Evidence map›Paper›PMID 29340707›Full record

ArticleCellular and molecular life sciences : CMLS2018

VRK1 and AURKB form a complex that cross inhibit their kinase activity and the phosphorylation of histone H3 in the progression of mitosis.

David S Moura, Ignacio Campillo-Marcos, Marta Vázquez-Cedeira, Pedro A Lazo

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed, 77 citations in OpenAlex.

  1. NovelNeurology. Genetics · 2026
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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 2 institutions in 1 country.

David S MouraExperimental Therapeutics and Translational Oncology Program, Instituto de Biología Molecular y Celular del Cáncer-Centro de Investigación del Cáncer, CSIC-Universidad de Salamanca, Campus Miguel de Unamuno, 37007, Salamanca, Spain.ORCID http://orcid.org/0000-0002-6514-2419
Ignacio Campillo-MarcosExperimental Therapeutics and Translational Oncology Program, Instituto de Biología Molecular y Celular del Cáncer-Centro de Investigación del Cáncer, CSIC-Universidad de Salamanca, Campus Miguel de Unamuno, 37007, Salamanca, Spain.ORCID http://orcid.org/0000-0002-7657-7127
Marta Vázquez-CedeiraExperimental Therapeutics and Translational Oncology Program, Instituto de Biología Molecular y Celular del Cáncer-Centro de Investigación del Cáncer, CSIC-Universidad de Salamanca, Campus Miguel de Unamuno, 37007, Salamanca, Spain.
Pedro A LazoExperimental Therapeutics and Translational Oncology Program, Instituto de Biología Molecular y Celular del Cáncer-Centro de Investigación del Cáncer, CSIC-Universidad de Salamanca, Campus Miguel de Unamuno, 37007, Salamanca, Spain. pedro.lazo@csic.es.ORCID http://orcid.org/0000-0001-8997-3025
Universidad de Salamanca · ESInstituto de Investigación Biomédica de Salamanca · ES

Funding

Consejería de Educación, Junta de Castilla y León CSI001U16Ministerio de Economía y Competitividad SAF2013-44810-RMinisterio de Economía y Competitividad SAF2014-57791-REDCMinisterio de Economía y Competitividad SAF2016-75744-R
6 · The paper itself

Abstract

Regulation of cell division requires the integration of signals implicated in chromatin reorganization and coordination of its sequential changes in mitosis. Vaccinia-related kinase 1 (VRK1) and Aurora B (AURKB) are two nuclear kinases involved in different steps of cell division. We have studied whether there is any functional connection between these two nuclear kinases, which phosphorylate histone H3 in Thr3 and Ser10, respectively. VRK1 and AURKB are able to form a stable protein complex, which represents only a minor subpopulation of each kinase within the cell and is detected following nocodazole release. Each kinase is able to inhibit the kinase activity of the other kinase, as well as inhibit their specific phosphorylation of histone H3. In locations where the two kinases interact, there is a different pattern of histone modifications, indicating that there is a local difference in chromatin during mitosis because of the local complexes formed by these kinases and their asymmetric intracellular distribution. Depletion of VRK1 downregulates the gene expression of BIRC5 (survivin) that recognizes H3-T3ph, both are dependent on the activity of VRK1, and is recovered with kinase active murine VRK1, but not with a kinase-dead protein. The H3-Thr3ph-survivin complex is required for AURB recruitment, and their loss prevents the localization of ACA and AURKB in centromeres. The cross inhibition of the kinases at the end of mitosis might facilitate the formation of daughter cells. A sequential role for VRK1, AURKB, and haspin in the progression of mitosis is proposed.

Indexed as

Aurora Kinase BCells, CulturedEnzyme ActivationFeedback, PhysiologicalGene Expression RegulationHEK293 CellsHeLa CellsHistonesHumansIntracellular Signaling Peptides and ProteinsMitosisPhosphorylationProtein BindingProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesReceptor Cross-TalkAURKB protein, humanAurora Kinase BHistonesIntracellular Signaling Peptides and ProteinsProtein Serine-Threonine KinasesVRK1 protein, humanAurora kinase BHistone H3KinasePhosphorylationSurvivinVRK1

Identifiers

PMID29340707
PMCPMC6003988
OpenAlexW2783102394

What Socratic 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 Socratic graph.