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Sequential activation and inactivation of dishevelled in the Wnt/{beta}-catenin pathway by casein kinases.

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F11%3A00049416" target="_blank" >RIV/00216224:14310/11:00049416 - isvavai.cz</a>

  • Alternative codes found

    RIV/60076658:12310/11:43883032

  • Result on the web

    <a href="http://dx.doi.org/10.1074/jbc.M110.169870" target="_blank" >http://dx.doi.org/10.1074/jbc.M110.169870</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1074/jbc.M110.169870" target="_blank" >10.1074/jbc.M110.169870</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Sequential activation and inactivation of dishevelled in the Wnt/{beta}-catenin pathway by casein kinases.

  • Original language description

    Dishevelled (Dvl) is a key component in the Wnt/beta-catenin signaling pathway. Dvl can multimerize to form dynamic protein aggregates, which are required for the activation of downstream signaling. Upon pathway activation by Wnts, Dvl becomes phosphorylated to yield phosphorylated and shifted-(PS) Dvl. Both activation of Dvl in Wnt/beta-catenin signaling and Wnt-induced PS-Dvl formation are dependent on casein kinase 1 (CK1)delta/epsilon activity. However, the overexpression of CK1 was shown to dissolve Dvl aggregates and endogenous PS-Dvl forms irrespective of whether or not the activating Wnt triggers the Wnt/beta-catenin pathway. Using a combination of gain-of-function, loss-of-function and domain mapping approaches, we attempted to solve this discrepancy regarding the role of CK1epsilon in Dvl biology. We analyzed mutual interaction of CK1delta/epsilon and two other Dvl kinases, CK2 and PAR1, in Wnt/beta-catenin pathway.

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    ED - Physiology

  • 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

    2011

  • 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

    286

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    15

  • Pages from-to

    10396-10410

  • UT code for WoS article

    000288547000056

  • EID of the result in the Scopus database