Evidence map›Paper›PMID 33044553›Full record

ArticleThe Journal of cell biology2020

The EB1-Kinesin-14 complex is required for efficient metaphase spindle assembly and kinetochore bi-orientation.

Nikolay Kornakov, Bastian Möllers, Stefan Westermann

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

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  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
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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

3 authors at 1 institution in 1 country.

Nikolay KornakovDepartment of Molecular Genetics, Faculty of Biology, Center of Medical Biotechnology, University of Duisburg-Essen, Essen, Germany.
Bastian MöllersDepartment of Molecular Genetics, Faculty of Biology, Center of Medical Biotechnology, University of Duisburg-Essen, Essen, Germany.
Stefan WestermannDepartment of Molecular Genetics, Faculty of Biology, Center of Medical Biotechnology, University of Duisburg-Essen, Essen, Germany.
University of Duisburg-Essen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kinesin-14s are conserved molecular motors required for high-fidelity chromosome segregation, but their specific contributions to spindle function have not been fully defined. Here, we show that key functions of budding yeast Kinesin-14 Cik1-Kar3 are accomplished in a complex with Bim1 (yeast EB1). Genetic complementation of mitotic phenotypes identifies a novel KLTF peptide motif in the Cik1 N-terminus. We show that this motif is one element of a tripartite binding interface required to form a high-affinity Bim1-Cik1-Kar3 complex. Lack of Bim1-binding by Cik1-Kar3 delays cells in mitosis and impairs microtubule bundle organization and dynamics. Conversely, constitutive targeting of Cik1-Kar3 to microtubule plus ends induces the formation of nuclear microtubule bundles. Cells lacking the Bim1-Cik1-Kar3 complex rely on the conserved microtubule bundler Ase1/PRC1 for metaphase spindle organization, and simultaneous loss of plus-end targeted Kar3 and Ase1 is lethal. Our results reveal the contributions of an EB1-Kinesin-14 complex for spindle formation as a prerequisite for efficient kinetochore clustering and bi-orientation.

Indexed as

Cell Cycle ProteinsKinesinsKinetochoresMicrotubule-Associated ProteinsMicrotubule ProteinsMultiprotein ComplexesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle ApparatusAse1 protein, S cerevisiaeBIM1 protein, S cerevisiaeCell Cycle ProteinsCIK1 protein, S cerevisiaeKAR3 protein, S cerevisiaeKinesinsMicrotubule-Associated ProteinsMicrotubule ProteinsMultiprotein ComplexesSaccharomyces cerevisiae Proteins

Identifiers

PMID33044553
PMCPMC7545359
OpenAlexW3091827143

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.