Evidence map›Paper›PMID 26190758›Full record

ArticleNature communications2015

Tyrosine glycosylation of Rho by Yersinia toxin impairs blastomere cell behaviour in zebrafish embryos.

Thomas Jank, Stephanie Eckerle, Marcus Steinemann, Christoph Trillhaase, Marianne Schimpl, Sebastian Wiese, Daan M F van Aalten, Wolfgang Driever, Klaus Aktories

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Article
  3. Tyrosine-modifying glycosylation by Yersinia effectors.The Journal of biological chemistry · 2024
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Glycosylating Effectors ofBiomolecules · 2022
    Review
  10. Article
  11. Zebrafish as a Model for Fish Diseases in Aquaculture.Pathogens (Basel, Switzerland) · 2020
    Review
  12. Inverse control of Rab proteins byScience advances · 2020
    Article
  13. Review
  14. Nucleocytoplasmic O-glycosylation in protists.Current opinion in structural biology · 2019
    Review
  15. Article
  16. Review
  17. Article
  18. The Infection Process ofFrontiers in cellular and infection microbiology · 2018
    Review
  19. Article
  20. 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

9 authors at 3 institutions in 2 countries.

Thomas JankInstitute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University Freiburg, D-79104 Freiburg, Germany.
Stephanie EckerleDepartment of Developmental Biology, Institute Biology I, Faculty of Biology, Albert-Ludwigs-University Freiburg, D-79104 Freiburg, Germany.
Marcus SteinemannInstitute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University Freiburg, D-79104 Freiburg, Germany.
Christoph TrillhaaseInstitute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University Freiburg, D-79104 Freiburg, Germany.
Marianne SchimplMRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK.
Sebastian WieseCenter for Biological Systems Analysis, Albert-Ludwigs-University Freiburg, D-79104 Freiburg, Germany.
Daan M F van AaltenMRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK.
Wolfgang Driever1] Department of Developmental Biology, Institute Biology I, Faculty of Biology, Albert-Ludwigs-University Freiburg, D-79104 Freiburg, Germany [2] Centre for Biological Signalling Studies (BIOSS), Albert-Ludwigs-University Freiburg, D-79104 Freiburg, Germany.
Klaus Aktories1] Institute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University Freiburg, D-79104 Freiburg, Germany [2] Centre for Biological Signalling Studies (BIOSS), Albert-Ludwigs-University Freiburg, D-79104 Freiburg, Germany.
University of Freiburg · DEMRC Protein Phosphorylation and Ubiquitylation Unit · GBUniversity of Dundee · GB

Funding

Department of Health M004139Medical Research Council G0900138Medical Research Council MR/M004139/1Wellcome Trust 087590Wellcome Trust WT087590MA
6 · The paper itself

Abstract

Yersinia species cause zoonotic infections, including enterocolitis and plague. Here we studied Yersinia ruckeri antifeeding prophage 18 (Afp18), the toxin component of the phage tail-derived protein translocation system Afp, which causes enteric redmouth disease in salmonid fish species. Here we show that microinjection of the glycosyltransferase domain Afp18(G) into zebrafish embryos blocks cytokinesis, actin-dependent motility and cell blebbing, eventually abrogating gastrulation. In zebrafish ZF4 cells, Afp18(G) depolymerizes actin stress fibres by mono-O-GlcNAcylation of RhoA at tyrosine-34; thereby Afp18(G) inhibits RhoA activation by guanine nucleotide exchange factors, and blocks RhoA, but not Rac and Cdc42 downstream signalling. The crystal structure of tyrosine-GlcNAcylated RhoA reveals an open conformation of the effector loop distinct from recently described structures of GDP- or GTP-bound RhoA. Unravelling of the molecular mechanism of the toxin component Afp18 as glycosyltransferase opens new perspectives in studies of phage tail-derived protein translocation systems, which are preserved from archaea to human pathogenic prokaryotes.

Indexed as

AnimalsBacterial ToxinsBlastomeresCell MovementCytokinesisEmbryo, NonmammalianGlycosylationGlycosyltransferasesGuanine Nucleotide Exchange FactorsMonomeric GTP-Binding ProteinsProtein ConformationSignal TransductionTyrosineYersinia ruckeriZebrafishZebrafish ProteinsBacterial ToxinsGlycosyltransferasesGuanine Nucleotide Exchange FactorsMonomeric GTP-Binding Proteinsrhoab protein, zebrafishTyrosineZebrafish Proteins

Identifiers

PMID26190758
PMCPMC4518317
OpenAlexW2264302114

What OpenQuestion holds

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LicenceCC BY
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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.