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Dishevelled is a NEK2 kinase substrate controlling dynamics of centrosomal linker proteins

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F16%3A00471960" target="_blank" >RIV/68081707:_____/16:00471960 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14310/16:00088644

  • Result on the web

    <a href="http://dx.doi.org/10.1073/pnas.1608783113" target="_blank" >http://dx.doi.org/10.1073/pnas.1608783113</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1073/pnas.1608783113" target="_blank" >10.1073/pnas.1608783113</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Dishevelled is a NEK2 kinase substrate controlling dynamics of centrosomal linker proteins

  • Original language description

    Dishevelled (DVL) is a key scaffolding protein and a branching point in Wnt signaling pathways. Here, we present conclusive evidence that DVL regulates the centrosomal cycle. We demonstrate that DVL dishevelled and axin (DIX) domain, but not DIX domain-mediated multimerization, is essential for DVL's centrosomal localization. DVL accumulates during the cell cycle and associates with NIMA-related kinase 2 (NEK2), which is able to phosphorylate DVL at amultitude of residues, as detected by a set of novel phospho-specific antibodies. This creates interfaces for efficient binding to CDK5 regulatory subunit-associated protein 2 (CDK5RAP2) and centrosomal Nek2-associated protein 1 (C-NAP1), two proteins of the centrosomal linker. Displacement of DVL from the centrosome and its release into the cytoplasm on NEK2 phosphorylation is coupled to the removal of linker proteins, an event necessary for centrosomal separation and proper formation of the mitotic spindle. Lack of DVL prevents NEK2-controlled dissolution of loose centrosomal linker and subsequent centrosomal separation. Increased DVL levels, in contrast, sequester centrosomal NEK2 and mimic monopolar spindle defects induced by a dominant negative version of this kinase. Our study thus uncovers molecular crosstalk between centrosome and Wnt signaling.

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    BO - Biophysics

  • OECD FORD branch

Result continuities

  • Project

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

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2016

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Proceedings of the National Academy of Sciences of the United States of America

  • ISSN

    0027-8424

  • e-ISSN

  • Volume of the periodical

    113

  • Issue of the periodical within the volume

    33

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    6

  • Pages from-to

    9304-9309

  • UT code for WoS article

    000381399200059

  • EID of the result in the Scopus database