ArticleMolecular and cellular biology2014
Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase.
Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers, 1 of them a synthesis that pooled it.
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Who cites it
57 citing papers in PubMed, 1 synthesis or guideline pooled it, 99 citations in OpenAlex.
- Recent progress in molecular mechanisms of Salmonella effectors involved in gut epithelium invasion.Molecular biology reports · 2025Pooled it
- Review
- Ubiquitination and autophagy in host-pathogen interactions: from immune surveillance to therapeutic targeting.Nature reviews. Immunology · 2026Review
- Covalent fragment screening to inhibit the E3 ligase activity of bacterial NEL enzymes SspH1 and SspH2.RSC chemical biology · 2026Article
- IPTG- and estradiol-inducible gene expression systems in the unicellular red alga Cyanidioschyzon merolae.Plant physiology · 2026Article
- Shigella flexneri evades LPS ubiquitylation through IpaH1.4-mediated degradation of RNF213.Nature structural & molecular biology · 2025Article
- Nucleomodulins from gut bacteria: diverse mechanisms of translocation and interaction with host nuclear processes.Applied and environmental microbiology · 2025Review
- Tracing the evolution: the rise ofmSystems · 2025Article
- Infection biology ofEcoSal Plus · 2024Review
- TheBiochemistry · 2024Article
- Protein destroyer: Inducible E3-DART for targeted protein degradation in plants.The Plant cell · 2024Article
- Rapid depletion of target proteins in plants by an inducible protein degradation system.The Plant cell · 2024Article
- Specificities and redundancies in the NEL family of bacterial E3 ubiquitin ligases ofFrontiers in immunology · 2024Article
- Strategies adopted by Salmonella to survive in host: a review.Archives of microbiology · 2023Review
- Ubiquitin-targeted bacterial effectors: rule breakers of the ubiquitin system.The EMBO journal · 2023Review
- Speaking the host language: howMicrobiology (Reading, England) · 2023Review
- A host E3 ubiquitin ligase regulatesmLife · 2023Article
- Article
- Insights into the GSDMB-mediated cellular lysis and its targeting by IpaH7.8.Nature communications · 2023Article
- Manipulation of host immune defenses by effector proteins delivered from multiple secretion systems ofFrontiers in immunology · 2023Review
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
Abstract
IpaH proteins are bacterium-specific E3 enzymes that function as type three secretion system (T3SS) effectors in Salmonella, Shigella, and other Gram-negative bacteria. IpaH enzymes recruit host substrates for ubiquitination via a leucine-rich repeat (LRR) domain, which can inhibit the catalytic domain in the absence of substrate. The basis for substrate recognition and the alleviation of autoinhibition upon substrate binding is unknown. Here, we report the X-ray structure of Salmonella SspH1 in complex with human PKN1. The LRR domain of SspH1 interacts specifically with the HR1b coiled-coil subdomain of PKN1 in a manner that sterically displaces the catalytic domain from the LRR domain, thereby activating catalytic function. SspH1 catalyzes the ubiquitination and proteasome-dependent degradation of PKN1 in cells, which attenuates androgen receptor responsiveness but not NF-κB activity. These regulatory features are conserved in other IpaH-substrate interactions. Our results explain the mechanism whereby substrate recognition and enzyme autoregulation are coupled in this class of bacterial ubiquitin ligases.
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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.