Evidence map›Paper›PMID 20140229›Full record

ArticlePloS one2010

Staphylococcal PknB as the first prokaryotic representative of the proline-directed kinases.

Malgorzata Miller, Stefanie Donat, Sonja Rakette, Thilo Stehle, Thijs R H M Kouwen, Sander H Diks, Annette Dreisbach, Ewoud Reilman, Katrin Gronau, Dörte Becher and 3 more

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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.6field-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

27 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  4. A membrane-depolarizing toxin substrate of theProceedings of the National Academy of Sciences of the United States of America · 2020
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  8. Functional analysis of the EsaB component of theMicrobiology (Reading, England) · 2017
    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

13 authors at 6 institutions in 3 countries.

Malgorzata MillerDepartment of Medical Microbiology, University Medical Center Groningen and University of Groningen, Groningen, The Netherlands.
Stefanie Donat
Sonja Rakette
Thilo Stehle
Thijs R H M Kouwen
Sander H Diks
Annette Dreisbach
Ewoud Reilman
Katrin Gronau
Dörte Becher
Maikel P Peppelenbosch
Jan Maarten van Dijl
Knut Ohlsen
University of Groningen · NLUniversität Greifswald · DEUniversity Medical Center Groningen · NLUniversity of Würzburg · DEUniversity of Tübingen · DEVanderbilt University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotic cell types, virtually all cellular processes are under control of proline-directed kinases and especially MAP kinases. Serine/threonine kinases in general were originally considered as a eukaryote-specific enzyme family. However, recent studies have revealed that orthologues of eukaryotic serine/threonine kinases exist in bacteria. Moreover, various pathogenic species, such as Yersinia and Mycobacterium, require serine/threonine kinases for successful invasion of human host cells. The substrates targeted by bacterial serine/threonine kinases have remained largely unknown. Here we report that the serine/threonine kinase PknB from the important pathogen Staphylococcus aureus is released into the external milieu, which opens up the possibility that PknB does not only phosphorylate bacterial proteins but also proteins of the human host. To identify possible human targets of purified PknB, we studied in vitro phosphorylation of peptide microarrays and detected 68 possible human targets for phosphorylation. These results show that PknB is a proline-directed kinase with MAP kinase-like enzymatic activity. As the potential cellular targets for PknB are involved in apoptosis, immune responses, transport, and metabolism, PknB secretion may help the bacterium to evade intracellular killing and facilitate its growth. In apparent agreement with this notion, phosphorylation of the host-cell response coordinating transcription factor ATF-2 by PknB was confirmed by mass spectrometry. Taken together, our results identify PknB as the first prokaryotic representative of the proline-directed kinase/MAP kinase family of enzymes.

Indexed as

Activating Transcription Factor 2Amino Acid SequenceBacterial ProteinsBinding SitesBlotting, WesternHumansMAP Kinase Kinase 4Mass SpectrometryMutationp38 Mitogen-Activated Protein KinasesPeptidesPhosphorylationProlineProtein Array AnalysisProtein Serine-Threonine KinasesStaphylococcus aureusActivating Transcription Factor 2ATF2 protein, humanBacterial ProteinsMAP Kinase Kinase 4p38 Mitogen-Activated Protein KinasesPeptidesProlineProtein Serine-Threonine Kinases

Identifiers

PMID20140229
PMCPMC2816222
OpenAlexW2089833148

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Registered trials

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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.