Evidence map›Paper›PMID 25348260›Full record

ArticleNature communications2014

Kinesin-14 and kinesin-5 antagonistically regulate microtubule nucleation by γ-TuRC in yeast and human cells.

Zachary T Olmsted, Andrew G Colliver, Timothy D Riehlman, Janet L Paluh

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

36 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
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  4. 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
    Article
  5. Article
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  7. Mitotic spindle formation in the absence of Polo kinase.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. 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
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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

4 authors at 1 institution in 1 country.

Zachary T OlmstedState University of New York Polytechnic Institute, College of Nanoscale Science, Nanobioscience Constellation, Albany, New York 12203, USA.
Andrew G ColliverState University of New York Polytechnic Institute, College of Nanoscale Science, Nanobioscience Constellation, Albany, New York 12203, USA.
Timothy D RiehlmanState University of New York Polytechnic Institute, College of Nanoscale Science, Nanobioscience Constellation, Albany, New York 12203, USA.
Janet L PaluhState University of New York Polytechnic Institute, College of Nanoscale Science, Nanobioscience Constellation, Albany, New York 12203, USA.
SUNY Polytechnic Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bipolar spindle assembly is a critical control point for initiation of mitosis through nucleation and organization of spindle microtubules and is regulated by kinesin-like proteins. In fission yeast, the kinesin-14 Pkl1 binds the γ-tubulin ring complex (γ-TuRC) microtubule-organizing centre at spindle poles and can alter its structure and function. Here we show that kinesin-14 blocks microtubule nucleation in yeast and reveal that this inhibition is countered by the kinesin-5 protein, Cut7. Furthermore, we demonstrate that Cut7 binding to γ-TuRC and the Cut7 BimC domain are both required for inhibition of Pkl1. We also demonstrate that a yeast kinesin-14 peptide blocks microtubule nucleation in two human breast cancer cell lines, suggesting that this mechanism is evolutionarily conserved. In conclusion, using genetic, biochemical and cell biology approaches we uncover antagonistic control of microtubule nucleation at γ-TuRC by two kinesin-like proteins, which may represent an attractive anti-mitotic target for cancer therapies.

Indexed as

Breast NeoplasmsCell Line, TumorChromosome SegregationFemaleHumansKinesinsMCF-7 CellsMicrobial ViabilityMicrotubule-Organizing CenterMicrotubulesMutationPeptidesProtein BindingProtein Structure, TertiarySchizosaccharomycesSchizosaccharomyces pombe ProteinsKinesinsPeptidesSchizosaccharomyces pombe ProteinsTubulin

Identifiers

PMID25348260
PMCPMC4220466
OpenAlexW1988517985

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.