ArticlePloS one2009
Fido, a novel AMPylation domain common to fic, doc, and AvrB.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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Who cites it
83 citing papers in PubMed, 132 citations in OpenAlex.
- The toxin-antitoxin complex Fic-1-AntF functions as a deAMPylase that regulates the activity of DNA gyrase.mLife · 2026Article
- Inhibition of FicD-mediated AMPylation and deAMPylation by isoprenoid diphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Ribonuclease RNase Z is an evolutionarily conserved deAMPylase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Pseudomonas gelidaquae sp. nov., an Antarctic bacterium with a distinctive Type III Secretion System, isolated from Fildes Bay, King George Island.Antonie van Leeuwenhoek · 2025Article
- Small-Molecule FICD Inhibitors Suppress Endogenous and Pathologic FICD-Mediated Protein AMPylation.ACS chemical biology · 2025Article
- Exploring the Role ofGenes · 2024Article
- Small molecule FICD inhibitors suppress endogenous and pathologic FICD-mediated protein AMPylation.bioRxiv : the preprint server for biology · 2024Article
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- The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3.Communications biology · 2023Article
- Type II bacterial toxin-antitoxins: hypotheses, facts, and the newfound plethora of the PezAT system.FEMS microbiology reviews · 2023Article
- Infancy-onset diabetes caused by de-regulated AMPylation of the human endoplasmic reticulum chaperone BiP.EMBO molecular medicine · 2023Article
- AMPylation of small GTPases by Fic enzymes.FEBS letters · 2023Review
- A secreted effector with a dual role as a toxin and as a transcriptional factor.Nature communications · 2022Article
- Evolutionary Diversification of Host-TargetedMicroorganisms · 2021Article
- Kinetic and structural parameters governing Fic-mediated adenylylation/AMPylation of the Hsp70 chaperone, BiP/GRP78.Cell stress & chaperones · 2021Article
- α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles.International journal of molecular sciences · 2021Review
- Fic and non-Fic AMPylases: protein AMPylation in metazoans.Open biology · 2021Article
- Identification of targets of AMPylating Fic enzymes by co-substrate-mediated covalent capture.Nature chemistry · 2020Article
- The Variety in the Common Theme of Translation Inhibition by Type II Toxin-Antitoxin Systems.Frontiers in genetics · 2020Review
23 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe Vibrio parahaemolyticus type III secreted effector VopS contains a fic domain that covalently modifies Rho GTPase threonine with AMP to inhibit downstream signaling events in host cells. The VopS fic domain includes a conserved sequence motif (HPFx[D/E]GN[G/K]R) that contributes to AMPylation. Fic domains are found in a variety of species, including bacteria, a few archaea, and metazoan eukaryotes. METHODOLOGY/PRINCIPAL
findingsWe show that the AMPylation activity extends to a eukaryotic fic domain in Drosophila melanogaster CG9523, and use sequence and structure based computational methods to identify related domains in doc toxins and the type III effector AvrB. The conserved sequence motif that contributes to AMPylation unites fic with doc. Although AvrB lacks this motif, its structure reveals a similar topology to the fic and doc folds. AvrB binds to a peptide fragment of its host virulence target in a similar manner as fic binds peptide substrate. AvrB also orients a phosphate group from a bound ADP ligand near the peptide-binding site and in a similar position as a bound fic phosphate. CONCLUSIONS/SIGNIFICANCE: The demonstrated eukaryotic fic domain AMPylation activity suggests that the VopS effector has exploited a novel host posttranslational modification. Fic domain-related structures give insight to the AMPylation active site and to the VopS fic domain interaction with its host GTPase target. These results suggest that fic, doc, and AvrB stem from a common ancestor that has evolved to AMPylate protein substrates.
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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.