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Phosphorylation of multiple proteins involved in ciliogenesis by Tau Tubulin Kinase 2

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F20%3A00114077" target="_blank" >RIV/00216224:14110/20:00114077 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.molbiolcell.org/doi/10.1091/mbc.E19-06-0334" target="_blank" >https://www.molbiolcell.org/doi/10.1091/mbc.E19-06-0334</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1091/mbc.E19-06-0334" target="_blank" >10.1091/mbc.E19-06-0334</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Phosphorylation of multiple proteins involved in ciliogenesis by Tau Tubulin Kinase 2

  • Original language description

    Primary cilia are organelles necessary for proper implementation of developmental and homeostasis processes. To initiate their assembly, coordinated actions of multiple proteins are needed. Tau tubulin kinase 2 (TTBK2) is a key player in the cilium assembly pathway, controlling the final step of cilia initiation. The function of TTBK2 in ciliogenesis is critically dependent on its kinase activity; however, the precise mechanism of TTBK2 action has so far not been fully understood due to the very limited information about its relevant substrates. In this study, we demonstrate that CEP83, CEP89, CCDC92, Rabin8, and DVL3 are substrates of TTBK2 kinase activity. Further, we characterize a set of phosphosites of those substrates and CEP164 induced by TTBK2 in vitro and in vivo. Intriguingly, we further show that identified TTBK2 phosphosites and consensus sequence delineated from those are distinct from motifs previously assigned to TTBK2. Finally, we show that TTBK2 is also required for efficient phosphorylation of many S/T sites in CEP164 and provide evidence that TTBK2-induced phosphorylations of CEP164 modulate its function, which in turn seems relevant for the process of cilia formation. In summary, our work provides important insight into the substrates-TTBK2 kinase relationship and suggests that phosphorylation of substrates on multiple sites by TTBK2 is probably involved in the control of ciliogenesis in human cells.

  • Czech name

    —

  • Czech description

    —

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

    —

  • OECD FORD branch

    10601 - Cell biology

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>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Molecular Biology of the Cell

  • ISSN

    1059-1524

  • e-ISSN

    1939-4586

  • Volume of the periodical

    31

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    15

  • Pages from-to

    1032-1046

  • UT code for WoS article

    000530664800004

  • EID of the result in the Scopus database

    2-s2.0-85084961482