Evidence map›Paper›PMID 30578316›Full record

ArticleJournal of cell science2019

The depolymerase activity of MCAK shows a graded response to Aurora B kinase phosphorylation through allosteric regulation.

Toni McHugh, Juan Zou, Vladimir A Volkov, Aurélie Bertin, Sandeep K Talapatra, Juri Rappsilber, Marileen Dogterom, Julie P I Welburn

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 41 citations in OpenAlex.

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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 3 institutions in 4 countries.

Toni McHughWellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.
Juan ZouWellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.
Vladimir A VolkovDepartment of Bionanoscience, Faculty of Applied Sciences, Delft University of Technology, Delft 2629, The Netherlands.
Aurélie BertinLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005 Paris, France.
Sandeep K TalapatraWellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.
Juri RappsilberWellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.ORCID 0000-0001-5999-1310
Marileen DogteromDepartment of Bionanoscience, Faculty of Applied Sciences, Delft University of Technology, Delft 2629, The Netherlands.
Julie P I WelburnWellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK Julie.Welburn@ed.ac.uk.ORCID 0000-0002-5440-6060
Wellcome Centre for Cell Biology · GBDelft University of Technology · NLCentre National de la Recherche Scientifique · FR

Funding

European Research Council 609822Wellcome Trust 103139/Z/13/ZWellcome Trust 207430/Z/17/Z
6 · The paper itself

Abstract

Kinesin-13 motors regulate precise microtubule dynamics and limit microtubule length throughout metazoans by depolymerizing microtubule ends. Recently, the kinesin-13 motor family member MCAK (also known Kif2C) has been proposed to undergo large conformational changes during its catalytic cycle, as it switches from being in solution to being bound to microtubules. Here, we reveal that MCAK has a compact conformation in solution through crosslinking and electron microscopy experiments. When MCAK is bound to the microtubule ends, it adopts an extended conformation with the N-terminus and neck region of MCAK interacting with the microtubule. Interestingly, the region of MCAK that interacts with the microtubule is the region phosphorylated by Aurora B and contains an end binding (EB) protein-binding motif. The level of phosphorylation of the N-terminus results in a graded microtubule depolymerase activity. Here, we show that the N-terminus of MCAK forms a platform to integrate Aurora B kinase downstream signals and in response fine-tunes its depolymerase activity during mitosis. We propose that this allosteric control mechanism allows decoupling of the N-terminus from the motor domain of MCAK to allow MCAK depolymerase activity at kinetochores.

Indexed as

Allosteric RegulationAmino Acid SequenceAnimalsAurora Kinase BBinding SitesCloning, MolecularCrystallography, X-RayGene ExpressionGenetic VectorsHumansKinesinsKinetochoresMicrotubulesMitosisModels, MolecularPhosphorylationAURKB protein, humanAurora Kinase BKIF2C protein, humanKinesinsRecombinant ProteinsAurora BMCAKMicrotubulesPhosphorylation

Identifiers

PMID30578316
PMCPMC6398471
OpenAlexW2906015109

What OpenQuestion holds

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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.