Evidence map›Paper›PMID 30206188›Full record

ArticleEMBO reports2018

Opposing kinesin complexes queue at plus tips to ensure microtubule catastrophe at cell ends.

John C Meadows, Liam J Messin, Anton Kamnev, Theresa C Lancaster, Mohan K Balasubramanian, Robert A Cross, Jonathan Ba Millar

Abstract read
In one paragraph

Article in EMBO reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

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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

7 authors.

John C MeadowsDivision of Biomedical Sciences, Centre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry, UK J.C.Meadows@warwick.ac.uk J.Millar@warwick.ac.uk.ORCID 0000-0001-7024-3014
Liam J MessinDivision of Biomedical Sciences, Centre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry, UK.
Anton KamnevDivision of Biomedical Sciences, Centre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry, UK.
Theresa C LancasterDivision of Biomedical Sciences, Centre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry, UK.
Mohan K BalasubramanianDivision of Biomedical Sciences, Centre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry, UK.
Robert A CrossDivision of Biomedical Sciences, Centre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry, UK.ORCID 0000-0002-0004-7832
Jonathan Ba MillarDivision of Biomedical Sciences, Centre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Coventry, UK J.C.Meadows@warwick.ac.uk J.Millar@warwick.ac.uk.ORCID 0000-0002-9930-3989

Funding

Medical Research Council MR/K001000/1Wellcome TrustWellcome Trust 103895/Z/14/ZWellcome Trust WT101885MA
6 · The paper itself

Abstract

In fission yeast, the lengths of interphase microtubule (iMT) arrays are adapted to cell length to maintain cell polarity and to help centre the nucleus and cell division ring. Here, we show that length regulation of iMTs is dictated by spatially regulated competition between MT-stabilising Tea2/Tip1/Mal3 (Kinesin-7) and MT-destabilising Klp5/Klp6/Mcp1 (Kinesin-8) complexes at iMT plus ends. During MT growth, the Tea2/Tip1/Mal3 complex remains bound to the plus ends of iMT bundles, thereby restricting access to the plus ends by Klp5/Klp6/Mcp1, which accumulate behind it. At cell ends, Klp5/Klp6/Mcp1 invades the space occupied by the Tea2/Tip1/Tea1 kinesin complex triggering its displacement from iMT plus ends and MT catastrophe. These data show that

Indexed as

Cell PolarityInterphaseKinesinsMicroscopy, FluorescenceMicrotubule-Associated ProteinsMicrotubulesMultiprotein ComplexesSchizosaccharomycesSchizosaccharomyces pombe ProteinsKinesinsKlp5 protein, S pombeKlp6 protein, S pombeMcp1 protein, S pombeMicrotubule-Associated ProteinsMultiprotein ComplexesSchizosaccharomyces pombe ProteinsTea2 protein, S pombecytoskeletonfission yeastkinesinmicrotubules

Identifiers

PMID30206188
PMCPMC6216294

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.