Evidence map›Paper›PMID 25504441›Full record

ArticleOncotarget2015

The activity regulation of the mitotic centromere-associated kinesin by Polo-like kinase 1.

Andreas Ritter, Mourad Sanhaji, Kerstin Steinhäuser, Susanne Roth, Frank Louwen, Juping Yuan

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 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

6 authors at 1 institution in 1 country.

Andreas RitterDepartment of Gynecology and Obstetrics, School of Medicine, J. W. Goethe-University, 60590 Frankfurt, Germany.
Mourad SanhajiDepartment of Gynecology and Obstetrics, School of Medicine, J. W. Goethe-University, 60590 Frankfurt, Germany.
Kerstin SteinhäuserDepartment of Gynecology and Obstetrics, School of Medicine, J. W. Goethe-University, 60590 Frankfurt, Germany.
Susanne RothDepartment of Gynecology and Obstetrics, School of Medicine, J. W. Goethe-University, 60590 Frankfurt, Germany.
Frank LouwenDepartment of Gynecology and Obstetrics, School of Medicine, J. W. Goethe-University, 60590 Frankfurt, Germany.
Juping YuanDepartment of Gynecology and Obstetrics, School of Medicine, J. W. Goethe-University, 60590 Frankfurt, Germany.
Goethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitotic centromere-associated kinesin (MCAK), a potent microtubule depolymerase, is involved in regulating microtubule dynamics. The activity and subcellular localization of MCAK are tightly regulated by key mitotic kinases, such as Polo-like kinase 1 (Plk1) by phosphorylating multiple residues in MCAK. Since Plk1 phosphorylates very often different residues of substrates at different stages, we have dissected individual phosphorylation of MCAK by Plk1 and characterized its function in more depth. We have recently shown that S621 in MCAK is the major phosphorylation site of Plk1, which is responsible for regulating MCAK's degradation by promoting the association of MCAK with APC/CCdc20. In the present study, we have addressed another two residues phosphorylated by Plk1, namely S632/S633 in the C-terminus of MCAK. Our data suggest that Plk1 phosphorylates S632/S633 and regulates its catalytic activity in mitosis. This phosphorylation is required for proper spindle assembly during early phases of mitosis. The subsequent dephosphorylation of S632/S633 might be necessary to timely align the chromosomes onto the metaphase plate. Therefore, our studies suggest new mechanisms by which Plk1 regulates MCAK: the degradation of MCAK is controlled by Plk1 phosphorylation on S621, whereas its activity is modulated by Plk1 phosphorylation on S632/S633 in mitosis.

Indexed as

MitosisCell Cycle ProteinsCentromereChromosome SegregationEnzyme ActivationHCT116 CellsHeLa CellsHumansKinesinsMetaphaseMicrotubulesMutationPhosphorylationPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsCell Cycle ProteinsKIF2C protein, humanKinesinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsSerinechromosome alignmentMCAKphosphorylationPlk1spindle assembly

Identifiers

PMID25504441
PMCPMC4466640
OpenAlexW1597713268

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.