Evidence map›Paper›PMID 39095439›Full record

ArticleNature communications2024

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

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Xinglei Liu *Department of Biochemistry and Gruss Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY, USA.ORCID 0000-0002-1457-9928
Lu Rao *Department of Biochemistry and Gruss Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY, USA.ORCID 0000-0002-7447-1484
Weihong QiuCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, CH, Utrecht, The Netherlands.
Florian BergerDepartment of Biochemistry & Biophysics and Department of Physics, Oregon State University, Corvallis, OR, USA. f.m.berger@uu.nl.ORCID 0000-0003-3355-4336
Arne GennerichDepartment of Biochemistry and Gruss Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY, USA. arne.gennerich@einsteinmed.edu.ORCID 0000-0002-8346-5473

Funding

MOLECULAR MECHANISM OF THE CYTOPLASMIC DYNEIN-DYNACTIN MOTOR COMPLEXR01GM098469 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI GENNERICH, ARNE · 2012 to 2025
$5.1M
Role of the Kinesin KIF1A in Neurological DiseaseR01NS114636 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI CHUNG, WENDY K, GENNERICH, ARNE · 2020 to 2024
$3.2M
Mechanistic Analysis of Kinesin-14 Motility and Regulation for Bipolar Spindle AssemblyR01GM127922 · NIGMS · OREGON STATE UNIVERSITY · PI QIU, WEIHONG · 2019 to 2023
$1.5M
NIGMS NIH HHS R01 GM098469NIGMS NIH HHS R01 GM127922NINDS NIH HHS R01 NS114636U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01GM127922U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01NS114636
6 · The paper itself

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.

Indexed as

KinesinsMicrotubulesSpindle ApparatusAnimalsHumansMicrotubule-Associated ProteinsKinesinsMicrotubule-Associated Proteins

Identifiers

PMID39095439
PMCPMC11297315

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.