Kinesin-14 HSET and KlpA are non-processive microtubule motors with load-dependent power strokes

Xinglei Liu; Lu Rao; Weihong Qiu; Florian Berger; Arne Gennerich

doi:10.1038/s41467-024-50990-x

Kinesin-14 HSET and KlpA are non-processive microtubule motors with load-dependent power strokes

Xinglei Liu, Lu Rao, Weihong Qiu, Florian Berger, Arne Gennerich

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Accurate chromosome segregation during cell division relies on coordinated actions of microtubule (MT)-based motor proteins in the mitotic spindle. Kinesin-14 motors play vital roles in spindle assembly and maintenance by crosslinking antiparallel MTs at the spindle midzone and anchoring spindle MTs’ minus ends at the poles. In this study, we investigate the force generation and motility of the Kinesin-14 motors HSET and KlpA. Our findings reveal that both motors are non-processive, producing single load-dependent power strokes per MT encounter, with estimated load-free power strokes of ~30 and ~35 nm, respectively. Each homodimeric motor generates forces of ~0.5 pN, but when assembled in teams, they cooperate to generate forces of 1 pN or more. Notably, the cooperative activity among multiple motors leads to increased MT-sliding velocities. These results quantitatively elucidate the structure-function relationship of Kinesin-14 motors and underscore the significance of cooperative behavior in their cellular functions.

Original language	English
Article number	6564
Number of pages	14
Journal	Nature Communications
Volume	15
Issue number	1
DOIs	https://doi.org/10.1038/s41467-024-50990-x
Publication status	Published - 3 Aug 2024

Bibliographical note

Publisher Copyright:
© The Author(s) 2024.

Funding

The authors would like to thank J. Vanlier and S. Weisenburger from LUMICKS for their helpful discussions on active trap calibration. X. Liu was supported by National Institutes of Health grants R01GM098469 and R01GM127922. L. Rao and A. Gennerich were supported by National Institutes of Health grants R01GM098469 and R01NS114636. W. Qiu was supported by the National Institutes of Health grant 1R01GM127922.

Funders	Funder number
National Institutes of Health	1R01GM127922, R01NS114636, R01GM098469
National Institutes of Health

Keywords

Cross-linking
Crystal-structure
Insights
Mechanisms
Motility
Movement
Ncd
Protein
Rotation
Transport

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abstract = "Accurate chromosome segregation during cell division relies on coordinated actions of microtubule (MT)-based motor proteins in the mitotic spindle. Kinesin-14 motors play vital roles in spindle assembly and maintenance by crosslinking antiparallel MTs at the spindle midzone and anchoring spindle MTs{\textquoteright} minus ends at the poles. In this study, we investigate the force generation and motility of the Kinesin-14 motors HSET and KlpA. Our findings reveal that both motors are non-processive, producing single load-dependent power strokes per MT encounter, with estimated load-free power strokes of \textasciitilde{}30 and \textasciitilde{}35 nm, respectively. Each homodimeric motor generates forces of \textasciitilde{}0.5 pN, but when assembled in teams, they cooperate to generate forces of 1 pN or more. Notably, the cooperative activity among multiple motors leads to increased MT-sliding velocities. These results quantitatively elucidate the structure-function relationship of Kinesin-14 motors and underscore the significance of cooperative behavior in their cellular functions.",

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AU - Berger, Florian

AU - Gennerich, Arne

N1 - Publisher Copyright: © The Author(s) 2024.

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Kinesin-14 HSET and KlpA are non-processive microtubule motors with load-dependent power strokes

Abstract

Bibliographical note

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Keywords

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