Evidence map›Paper›PMID 20957203›Full record

ArticlePloS one2010

Yersinia virulence factor YopM induces sustained RSK activation by interfering with dephosphorylation.

Moritz Hentschke, Laura Berneking, Cristina Belmar Campos, Friedrich Buck, Klaus Ruckdeschel, Martin Aepfelbacher

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 64 citations in OpenAlex.

  1. ThebioRxiv : the preprint server for biology · 2026
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  6. A case of convergent evolution: Several viral and bacterial pathogens hijack RSK kinases through a common linear motif.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  7. Article
  8. Review
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  12. The pyrin inflammasome in host-microbe interactions.Current opinion in microbiology · 2020
    Review
  13. Article
  14. Chromosomally-EncodedFrontiers in cellular and infection microbiology · 2019
    Article
  15. Article
  16. Review
  17. Review
  18. Article
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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 2 institutions in 1 country.

Moritz HentschkeInstitute of Medical Microbiology, Virology and Hygiene, University Medical Center Eppendorf, Hamburg, Germany. jbaltzer@mta.ca
Laura Berneking
Cristina Belmar Campos
Friedrich Buck
Klaus Ruckdeschel
Martin Aepfelbacher
Universität Hamburg · DEUniversity Medical Center Hamburg-Eppendorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPathogenic yersiniae inject several effector proteins (Yops) into host cells, which subverts immune functions and enables the bacteria to survive within the host organism. YopM, whose deletion in enteropathogenic yersiniae results in a dramatic loss of virulence, has previously been shown to form a complex with and activate the multifunctional kinases PKN2 and RSK1 in transfected cells. METHODOLOGY/PRINCIPAL

findingsIn a near physiological approach with double-affinity-tagged YopM being translocated into the macrophage cell line J774A.1 via the natural type three secretion system of Yersinia we verified the interaction of YopM with PKN2 and RSK1 and detected association with additional PKN and RSK isoforms. In transfected and infected cells YopM induced sustained phosphorylation of RSK at its activation sites serine-380 and serine-221 even in the absence of signalling from its upstream kinase ERK1/2, suggesting inhibition of dephosphorylation. ATP-depletion and in vitro assays using purified components directly confirmed that YopM shields RSK isoforms from phosphatase activity towards serines 380 and 221. CONCLUSIONS/SIGNIFICANCE: Our study suggests that during Yersinia infection YopM induces sustained activation of RSK by blocking dephosphorylation of its activatory phosphorylation sites. This may represent a novel mode of action of a bacterial virulence factor.

Indexed as

Amino Acid SequenceAnimalsBacterial Outer Membrane ProteinsBase SequenceBlotting, WesternCell LineChromatography, AffinityDNA PrimersEnzyme ActivationHumansMiceMolecular Sequence DataPhosphorylationRibosomal Protein S6 Kinases, 90-kDaSignal TransductionSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationBacterial Outer Membrane ProteinsDNA PrimersRibosomal Protein S6 Kinases, 90-kDaRps6ka1 protein, mouseyopM protein, Yersinia

Identifiers

PMID20957203
PMCPMC2950144
OpenAlexW2023221600

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.