Evidence map›Paper›PMID 28096179›Full record

ArticleThe EMBO journal2017

Dbf4-dependent kinase and the Rtt107 scaffold promote Mus81-Mms4 resolvase activation during mitosis.

Lissa N Princz, Philipp Wild, Julia Bittmann, F Javier Aguado, Miguel G Blanco, Joao Matos, Boris Pfander

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 64 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

7 authors at 3 institutions in 3 countries.

Lissa N PrinczMax Planck Institute of Biochemistry, DNA Replication and Genome Integrity, Martinsried, Germany.
Philipp WildInstitute of Biochemistry, Eidgenössische Technische Hochschule, Zürich, Switzerland.
Julia BittmannMax Planck Institute of Biochemistry, DNA Replication and Genome Integrity, Martinsried, Germany.
F Javier AguadoDepartment of Biochemistry and Molecular Biology, Center for Research in Molecular Medicine and Chronic Diseases, Universidade de Santiago de Compostela, Santiago de Compostela, Spain.
Miguel G BlancoDepartment of Biochemistry and Molecular Biology, Center for Research in Molecular Medicine and Chronic Diseases, Universidade de Santiago de Compostela, Santiago de Compostela, Spain.ORCID 0000-0002-2883-7326
Joao MatosInstitute of Biochemistry, Eidgenössische Technische Hochschule, Zürich, Switzerland.
Boris PfanderMax Planck Institute of Biochemistry, DNA Replication and Genome Integrity, Martinsried, Germany bpfander@biochem.mpg.de.ORCID 0000-0003-2180-5054
Max Planck Institute of Biochemistry · DEBoard of the Swiss Federal Institutes of Technology · CHUniversidade de Santiago de Compostela · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA repair by homologous recombination is under stringent cell cycle control. This includes the last step of the reaction, disentanglement of DNA joint molecules (JMs). Previous work has established that JM resolving nucleases are activated specifically at the onset of mitosis. In case of budding yeast Mus81-Mms4, this cell cycle stage-specific activation is known to depend on phosphorylation by CDK and Cdc5 kinases. Here, we show that a third cell cycle kinase, Cdc7-Dbf4 (DDK), targets Mus81-Mms4 in conjunction with Cdc5-both kinases bind to as well as phosphorylate Mus81-Mms4 in an interdependent manner. Moreover, DDK-mediated phosphorylation of Mms4 is strictly required for Mus81 activation in mitosis, establishing DDK as a novel regulator of homologous recombination. The scaffold protein Rtt107, which binds the Mus81-Mms4 complex, interacts with Cdc7 and thereby targets DDK and Cdc5 to the complex enabling full Mus81 activation. Therefore, Mus81 activation in mitosis involves at least three cell cycle kinases, CDK, Cdc5 and DDK Furthermore, tethering of the kinases in a stable complex with Mus81 is critical for efficient JM resolution.

Indexed as

MitosisCell Cycle ProteinsDNA-Binding ProteinsEndonucleasesEnzyme ActivationFlap EndonucleasesNuclear ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCDC5 protein, S cerevisiaeCDC7 protein, S cerevisiaeCell Cycle ProteinsDNA-Binding ProteinsEndonucleasesFlap EndonucleasesMMS4 protein, S cerevisiaeMUS81 protein, S cerevisiaeNuclear ProteinsProtein Serine-Threonine KinasesRTT107 protein, S cerevisiaeSaccharomyces cerevisiae Proteinscell cyclegenome stabilityhomologous recombinationjoint molecule resolutionpost‐translational modification

Identifiers

PMID28096179
PMCPMC5331752
OpenAlexW2572506455

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.