Evidence map›Paper›PMID 25902441›Full record

ArticleBiophysical journal2015

The Kinesin-8 Kip3 switches protofilaments in a sideward random walk asymmetrically biased by force.

Michael Bugiel, Elisa Böhl, Erik Schäffer

Abstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
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  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Directionally biased sidestepping of Kip3/kinesin-8 is regulated by ATP waiting time and motor-microtubule interaction strength.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Article
  14. Kinesin rotates unidirectionally and generates torque while walking on microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Working stroke of the kinesin-14, ncd, comprises two substeps of different direction.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Michael BugielCellular Nanoscience Group, Center for Plant Molecular Biology, Eberhard Karls Universität Tübingen, Tübingen, Germany.
Elisa BöhlCellular Nanoscience Group, Center for Plant Molecular Biology, Eberhard Karls Universität Tübingen, Tübingen, Germany.
Erik SchäfferCellular Nanoscience Group, Center for Plant Molecular Biology, Eberhard Karls Universität Tübingen, Tübingen, Germany. Electronic address: erik.schaeffer@uni-tuebingen.de.

Funding

European Research Council 260875
6 · The paper itself

Abstract

Molecular motors translocate along cytoskeletal filaments, as in the case of kinesin motors on microtubules. Although conventional kinesin-1 tracks a single microtubule protofilament, other kinesins, akin to dyneins, switch protofilaments. However, the molecular trajectory-whether protofilament switching occurs in a directed or stochastic manner-is unclear. Here, we used high-resolution optical tweezers to track the path of single budding yeast kinesin-8, Kip3, motor proteins. Under applied sideward loads, we found that individual motors stepped sideward in both directions, with and against loads, with a broad distribution in measured step sizes. Interestingly, the force response depended on the direction. Based on a statistical analysis and simulations accounting for the geometry, we propose a diffusive sideward stepping motion of Kip3 on the microtubule lattice, asymmetrically biased by force. This finding is consistent with previous multimotor gliding assays and sheds light on the molecular switching mechanism. For kinesin-8, the diffusive switching mechanism may enable the motor to bypass obstacles and reach the microtubule end for length regulation. For other motors, such a mechanism may have implications for torque generation around the filament axis.

Indexed as

AnimalsKinesinsMicrotubulesOptical TweezersRatsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSwineTorqueKinesinsKIP3 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID25902441
PMCPMC4407264

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.