Evidence map›Paper›PMID 29117528›Full record

ArticleBiophysical journal2017

Ensembles of Bidirectional Kinesin Cin8 Produce Additive Forces in Both Directions of Movement.

Todd Fallesen, Johanna Roostalu, Christian Duellberg, Gunnar Pruessner, Thomas Surrey

Abstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Distinct regions of the kinesin-5 C-terminal tail are essential for mitotic spindle midzone localization and sliding force.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

5 authors.

Todd FallesenThe Francis Crick Institute, Imperial College London, London, United Kingdom.
Johanna RoostaluThe Francis Crick Institute, Imperial College London, London, United Kingdom.
Christian DuellbergThe Francis Crick Institute, Imperial College London, London, United Kingdom.
Gunnar PruessnerDepartment of Mathematics, Imperial College London, London, United Kingdom. Electronic address: g.pruessner@imperial.ac.uk.
Thomas SurreyThe Francis Crick Institute, Imperial College London, London, United Kingdom. Electronic address: thomas.surrey@crick.ac.uk.

Funding

European Research Council 323042Wellcome Trust FC001163
6 · The paper itself

Abstract

Most kinesin motors move in only one direction along microtubules. Members of the kinesin-5 subfamily were initially described as unidirectional plus-end-directed motors and shown to produce piconewton forces. However, some fungal kinesin-5 motors are bidirectional. The force production of a bidirectional kinesin-5 has not yet been measured. Therefore, it remains unknown whether the mechanism of the unconventional minus-end-directed motility differs fundamentally from that of plus-end-directed stepping. Using force spectroscopy, we have measured here the forces that ensembles of purified budding yeast kinesin-5 Cin8 produce in microtubule gliding assays in both plus- and minus-end direction. Correlation analysis of pause forces demonstrated that individual Cin8 molecules produce additive forces in both directions of movement. In ensembles, Cin8 motors were able to produce single-motor forces up to a magnitude of ∼1.5 pN. Hence, these properties appear to be conserved within the kinesin-5 subfamily. Force production was largely independent of the directionality of movement, indicating similarities between the motility mechanisms for both directions. These results provide constraints for the development of models for the bidirectional motility mechanism of fission yeast kinesin-5 and provide insight into the function of this mitotic motor.

Indexed as

Mechanical PhenomenaMovementAnimalsBiomechanical PhenomenaKinesinsMicroscopy, Atomic ForceMicrotubulesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCIN8 protein, S cerevisiaeKinesinsSaccharomyces cerevisiae Proteins

Identifiers

PMID29117528
PMCPMC5685778

What OpenQuestion holds

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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.