Evidence map›Paper›PMID 25523213›Full record

ArticleNature communications2014

The Escherichia coli effector EspJ blocks Src kinase activity via amidation and ADP ribosylation.

Joanna C Young, Abigail Clements, Alexander E Lang, James A Garnett, Diana Munera, Ana Arbeloa, Jaclyn Pearson, Elizabeth L Hartland, Stephen J Matthews, Aurelie Mousnier and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021
    Review
  4. Mammalian lectin arrays for screening host-microbe interactions.The Journal of biological chemistry · 2020
    Article
  5. Review
  6. EnteropathogenicInternational journal of molecular sciences · 2020
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. TheProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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

15 authors at 6 institutions in 3 countries.

Joanna C YoungMRC Centre for Molecular Bacteriology and Infection, Imperial College, SW7 2AZ London, UK.
Abigail ClementsMRC Centre for Molecular Bacteriology and Infection, Imperial College, SW7 2AZ London, UK.
Alexander E LangInstitute of Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, D-79104 Freiburg, Germany.
James A GarnettCentre for Structural Biology, Imperial College, SW7 2AZ London, UK.
Diana MuneraMRC Centre for Molecular Bacteriology and Infection, Imperial College, SW7 2AZ London, UK.
Ana ArbeloaMRC Centre for Molecular Bacteriology and Infection, Imperial College, SW7 2AZ London, UK.
Jaclyn PearsonDepartment of Microbiology and Immunology, University of Melbourne, at the Peter Doherty Institute for Infection and Immunity, Melbourne Victoria 3010, Australia.
Elizabeth L HartlandDepartment of Microbiology and Immunology, University of Melbourne, at the Peter Doherty Institute for Infection and Immunity, Melbourne Victoria 3010, Australia.
Stephen J MatthewsCentre for Structural Biology, Imperial College, SW7 2AZ London, UK.
Aurelie MousnierMRC Centre for Molecular Bacteriology and Infection, Imperial College, SW7 2AZ London, UK.
David J BarryCell Motility Laboratory, Cancer Research UK, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3LY, UK.
Michael WayCell Motility Laboratory, Cancer Research UK, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3LY, UK.
Andreas SchlosserRudolf Virchow Center for Experimental Biomedicine, University of Wuerzburg, 97080 Würzburg, Germany.
Klaus Aktories1] Institute of Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, D-79104 Freiburg, Germany [2] Centre for Biological Signalling Studies (BIOSS), University of Freiburg, D-79104 Freiburg, Germany.
Gad FrankelMRC Centre for Molecular Bacteriology and Infection, Imperial College, SW7 2AZ London, UK.
Imperial College London · GBPeter Doherty Institute · AUUniversity of Freiburg · DECancer Research UK · GBThe Honourable Society of Lincoln's Inn · GBUniversity of Würzburg · DE

Funding

Cancer Research UKMedical Research Council MR/J006874/1Wellcome Trust 100280
6 · The paper itself

Abstract

The hallmark of enteropathogenic Escherichia coli (EPEC) infection is the formation of actin-rich pedestal-like structures, which are generated following phosphorylation of the bacterial effector Tir by cellular Src and Abl family tyrosine kinases. This leads to recruitment of the Nck-WIP-N-WASP complex that triggers Arp2/3-dependent actin polymerization in the host cell. The same phosphorylation-mediated signalling network is also assembled downstream of the Vaccinia virus protein A36 and the phagocytic Fc-gamma receptor FcγRIIa. Here we report that the EPEC type-III secretion system effector EspJ inhibits autophosphorylation of Src and phosphorylation of the Src substrates Tir and FcγRIIa. Consistent with this, EspJ inhibits actin polymerization downstream of EPEC, Vaccinia virus and opsonized red blood cells. We identify EspJ as a unique adenosine diphosphate (ADP) ribosyltransferase that directly inhibits Src kinase by simultaneous amidation and ADP ribosylation of the conserved kinase-domain residue, Src E310, resulting in glutamine-ADP ribose.

Indexed as

Adenosine DiphosphateAmino Acid MotifsEnterohemorrhagic Escherichia coliEscherichia coli InfectionsEscherichia coli ProteinsHumansPhosphorylationProtein Processing, Post-TranslationalReceptors, IgGsrc-Family KinasesAdenosine DiphosphateEscherichia coli ProteinsEspJ protein, E coliFc gamma receptor IIAReceptors, IgGsrc-Family Kinases

Identifiers

PMID25523213
PMCPMC4284639
OpenAlexW1985723289

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.