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Flagellar microtubule doublet assembly in vitro reveals a regulatory role of tubulin C-terminal tails

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F19%3A00521410" target="_blank" >RIV/86652036:_____/19:00521410 - isvavai.cz</a>

  • Result on the web

    <a href="https://science.sciencemag.org/content/363/6424/285" target="_blank" >https://science.sciencemag.org/content/363/6424/285</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1126/science.aav2567" target="_blank" >10.1126/science.aav2567</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Flagellar microtubule doublet assembly in vitro reveals a regulatory role of tubulin C-terminal tails

  • Original language description

    Microtubule doublets (MTDs), consisting of an incomplete B-microtubule at the surface of a complete A-microtubule, provide a structural scaffold mediating intraflagellar transport and ciliary beating. Despite the fundamental role of MTDs, the molecular mechanism governing their formation is unknown. We used a cell-free assay to demonstrate a crucial inhibitory role of the carboxyl-terminal (C-terminal) tail of tubulin in MTD assembly. Removal of the C-terminal tail of an assembled A-microtubule allowed for the nucleation of a B-microtubule on its surface. C-terminal tails of only one A-microtubule protofilament inhibited this side-to-surface tubulin interaction, which would be overcome in vivo with binding protein partners. The dynamics of B-microtubule nucleation and its distinctive isotropic elongation was elucidated by using live imaging. Thus, inherent interaction properties of tubulin provide a structural basis driving flagellar MTD assembly.

  • 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

    10608 - Biochemistry and molecular 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)

Others

  • Publication year

    2019

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Science

  • ISSN

    0036-8075

  • e-ISSN

  • Volume of the periodical

    363

  • Issue of the periodical within the volume

    6424

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    4

  • Pages from-to

    285-288

  • UT code for WoS article

    000456140700037

  • EID of the result in the Scopus database