Changes in microtubule overlap length regulate kinesin-14-driven microtubule sliding
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F17%3A00484511" target="_blank" >RIV/86652036:_____/17:00484511 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1038/NCHEMBIO.2495" target="_blank" >http://dx.doi.org/10.1038/NCHEMBIO.2495</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/NCHEMBIO.2495" target="_blank" >10.1038/NCHEMBIO.2495</a>
Alternative languages
Result language
angličtina
Original language name
Changes in microtubule overlap length regulate kinesin-14-driven microtubule sliding
Original language description
Microtubule-crosslinking motor proteins, which slide antiparallel microtubules, are required for the remodeling of microtubule networks. Hitherto, all microtubule-crosslinking motors have been shown to slide microtubules at a constant velocity until no overlap remains between them, leading to the breakdown of the initial microtubule geometry. Here, we show in vitro that the sliding velocity of microtubules, driven by human kinesin-14 HSET, decreases when microtubules start to slide apart, resulting in the maintenance of finite-length microtubule overlaps. We quantitatively explain this feedback using the local interaction kinetics of HSET with overlapping microtubules that cause retention of HSET in shortening overlaps. Consequently, the increased HSET density in the overlaps leads to a density-dependent decrease in sliding velocity and the generation of an entropic force that antagonizes the force exerted by the motors. Our results demonstrate that a spatial arrangement of microtubules can regulate the collective action of molecular motors through the local alteration of their individual interaction kinetics.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Chemical Biology
ISSN
1552-4450
e-ISSN
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Volume of the periodical
13
Issue of the periodical within the volume
12
Country of publishing house
US - UNITED STATES
Number of pages
8
Pages from-to
1245-1252
UT code for WoS article
000415917900008
EID of the result in the Scopus database
2-s2.0-85034815412