The tyrosine Y250 2.39 in Frizzled 4 defines a conserved motif
important for structural integrity of the receptor and
recruitment of Disheveled.

J 2017

The tyrosine Y250 2.39 in Frizzled 4 defines a conserved motif important for structural integrity of the receptor and recruitment of Disheveled.

STRAKOVÁ, Kateřina; Pierre MATRICON; Chika YOKOTA; Elisa ARTHOFER; Ondřej BERNATÍK et al.

Základní údaje

Originální název

The tyrosine Y250 2.39 in Frizzled 4 defines a conserved motif important for structural integrity of the receptor and recruitment of Disheveled.

Autoři

STRAKOVÁ, Kateřina; Pierre MATRICON; Chika YOKOTA; Elisa ARTHOFER; Ondřej BERNATÍK; David RODRIGUEZ; Ernesto ARENAS CASES; Jens CARLSSON; Vítězslav BRYJA a Gunnar SCHULTE

Vydání

Cellular Signalling, New York, ELSEVIER SCIENCE, 2017, 0898-6568

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

30105 Physiology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.487

Kód RIV

RIV/00216224:14310/17:00095350

Organizační jednotka

Přírodovědecká fakulta

DOI

https://doi.org/10.1016/j.cellsig.2017.06.018

UT WoS

000408788800009

EID Scopus

2-s2.0-85021746143

Klíčová slova anglicky

Disheveled; DVL2; Frizzled; FZD(4); GNA12; GNA13

Štítky

NZ, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 12. 4. 2018 15:17, Ing. Nicole Zrilić

Anotace

V originále

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.

Návaznosti

EE2.3.20.0180, projekt VaV

Název: Spolupráce mezi Masarykovou univerzitou a Karolinska Institutet, Stockholm na poli biomedicíny

GA13-32990S, projekt VaV

Název: Posttranslační modifikace receptorů na buněčném povrchu jako určující faktor pro specificitu signálu

Investor: Grantová agentura ČR, Posttranslační modifikace receptorů na buněčném povrchu jako určující faktor pro specificitu signálu

Citovat

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://doi.org/10.1016/j.cellsig.2017.06.018.

@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 = {https://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://doi.org/10.1016/j.cellsig.2017.06.018.

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