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Functional Analysis of Dishevelled-3 Phosphorylation Identifies Distinct Mechanisms Driven by Casein Kinase 1 epsilon and Frizzled5

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F14%3A00074125" target="_blank" >RIV/00216224:14310/14:00074125 - isvavai.cz</a>

  • Alternative codes found

    RIV/68081707:_____/14:00435068

  • Result on the web

    <a href="http://www.ncbi.nlm.nih.gov/pubmed/24993822" target="_blank" >http://www.ncbi.nlm.nih.gov/pubmed/24993822</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1074/jbc.M114.590638" target="_blank" >10.1074/jbc.M114.590638</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Functional Analysis of Dishevelled-3 Phosphorylation Identifies Distinct Mechanisms Driven by Casein Kinase 1 epsilon and Frizzled5

  • Original language description

    Background: Phosphorylation of Dishevelled (Dvl) by casein kinase 1E (CK1E) is a key event in Wnt signal transduction. Results: Dvl3 residues phosphorylated by CK1E were identified by proteomics and analyzed functionally. Conclusion: Individual phosphorylation events control different aspects of Dvl biology. Significance: CK1E and Fzd5, a Wnt receptor, act on Dvl via distinct mechanism, suggesting that CK1E is not directly downstream of Frizzled5. Dishevelled-3 (Dvl3), a key component of the Wnt signaling pathways, acts downstream of Frizzled (Fzd) receptors and gets heavily phosphorylated in response to pathway activation by Wnt ligands. Casein kinase 1E (CK1E) was identified as the major kinase responsible for Wnt-induced Dvl3 phosphorylation. Currently it is not clear which Dvl residues are phosphorylated and what is the consequence of individual phosphorylation events.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2014

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Biological Chemistry

  • ISSN

    0021-9258

  • e-ISSN

  • Volume of the periodical

    289

  • Issue of the periodical within the volume

    34

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    14

  • Pages from-to

    23520-23533

  • UT code for WoS article

    000341505000023

  • EID of the result in the Scopus database