ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structural basis for the recruitment and activation of the Legionella phospholipase VipD by the host GTPase Rab5.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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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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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.
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Who cites it
29 citing papers in PubMed, 52 citations in OpenAlex.
- A novel RAB5 binding site in human VPS34-CII that is likely the primordial site in eukaryotic evolution.eLife · 2026Article
- Patatin-domain-containing (phospho)lipases under control: Mammalian co-regulators and pathogenic activation mechanisms.FEBS open bio · 2026Review
- Legionella effector protein SidG disrupts host cytoskeleton via targeting Arp2/3 complex.PLoS pathogens · 2026Article
- Article
- Genetic evidence for a regulated cysteine protease catalytic triad in LegA7, abioRxiv : the preprint server for biology · 2024Article
- Article
- Eat or Be Eaten: Strategies Used byInfection and immunity · 2023Review
- Metagenome diversity illuminates origins of pathogen effectors.bioRxiv : the preprint server for biology · 2023Article
- VpdC is a ubiquitin-activated phospholipase effector that regulatesProceedings of the National Academy of Sciences of the United States of America · 2022Article
- New Global Insights on the Regulation of the Biphasic Life Cycle and Virulence Via ClpP-Dependent Proteolysis in Legionella pneumophila.Molecular & cellular proteomics : MCP · 2022Article
- Modulation of phagosome phosphoinositide dynamics by a Legionella phosphoinositide 3-kinase.EMBO reports · 2021Article
- Characterization of the ExoU activation mechanism using EPR and integrative modeling.Scientific reports · 2020Article
- How to choose templates for modeling of protein complexes: Insights from benchmarking template-based docking.Proteins · 2020Article
- Glucosylation by the Legionella Effector SetA Promotes the Nuclear Localization of the Transcription Factor TFEB.iScience · 2020Article
- Components of the endocytic and recycling trafficking pathways interfere with the integrity of the Legionella-containing vacuole.Cellular microbiology · 2020Article
- Phosphoinositides and the Fate ofFrontiers in immunology · 2020Review
- Identification and Verification of Ubiquitin-Activated Bacterial Phospholipases.Journal of bacteriology · 2019Article
- Rab GTPases and their interacting protein partners: Structural insights into Rab functional diversity.Small GTPases · 2018Review
- Subversion of the Endocytic and Secretory Pathways by Bacterial Effector Proteins.Frontiers in cell and developmental biology · 2018Review
- Probing the druggability of membrane-bound Rab5 by molecular dynamics simulations.Journal of enzyme inhibition and medicinal chemistry · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
A challenge for microbial pathogens is to assure that their translocated effector proteins target only the correct host cell compartment during infection. The Legionella pneumophila effector vacuolar protein sorting inhibitor protein D (VipD) localizes to early endosomal membranes and alters their lipid and protein composition, thereby protecting the pathogen from endosomal fusion. This process requires the phospholipase A1 (PLA1) activity of VipD that is triggered specifically on VipD binding to the host cell GTPase Rab5, a key regulator of endosomes. Here, we present the crystal structure of VipD in complex with constitutively active Rab5 and reveal the molecular mechanism underlying PLA1 activation. An active site-obstructing loop that originates from the C-terminal domain of VipD is repositioned on Rab5 binding, thereby exposing the catalytic pocket within the N-terminal PLA1 domain. Substitution of amino acid residues located within the VipD-Rab5 interface prevented Rab5 binding and PLA1 activation and caused a failure of VipD mutant proteins to target to Rab5-enriched endosomal structures within cells. Experimental and computational analyses confirmed an extended VipD-binding interface on Rab5, explaining why this L. pneumophila effector can compete with cellular ligands for Rab5 binding. Together, our data explain how the catalytic activity of a microbial effector can be precisely linked to its subcellular localization.
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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.