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Diffusive tail anchorage determines velocity and force produced by kinesin-14 between crosslinked microtubules

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F18%3A00491034" target="_blank" >RIV/86652036:_____/18:00491034 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1038/s41467-018-04656-0" target="_blank" >http://dx.doi.org/10.1038/s41467-018-04656-0</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/s41467-018-04656-0" target="_blank" >10.1038/s41467-018-04656-0</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Diffusive tail anchorage determines velocity and force produced by kinesin-14 between crosslinked microtubules

  • Original language description

    Form and function of the mitotic spindle depend on motor proteins that crosslink microtubules and move them relative to each other. Among these are kinesin-14s, such as Ncd, which interact with one microtubule via their non-processive motor domains and with another via their diffusive tail domains, the latter allowing the protein to slip along the microtubule surface. Little is known about the influence of the tail domains on the protein's performance. Here, we show that diffusive anchorage of Ncd's tail domains impacts velocity and force considerably. Tail domain slippage reduced velocities from 270 nm s-1 to 60 nm s-1 and forces from several piconewtons to the sub-piconewton range. These findings challenge the notion that kinesin-14 may act as an antagonizer of other crosslinking motors, such as kinesin-5, during mitosis. It rather suggests a role of kinesin-14 as a flexible element, pliantly sliding and crosslinking microtubules to facilitate remodeling of the mitotic spindle.

  • 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

    10610 - Biophysics

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

    2018

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Nature Communications

  • ISSN

    2041-1723

  • e-ISSN

  • Volume of the periodical

    9

  • Issue of the periodical within the volume

    JUN 7 2018

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    9

  • Pages from-to

  • UT code for WoS article

    000434379800011

  • EID of the result in the Scopus database

    2-s2.0-85048211823