cases, Ernesto and Carlsson, Jens and Bryja, Vítězslav and Schulte, Gunnar},
article_location = {New York},
article_number = {October},
doi = {http://dx.doi.org/10.1016/j.cellsig.2017.06.018},
keywords = {Disheveled; DVL2; Frizzled; FZD(4); GNA12; GNA13},
language = {eng},
issn = {0898-6568},
journal = {Cellular Signalling},
title = {The tyrosine Y250 2.39 in Frizzled 4 defines a conserved motif important for structural integrity of the receptor and recruitment of Disheveled.},
url = {http://www.sciencedirect.com/science/article/pii/S0898656817301766?via%3Dihub},
volume = {38},
year = {2017}
}
TY - JOUR
ID - 1402056
AU - Straková, Kateřina - Matricon, Pierre - Yokota, Chika - Arthofer, Elisa - Bernatík, Ondřej - Rodriguez, David - Arenas Cases, Ernesto - Carlsson, Jens - Bryja, Vítězslav - Schulte, Gunnar
PY - 2017
TI - The tyrosine Y250 2.39 in Frizzled 4 defines a conserved motif important for structural integrity of the receptor and recruitment of Disheveled.
JF - Cellular Signalling
VL - 38
IS - October
SP - 85-96
EP - 85-96
PB - ELSEVIER SCIENCE
SN - 08986568
KW - Disheveled
KW - DVL2
KW - Frizzled
KW - FZD(4)
KW - GNA12
KW - GNA13
UR - http://www.sciencedirect.com/science/article/pii/S0898656817301766?via%3Dihub
L2 - http://www.sciencedirect.com/science/article/pii/S0898656817301766?via%3Dihub
N2 - Frizzleds (FZDs) are unconventional G protein-coupled receptors, which activate diverse intracellular signaling pathways via the phosphoprotein Disheveled (DVL) and heterotrimeric G proteins. The interaction interplay of FZDs with DVL and G proteins is complex, involves different regions of FZD and the potential dynamics are poorly understood. In the present study, we aimed to characterize the function of a highly conserved tyrosine (Y2502.39) in the intracellular loop 1 (IL1) of human FZD4. We have found Y2502.39 to be crucial for DVL2 interaction and DVL2 translocation to the plasma membrane. Mutant FZD4-Y2502.39F, impaired in DVL2 binding, was defective in both beta-catenin-dependent and beta-catenin-independent WNT signaling induced in Xenopus laevis embryos. The same mutant maintained interaction with the heterotrimeric G proteins Galfa12 and Galfa13 and was able to mediate WNT-induced G protein dissociation and G protein-dependent YAP/TAZ signaling. We conclude from modeling and dynamics simulation efforts that Y2502.39 is important for the structural integrity of the FZD-DVL, but not for the FZD-G protein interface and hypothesize that the interaction network of Y2502.39 and H3484.46 plays a role in specifying downstream signaling pathways induced by the receptor.
ER -
STRAKOVÁ, Kateřina, Pierre MATRICON, Chika YOKOTA, Elisa ARTHOFER, Ondřej BERNATÍK, David RODRIGUEZ, Ernesto ARENAS CASES, Jens CARLSSON, Vítězslav BRYJA a Gunnar SCHULTE. The tyrosine Y250 2.39 in Frizzled 4 defines a conserved motif important for structural integrity of the receptor and recruitment of Disheveled. \textit{Cellular Signalling}. New York: ELSEVIER SCIENCE, 2017, roč.~38, October, s.~85-96. ISSN~0898-6568. Dostupné z: https://dx.doi.org/10.1016/j.cellsig.2017.06.018.
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