Evidence map›Paper›PMID 32973148›Full record

ArticleNature communications2020

Cross-regulation of viral kinases with cyclin A secures shutoff of host DNA synthesis.

Boris Bogdanow, Max Schmidt, Henry Weisbach, Iris Gruska, Barbara Vetter, Koshi Imami, Eleonore Ostermann, Wolfram Brune, Matthias Selbach, Christian Hagemeier and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.5field-weighted citation impact, top 10% 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, 23 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

11 authors at 5 institutions in 2 countries.

Boris Bogdanow *Research group "Proteome Dynamics", Max Delbrück Center for Molecular Medicine, 13125, Berlin, Germany.
Max Schmidt *Labor für Pädiatrische Molekularbiologie, Charité Universitätsmedizin Berlin, 13353, Berlin, Germany.
Henry WeisbachLabor für Pädiatrische Molekularbiologie, Charité Universitätsmedizin Berlin, 13353, Berlin, Germany.
Iris GruskaLabor für Pädiatrische Molekularbiologie, Charité Universitätsmedizin Berlin, 13353, Berlin, Germany.ORCID http://orcid.org/0000-0002-9539-609X
Barbara VetterLabor für Pädiatrische Molekularbiologie, Charité Universitätsmedizin Berlin, 13353, Berlin, Germany.
Koshi ImamiResearch group "Proteome Dynamics", Max Delbrück Center for Molecular Medicine, 13125, Berlin, Germany.ORCID http://orcid.org/0000-0002-7451-4982
Eleonore OstermannHeinrich Pette Institute, Leibniz Institute for Experimental Virology, 20251, Hamburg, Germany.ORCID http://orcid.org/0000-0002-7539-2155
Wolfram BruneHeinrich Pette Institute, Leibniz Institute for Experimental Virology, 20251, Hamburg, Germany.ORCID http://orcid.org/0000-0002-6078-5255
Matthias SelbachResearch group "Proteome Dynamics", Max Delbrück Center for Molecular Medicine, 13125, Berlin, Germany.ORCID http://orcid.org/0000-0003-2454-8751
Christian HagemeierLabor für Pädiatrische Molekularbiologie, Charité Universitätsmedizin Berlin, 13353, Berlin, Germany.
Lüder WiebuschLabor für Pädiatrische Molekularbiologie, Charité Universitätsmedizin Berlin, 13353, Berlin, Germany. lueder.wiebusch@charite.de.ORCID http://orcid.org/0000-0002-7210-6731
Charité - Universitätsmedizin Berlin · DEMax Delbrück Center · DELeibniz Institute of Virology (LIV) · DEDeutsche Gesellschaft für Hämatologie und Medizinische Onkologie · DEPharmaFGP (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herpesviruses encode conserved protein kinases (CHPKs) to stimulate phosphorylation-sensitive processes during infection. How CHPKs bind to cellular factors and how this impacts their regulatory functions is poorly understood. Here, we use quantitative proteomics to determine cellular interaction partners of human herpesvirus (HHV) CHPKs. We find that CHPKs can target key regulators of transcription and replication. The interaction with Cyclin A and associated factors is identified as a signature of β-herpesvirus kinases. Cyclin A is recruited via RXL motifs that overlap with nuclear localization signals (NLS) in the non-catalytic N termini. This architecture is conserved in HHV6, HHV7 and rodent cytomegaloviruses. Cyclin A binding competes with NLS function, enabling dynamic changes in CHPK localization and substrate phosphorylation. The cytomegalovirus kinase M97 sequesters Cyclin A in the cytosol, which is essential for viral inhibition of cellular replication. Our data highlight a fine-tuned and physiologically important interplay between a cellular cyclin and viral kinases.

Indexed as

AnimalsCyclin ACytomegalovirusDNADNA ReplicationHEK293 CellsHerpesviridaeHerpesviridae InfectionsHumansMiceNIH 3T3 CellsNuclear Localization SignalsPhosphorylationProtein Interaction MapsProtein KinasesViral ProteinsCyclin ADNANuclear Localization SignalsProtein KinasesViral Proteins

Identifiers

PMID32973148
PMCPMC7518283
OpenAlexW3087854134

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.