Intrinsically Disordered Domain of Kinesin-3 Kif14 Enables
Unique Functional Diversity

J 2020

Intrinsically Disordered Domain of Kinesin-3 Kif14 Enables Unique Functional Diversity

ZHERNOV, Ilia; Stefan DIEZ; Marcus BRAUN a Zdenek LANSKY

Základní údaje

Originální název

Intrinsically Disordered Domain of Kinesin-3 Kif14 Enables Unique Functional Diversity

Autoři

ZHERNOV, Ilia; Stefan DIEZ; Marcus BRAUN a Zdenek LANSKY

Vydání

Current Biology, CAMBRIDGE, CELL PRESS, 2020, 0960-9822

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 10.834

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:90043/20:00139215

Organizační jednotka

CIISB

DOI

https://doi.org/10.1016/j.cub.2020.06.039

UT WoS

000577931900006

Klíčová slova anglicky

MICROTUBULE CROSS-LINKING; SINGLE MICROTUBULES; PROCESSIVE MOTOR; PROTEIN; PREDICTION; MOTILITY; TUBULIN; BINDING; PRC1; RECONSTITUTION

Štítky

ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 3. 2025 20:22, Mgr. Eva Dubská

Anotace

V originále

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.

Návaznosti

90043, velká výzkumná infrastruktura

Název: CIISB

Citovat

ZHERNOV, Ilia; Stefan DIEZ; Marcus BRAUN a Zdenek LANSKY. Intrinsically Disordered Domain of Kinesin-3 Kif14 Enables Unique Functional Diversity. Current Biology. CAMBRIDGE: CELL PRESS, 2020, roč. 30, č. 17, s. 3342-3356. ISSN 0960-9822. Dostupné z: https://doi.org/10.1016/j.cub.2020.06.039.

@article{2487325,
   author = {Zhernov, Ilia and Diez, Stefan and Braun, Marcus and Lansky, Zdenek},
   article_location = {CAMBRIDGE},
   article_number = {17},
   doi = {https://doi.org/10.1016/j.cub.2020.06.039},
   keywords = {MICROTUBULE CROSS-LINKING; SINGLE MICROTUBULES; PROCESSIVE MOTOR; PROTEIN; PREDICTION; MOTILITY; TUBULIN; BINDING; PRC1; RECONSTITUTION},
   language = {eng},
   issn = {0960-9822},
   journal = {Current Biology},
   title = {Intrinsically Disordered Domain of Kinesin-3 Kif14 Enables Unique Functional Diversity},
   url = {https://www.sciencedirect.com/science/article/pii/S0960982220308551?via%3Dihub},
   volume = {30},
   year = {2020}
}

TY  - JOUR
ID  - 2487325
AU  - Zhernov, Ilia - Diez, Stefan - Braun, Marcus - Lansky, Zdenek
PY  - 2020
TI  - Intrinsically Disordered Domain of Kinesin-3 Kif14 Enables Unique Functional Diversity
JF  - Current Biology
VL  - 30
IS  - 17
SP  - 3342-3356
EP  - 3342-3356
PB  - CELL PRESS
SN  - 09609822
KW  - MICROTUBULE CROSS-LINKING
KW  - SINGLE MICROTUBULES
KW  - PROCESSIVE MOTOR
KW  - PROTEIN
KW  - PREDICTION
KW  - MOTILITY
KW  - TUBULIN
KW  - BINDING
KW  - PRC1
KW  - RECONSTITUTION
UR  - https://www.sciencedirect.com/science/article/pii/S0960982220308551?via%3Dihub
N2  - 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.
ER  -

ZHERNOV, Ilia; Stefan DIEZ; Marcus BRAUN a Zdenek LANSKY. Intrinsically Disordered Domain of Kinesin-3 Kif14 Enables Unique Functional Diversity. \textit{Current Biology}. CAMBRIDGE: CELL PRESS, 2020, roč.~30, č.~17, s.~3342-3356. ISSN~0960-9822. Dostupné z: https://doi.org/10.1016/j.cub.2020.06.039.

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