Intrinsically Disordered Domain of Kinesin-3 Kif14 Enables Unique Functional Diversity
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F20%3A00534447" target="_blank" >RIV/86652036:_____/20:00534447 - isvavai.cz</a>
Result on the web
<a href="https://www.biorxiv.org/content/biorxiv/early/2020/01/31/2020.01.30.926501.full.pdf" target="_blank" >https://www.biorxiv.org/content/biorxiv/early/2020/01/31/2020.01.30.926501.full.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.cub.2020.06.039" target="_blank" >10.1016/j.cub.2020.06.039</a>
Alternative languages
Result language
angličtina
Original language name
Intrinsically Disordered Domain of Kinesin-3 Kif14 Enables Unique Functional Diversity
Original language description
In addition to their force-generating motor domains, kinesin motor proteins feature various accessory domains enabling them to fulfill a variety of functions in the cell. Human kinesin-3, Kif14, localizes to the midbody of the mitotic spindle and is involved in the progression of cytokinesis. The specific motor properties enabling Kif14's cellular functions, however, remain unknown. Here, we show in vitro that the intrinsically disordered N-terminal domain of Kif14 enables unique functional diversity of the kinesin. Using single molecule TIRF microscopy, we found that Kif14 exists either as a diffusible monomer or as processive dimer and that the disordered domain (1) enables diffusibility of the monomeric Kif14, (2) renders the dimeric Kif14 super-processive and enables the kinesin to pass through highly crowded areas, (3) enables robust, autonomous Kif14 tracking of growing microtubule tips, independent of microtubule end-binding (EB) proteins, and (4) is sufficient to enable crosslinking of parallel microtubules and necessary to enable Kif14-driven sliding of antiparallel ones. We explain these features of Kif14 by the observed diffusible interaction of the disordered domain with the microtubule lattice and the observed increased affinity of the disordered domain for GTP-bound tubulin. We suggest that the disordered domain tethers the motor domain to the microtubule providing a diffusible foothold and a regulatory hub, tuning the kinesin's interaction with microtubules. Our findings thus exemplify pliable protein tethering as a fundamental mechanism of molecular motor regulation.
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
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
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
Current Biology
ISSN
0960-9822
e-ISSN
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Volume of the periodical
30
Issue of the periodical within the volume
17
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
3342-3351
UT code for WoS article
000577931900006
EID of the result in the Scopus database
2-s2.0-85088373820