Evidence map›Paper›PMID 25626168›Full record

ArticleeLife2015

Non-catalytic motor domains enable processive movement and functional diversification of the kinesin-14 Kar3.

Christine Mieck, Maxim I Molodtsov, Katarzyna Drzewicka, Babet van der Vaart, Gabriele Litos, Gerald Schmauss, Alipasha Vaziri, Stefan Westermann

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.1field-weighted citation impact, top 9% of its field
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

22 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  6. Kinesin-14 motors participate in a force balance at microtubule plus-ends to regulate dynamic instability.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.Protein science : a publication of the Protein Society · 2021
    Article
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  16. Structural plasticity of the living kinetochore.The Journal of cell biology · 2017
    Article
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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

8 authors at 2 institutions in 1 country.

Christine MieckResearch Institute of Molecular Pathology, Vienna, Austria.
Maxim I MolodtsovResearch Institute of Molecular Pathology, Vienna, Austria.
Katarzyna DrzewickaResearch Institute of Molecular Pathology, Vienna, Austria.
Babet van der VaartResearch Institute of Molecular Pathology, Vienna, Austria.
Gabriele LitosResearch Institute of Molecular Pathology, Vienna, Austria.
Gerald SchmaussResearch Institute of Molecular Pathology, Vienna, Austria.
Alipasha VaziriResearch Institute of Molecular Pathology, Vienna, Austria.
Stefan WestermannResearch Institute of Molecular Pathology, Vienna, Austria.
Research Institute of Molecular Pathology · ATMax Perutz Labs · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Motor proteins of the conserved kinesin-14 family have important roles in mitotic spindle organization and chromosome segregation. Previous studies have indicated that kinesin-14 motors are non-processive enzymes, working in the context of multi-motor ensembles that collectively organize microtubule networks. In this study, we show that the yeast kinesin-14 Kar3 generates processive movement as a heterodimer with the non-motor proteins Cik1 or Vik1. By analyzing the single-molecule properties of engineered motors, we demonstrate that the non-catalytic domain has a key role in the motility mechanism by acting as a 'foothold' that allows Kar3 to bias translocation towards the minus end. This mechanism rivals the speed and run length of conventional motors, can support transport of the Ndc80 complex in vitro and is critical for Kar3 function in vivo. Our findings provide an example for a non-conventional translocation mechanism and can explain how Kar3 substitutes for key functions of Dynein in the yeast nucleus.

Indexed as

Catalytic DomainDimerizationMicrotubule-Associated ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubcellular FractionsKAR3 protein, S cerevisiaeMicrotubule-Associated ProteinsSaccharomyces cerevisiae Proteinsbiophysicscell biologycytoskeletonkinesinsmicrotubulesS. cerevisiaestructural biology

Identifiers

PMID25626168
PMCPMC4338441
OpenAlexW2031792634

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.