ArticleThe Journal of experimental medicine2010
Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila.
Article in The Journal of experimental medicine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
What it found
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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.
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Who cites it
83 citing papers in PubMed, 126 citations in OpenAlex.
- Host prenylation promotes membrane association of theMicrobiology (Reading, England) · 2026Article
- Localization of the PelC and PelE effectors to theInfection and immunity · 2026Article
- Protein farnesylation: from molecular mechanisms to therapeutic targeting in cancer, aging, and beyond.Frontiers in pharmacology · 2026Review
- In Vitro synergy of Farnesyltransferase inhibitors in combination with colistin against ESKAPE bacteria.PloS one · 2025Article
- Review
- Brucella effectors NyxA and NyxB target SENP3 to modulate the subcellular localisation of nucleolar proteins.Nature communications · 2023Article
- Poxviral ANKR/F-box Proteins: Substrate Adapters for Ubiquitylation and More.Pathogens (Basel, Switzerland) · 2022Review
- A Search for NovelFrontiers in cellular and infection microbiology · 2022Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Evolution and Adaptation ofBiomolecules · 2021Review
- The Ecology and Evolution of Amoeba-Bacterium Interactions.Applied and environmental microbiology · 2021Review
- Bacteria Are New Targets for Inhibitors of Human Farnesyltransferase.Frontiers in microbiology · 2021Article
- Structure-Based Deep Mining Reveals First-Time Annotations for 46 Percent of the Dark Annotation Space of the 9,671-Member Superproteome of the Nucleocytoplasmic Large DNA Viruses.Journal of virology · 2020Article
- Review
- Structural insight into the membrane targeting domain of the Legionella deAMPylase SidD.PLoS pathogens · 2020Article
- Phosphoinositides and the Fate ofFrontiers in immunology · 2020Review
- Article
- Nutrition and Bipartite Metabolism of Intracellular Pathogens.Trends in microbiology · 2019Review
- Intracellular parasitism, the driving force of evolution of Legionella pneumophila and the genus Legionella.Genes and immunity · 2019Review
- Evasion of phagotrophic predation by protist hosts and innate immunity of metazoan hosts by Legionella pneumophila.Cellular microbiology · 2019Review
23 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Farnesylation involves covalent linkage of eukaryotic proteins to a lipid moiety to anchor them into membranes, which is essential for the biological function of Ras and other proteins. A large cadre of bacterial effectors is injected into host cells by intravacuolar pathogens through elaborate type III-VII translocation machineries, and many of these effectors are incorporated into the pathogen-containing vacuolar membrane by unknown mechanisms. The Dot/Icm type IV secretion system of Legionella pneumophila injects into host cells the F-box effector Ankyrin B (AnkB), which functions as platforms for the docking of polyubiquitinated proteins to the Legionella-containing vacuole (LCV) to enable intravacuolar proliferation in macrophages and amoeba. We show that farnesylation of AnkB is indispensable for its anchoring to the cytosolic face of the LCV membrane, for its biological function within macrophages and Dictyostelium discoideum, and for intrapulmonary proliferation in mice. Remarkably, the protein farnesyltransferase, RCE-1 (Ras-converting enzyme-1), and isoprenyl cysteine carboxyl methyltransferase host farnesylation enzymes are recruited to the LCV in a Dot/Icm-dependent manner and are essential for the biological function of AnkB. In conclusion, this study shows novel localized recruitment of the host farnesylation machinery and its anchoring of an F-box effector to the LCV membrane, and this is essential for biological function in vitro and in vivo.
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Registered trials
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.