ArticleThe Journal of biological chemistry2015
A novel phosphatidylinositol 4,5-bisphosphate binding domain mediates plasma membrane localization of ExoU and other patatin-like phospholipases.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 36 citations in OpenAlex.
- Topical formulation of repurposed FDA-approved compounds inhibits Pseudomonas aeruginosa ExoU and improves corneal infection outcomes.PLoS pathogens · 2026Article
- Patatin-domain-containing (phospho)lipases under control: Mammalian co-regulators and pathogenic activation mechanisms.FEBS open bio · 2026Review
- Virulence regulation in the fish pathogenFrontiers in cellular and infection microbiology · 2026Review
- The fatty liver disease-causing protein PNPLA3-I148M alters lipid droplet-Golgi dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The fatty liver disease-causing protein PNPLA3-I148M alters lipid droplet-Golgi dynamics.bioRxiv : the preprint server for biology · 2023Article
- Exploring structural features and potential lipid interactions of Pseudomonas aeruginosa type three secretion effector PemB by spectroscopic and calorimetric experiments.Protein science : a publication of the Protein Society · 2023Article
- Expression of the GFP-mammalian pleckstrin homology (PH) domain of the phospholipase C δ1 in Saccharomyces cerevisiae BY4741.Molecular biology reports · 2022Article
- 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
- Subversion of host cell signaling: The arsenal of Rickettsial species.Frontiers in cellular and infection microbiology · 2022Review
- Role of Host and Bacterial Lipids inFrontiers in immunology · 2022Review
- 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
- Review
- Interactions of the effector ExoU fromThe Journal of biological chemistry · 2019Article
- SopF, a phosphoinositide binding effector, promotes the stability of the nascent Salmonella-containing vacuole.PLoS pathogens · 2019Article
- Identification and Verification of Ubiquitin-Activated Bacterial Phospholipases.Journal of bacteriology · 2019Article
- Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins.Advances in experimental medicine and biology · 2019Review
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Bacterial toxins require localization to specific intracellular compartments following injection into host cells. In this study, we examined the membrane targeting of a broad family of bacterial proteins, the patatin-like phospholipases. The best characterized member of this family is ExoU, an effector of the Pseudomonas aeruginosa type III secretion system. Upon injection into host cells, ExoU localizes to the plasma membrane, where it uses its phospholipase A2 activity to lyse infected cells. The targeting mechanism of ExoU is poorly characterized, but it was recently found to bind to the phospholipid phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), a marker for the plasma membrane of eukaryotic cells. We confirmed that the membrane localization domain (MLD) of ExoU had a direct affinity for PI(4,5)P2, and we determined that this binding was required for ExoU localization. Previously uncharacterized ExoU homologs from Pseudomonas fluorescens and Photorhabdus asymbiotica also localized to the plasma membrane and required PI(4,5)P2 for this localization. A conserved arginine within the MLD was critical for interaction of each protein with PI(4,5)P2 and for localization. Furthermore, we determined the crystal structure of the full-length P. fluorescens ExoU and found that it was similar to that of P. aeruginosa ExoU. Each MLD contains a four-helical bundle, with the conserved arginine exposed at its cap to allow for interaction with the negatively charged PI(4,5)P2. Overall, these findings provide a structural explanation for the targeting of patatin-like phospholipases to the plasma membrane and define the MLD of ExoU as a member of a new class of PI(4,5)P2 binding domains.
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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.