ArticlePLoS pathogens2019
Structural mechanism for guanylate-binding proteins (GBPs) targeting by the Shigella E3 ligase IpaH9.8.
Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 60 citations in OpenAlex.
- NLRP1B is an integrated decoy that subvertsProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanisms driving open-closed transitions and dimer stability of the large GTPases hGBP1 and hGBP5.Frontiers in molecular biosciences · 2026Article
- TheeLife · 2025Article
- Post-translational weapons of microbial warfare: how bacterial effectors hijack host cell death and xenophagy.Cell communication and signaling : CCS · 2025Review
- Deciphering the origins of guanylate-binding proteins in mammals (Monotreme, Marsupials and Placentals).BMC biology · 2025Article
- Shigella flexneri evades LPS ubiquitylation through IpaH1.4-mediated degradation of RNF213.Nature structural & molecular biology · 2025Article
- ThebioRxiv : the preprint server for biology · 2025Article
- Inter-kingdom signaling by the Legionella autoinducer LAI-1 involves the antimicrobial guanylate binding protein GBP.PLoS pathogens · 2025Article
- Crystal structures reveal nucleotide-induced conformational changes in G motifs and distal regions in human guanylate-binding protein 2.Communications biology · 2025Article
- Structural basis of antimicrobial membrane coat assembly by human GBP1.Nature structural & molecular biology · 2025Article
- Autophagy and Bacterial infections.Autophagy reports · 2025Review
- Review
- Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024Review
- Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection.Science (New York, N.Y.) · 2024Article
- Structural insights into the activation mechanism of antimicrobial GBP1.The EMBO journal · 2024Article
- Ubiquitin-targeted bacterial effectors: rule breakers of the ubiquitin system.The EMBO journal · 2023Review
- Article
- Functional cross-species conservation of guanylate-binding proteins in innate immunity.Medical microbiology and immunology · 2023Review
- Structural mechanisms of calmodulin activation of Shigella effector OspC3 to ADP-riboxanate caspase-4/11 and block pyroptosis.Nature structural & molecular biology · 2023Article
- Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The guanylate-binding proteins (GBPs) belong to the dynamin superfamily of GTPases and function in cell-autonomous defense against intracellular pathogens. IpaH9.8, an E3 ligase from the pathogenic bacterium Shigella flexneri, ubiquitinates a subset of GBPs and leads to their proteasomal degradation. Here we report the structure of a C-terminally truncated GBP1 in complex with the IpaH9.8 Leucine-rich repeat (LRR) domain. IpaH9.8LRR engages the GTPase domain of GBP1, and differences in the Switch II and α3 helix regions render some GBPs such as GBP3 and GBP7 resistant to IpaH9.8. Comparisons with other IpaH structures uncover interaction hot spots in their LRR domains. The C-terminal region of GBP1 undergoes a large rotation compared to previously determined structures. We further show that the C-terminal farnesylation modification also plays a role in regulating GBP1 conformation. Our results suggest a general mechanism by which the IpaH proteins target their cellular substrates and shed light on the structural dynamics of the GBPs.
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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.