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Dishevelled-3 conformation dynamics analyzed by FRET-based biosensors reveals a key role of casein kinase 1
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SYSNO ASEP 0520259 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Dishevelled-3 conformation dynamics analyzed by FRET-based biosensors reveals a key role of casein kinase 1 Author(s) Harnoš, J. (CZ)
Canizal, M.C.A. (DE)
Jurasek, M. (CZ)
Kumar, J. (CZ)
Holler, C. (DE)
Schambony, A. (DE)
Hanakova, K. (CZ)
Bernatík, O. (CZ)
Zdráhal, Z. (CZ)
Gomoryova, K. (CZ)
Gybel, T. (CZ)
Radaszkiewicz, T.W. (CZ)
Kravec, M. (CZ)
Trantírek, Lukáš (BFU-R)
Ryneš, J. (CZ)
Dave, Z. (CZ)
Fernandez-Llamazares, A.I. (NL)
Vácha, R. (CZ)
Tripsianes, K. (CZ)
Hoffmann, C. (DE)
Bryja, Vítězslav (BFU-R) RID, ORCIDNumber of authors 21 Article number 1804 Source Title Nature Communications. - : Nature Publishing Group
Roč. 10, APR 2019 (2019)Number of pages 18 s. Publication form Online - E Language eng - English Country GB - United Kingdom Keywords particle mesh ewald ; beta-catenin ; wnt/beta-catenin ; dix domain Subject RIV CE - Biochemistry OECD category Biochemical research methods R&D Projects EF15_003/0000477 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support BFU-R - RVO:68081707 UT WOS 000464979000002 DOI 10.1038/s41467-019-09651-7 Annotation Dishevelled (DVL) is the key component of the Wnt signaling pathway. Currently, DVL conformational dynamics under native conditions is unknown. To overcome this limitation, we develop the Fluorescein Arsenical Hairpin Binder- (FlAsH-) based FRET in vivo approach to study DVL conformation in living cells. Using this single-cell FRET approach, we demonstrate that (i) Wnt ligands induce open DVL conformation, (ii) DVL variants that are predominantly open, show more even subcellular localization and more efficient membrane recruitment by Frizzled (FZD) and (iii) Casein kinase 1 epsilon (CK1 epsilon) has a key regulatory function in DVL conformational dynamics. In silico modeling and in vitro biophysical methods explain how CK1 epsilon-specific phosphorylation events control DVL conformations via modulation of the PDZ domain and its interaction with DVL C-terminus. In summary, our study describes an experimental tool for DVL conformational sampling in living cells and elucidates the essential regulatory role of CK1 epsilon in DVL conformational dynamics. Workplace Institute of Biophysics Contact Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Year of Publishing 2020 Electronic address https://www.nature.com/articles/s41467-019-09651-7.pdf
Number of the records: 1