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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