Evidence map›Paper›PMID 25301945›Full record

ArticleThe Journal of biological chemistry2014

AMPylation of Rho GTPases subverts multiple host signaling processes.

Andrew R Woolery, Xiaobo Yu, Joshua LaBaer, Kim Orth

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. 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
2.8field-weighted citation impact, top 9% 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, 45 citations in OpenAlex.

  1. AMPylation: key roles in biological regulation across prokaryotes and eukaryotes.Frontiers in cellular and infection microbiology · 2026
    Review
  2. Article
  3. Article
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  5. Review
  6. Article
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  9. Bacterial Toxin and Effector Regulation of Intestinal Immune Signaling.Frontiers in cell and developmental biology · 2022
    Review
  10. Article
  11. Article
  12. Review
  13. MS-BasedACS infectious diseases · 2020
    Article
  14. TheScience signaling · 2020
    Article
  15. Article
  16. Article
  17. Review
  18. Bio-protocol · 2017
    Article
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  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

4 authors at 2 institutions in 1 country.

Andrew R WooleryFrom the Department of Molecular Biology, UT Southwestern Medical Center, Dallas, Texas 75390-9148 and.
Xiaobo YuThe Virginia G. Piper Center for Personalized Diagnostics, Biodesign Institute, Arizona State University, Tempe, Arizona 85287.
Joshua LaBaerThe Virginia G. Piper Center for Personalized Diagnostics, Biodesign Institute, Arizona State University, Tempe, Arizona 85287.
Kim OrthFrom the Department of Molecular Biology, UT Southwestern Medical Center, Dallas, Texas 75390-9148 and Kim.Orth@utsouthwestern.edu.
Arizona State University · USThe University of Texas Southwestern Medical Center · US

Funding

DIVISION OF CELL &MOLECULAR BIOLOGY TRAINING PROGRAMT32GM008203 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI COBB, MELANIE H. · 1987 to 2018
$7.0M
Biomarker Detection Using NAPPA Tumor Antigen ArraysU01CA117374 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI ANDERSON, KAREN SUE, LABAER, JOSHUA · 2005 to 2015
$6.2M
Analysis of an orchestrated cell death mediated by Vibrio parahaemolytics T3SS1R01AI087808 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2010 to 2014
$1.9M
NCI NIH HHS 5U01CA117374NCI NIH HHS U01 CA117374NIAID NIH HHS R01 AI087808NIAID NIH HHS R01-AI087808NIGMS NIH HHS 5T32GM008203
6 · The paper itself

Abstract

Rho GTPases are frequent targets of virulence factors as they are keystone signaling molecules. Herein, we demonstrate that AMPylation of Rho GTPases by VopS is a multifaceted virulence mechanism that counters several host immunity strategies. Activation of NFκB, Erk, and JNK kinase signaling pathways were inhibited in a VopS-dependent manner during infection with Vibrio parahaemolyticus. Phosphorylation and degradation of IKBα were inhibited in the presence of VopS as was nuclear translocation of the NFκB subunit p65. AMPylation also prevented the generation of superoxide by the phagocytic NADPH oxidase complex, potentially by inhibiting the interaction of Rac and p67. Furthermore, the interaction of GTPases with the E3 ubiquitin ligases cIAP1 and XIAP was hindered, leading to decreased degradation of Rac and RhoA during infection. Finally, we screened for novel Rac1 interactions using a nucleic acid programmable protein array and discovered that Rac1 binds to the protein C1QA, a protein known to promote immune signaling in the cytosol. Interestingly, this interaction was disrupted by AMPylation. We conclude that AMPylation of Rho Family GTPases by VopS results in diverse inhibitory consequences during infection beyond the most obvious phenotype, the collapse of the actin cytoskeleton.

Indexed as

Signal TransductionActive Transport, Cell NucleusAdenosine MonophosphateBacterial ProteinsCell NucleusComplement C1qHEK293 CellsHost-Pathogen InteractionsHumansI-kappa B KinaseImmunoblottingInhibitor of Apoptosis ProteinsMicroscopy, ConfocalModels, BiologicalPhosphorylationProtein BindingAdenosine MonophosphateBacterial ProteinsComplement C1qI-kappa B KinaseInhibitor of Apoptosis Proteinsrac1 GTP-Binding Proteinrho GTP-Binding ProteinsSuperoxidesTranscription Factor RelAX-Linked Inhibitor of Apoptosis ProteinAMPAMPylationC1qAGTPaseIAPNF-κB (NF-KB)RhoGTPasesRho (Rho GTPase)Signal TransductionVopS

Identifiers

PMID25301945
PMCPMC4239643
OpenAlexW2032118563

What OpenQuestion holds

Textmetadata
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.