ArticleThe Journal of biological chemistry2013
Identification of the major ubiquitin-binding domain of the Pseudomonas aeruginosa ExoU A2 phospholipase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Who cites it
25 citing papers in PubMed, 34 citations in OpenAlex.
- Patatin-domain-containing (phospho)lipases under control: Mammalian co-regulators and pathogenic activation mechanisms.FEBS open bio · 2026Review
- Site-directed spin label EPR studies of the structure and membrane interactions of the bacterial phospholipase ExoU.Applied magnetic resonance · 2024Article
- chiLife: An open-source Python package for in silico spin labeling and integrative protein modeling.PLoS computational biology · 2023Article
- Review
- The Pseudomonas aeruginosa Type III Secretion System Exoenzyme Effector ExoU Induces Mitochondrial Damage in a Murine Bone Marrow-Derived Macrophage Infection Model.Infection and immunity · 2022Article
- ExoU Induces Lung Endothelial Cell Damage and Activates Pro-Inflammatory Caspase-1 duringToxins · 2022Article
- Perspectives on theToxins · 2021Review
- The bacterial toxin ExoU requires a host trafficking chaperone for transportation and to induce necrosis.Nature communications · 2021Article
- A pipeline to evaluate inhibitors of the Pseudomonas aeruginosa exotoxin U.The Biochemical journal · 2021Article
- Characterization of the ExoU activation mechanism using EPR and integrative modeling.Scientific reports · 2020Article
- Interactions of the effector ExoU fromThe Journal of biological chemistry · 2019Article
- Identification and Verification of Ubiquitin-Activated Bacterial Phospholipases.Journal of bacteriology · 2019Article
- Identification of a ubiquitin-binding interface using Rosetta and DEER.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Exploitation of the host cell ubiquitin machinery by microbial effector proteins.Journal of cell science · 2017Review
- Cooperative Substrate-Cofactor Interactions and Membrane Localization of the Bacterial Phospholipase AThe Journal of biological chemistry · 2017Article
- Bacterial Sphingomyelinases and Phospholipases as Virulence Factors.Microbiology and molecular biology reviews : MMBR · 2016Review
- Chitinase 3-Like 1 (Chil1) Regulates Survival and Macrophage-Mediated Interleukin-1β and Tumor Necrosis Factor Alpha during Pseudomonas aeruginosa Pneumonia.Infection and immunity · 2016Article
- Lysine11-Linked Polyubiquitination of the AnkB F-Box Effector of Legionella pneumophila.Infection and immunity · 2016Article
- Ubiquitin activates patatin-like phospholipases from multiple bacterial species.Journal of bacteriology · 2015Article
- Association between Pseudomonas aeruginosa type III secretion, antibiotic resistance, and clinical outcome: a review.Critical care (London, England) · 2014Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Numerous Gram-negative bacterial pathogens use type III secretion systems to deliver effector molecules into the cytoplasm of a host cell. Many of these effectors have evolved to manipulate the host ubiquitin system to alter host cell physiology or the location, stability, or function of the effector itself. ExoU is a potent A2 phospholipase used by Pseudomonas aeruginosa to destroy membranes of infected cells. The enzyme is held in an inactive state inside of the bacterium due to the absence of a required eukaryotic activator, which was recently identified as ubiquitin. This study sought to identify the region of ExoU required to mediate this interaction and determine the properties of ubiquitin important for binding, ExoU activation, or both. Biochemical and biophysical approaches were used to map the ubiquitin-binding domain to a C-terminal four-helix bundle of ExoU. The hydrophobic patch of ubiquitin is required for full binding affinity and activation. Binding and activation were uncoupled by introducing an L8R substitution in ubiquitin. Purified L8R demonstrated a parental binding phenotype to ExoU but did not activate the phospholipase in vitro. Utilizing these new biochemical data and intermolecular distance measurements by double electron-electron resonance, we propose a model for an ExoU-monoubiquitin complex.
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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.