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Fatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling

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    SYSNO ASEP0364988
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleFatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling
    Author(s) Doubravská, Lenka (UMG-J)
    Krausová, Michaela (UMG-J) RID
    Gradl, D. (DE)
    Vojtěchová, Martina (UMG-J) RID
    Tůmová, Lucie (UMG-J)
    Lukáš, Jan (UMG-J)
    Valenta, Tomáš (UMG-J)
    Pospíchalová, Vendula (UMG-J)
    Fafílek, Bohumil (UMG-J) RID
    Plachý, Jiří (UMG-J) RID
    Sebesta, O. (CZ)
    Kořínek, Vladimír (UMG-J) RID
    Source TitleCellular Signalling. - : Elsevier - ISSN 0898-6568
    Roč. 23, č. 5 (2011), s. 837-848
    Number of pages12 s.
    Languageeng - English
    CountryGB - United Kingdom
    KeywordsWnt signaling ; post-translational modification ; acylation
    Subject RIVEB - Genetics ; Molecular Biology
    R&D ProjectsGA204/07/1567 GA ČR - Czech Science Foundation (CSF)
    1M0506 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    CEZAV0Z50520514 - UMG-J (2005-2011)
    UT WOS000288977400011
    DOI10.1016/j.cellsig.2011.01.007
    AnnotationMammalian Wnt ligands contain two types of post-translational modification: the covalent attachment of fatty acids at two distinct positions, and the N-glycosylation of multiple asparagines. We examined how these modifications contribute to the secretion, extracellular movement and signaling activity of mouse Wnt1 and Wnt3a ligands. We revealed that O-linked acylation of serine is required for the subsequent S-palmitoylation of cysteine. Interestingly, although double-acylation of Wnt1 was indispensable for signaling in mammalian cells, in Xenopus embryos the S-palmitoyl-deficient form retained the signaling activity. In the case of Wnt3a, the functional duality of the attached acyls was less prominent, since the ligand lacking S-linked palmitate was still capable of signaling in various cellular contexts. Finally, we show that the signaling competency of both Wnt1 and Wnt3a is related to their ability to associate with the extracellular matrix.
    WorkplaceInstitute of Molecular Genetics
    ContactNikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217
    Year of Publishing2012
Number of the records: 1  

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