ArticleThe Journal of biological chemistry2013
Escherichia coli virulence protein NleH1 interaction with the v-Crk sarcoma virus CT10 oncogene-like protein (CRKL) governs NleH1 inhibition of the ribosomal protein S3 (RPS3)/nuclear factor κB (NF-κB) pathway.
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 17 papers.
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17 citing papers in PubMed, 25 citations in OpenAlex.
- Modulation of host functions by bacterial serine/threonine protein kinase effector proteins.The Journal of biological chemistry · 2025Review
- Bacterial effector kinases and strategies to identify their target host substrates.Frontiers in microbiology · 2023Review
- Targeting of microvillus protein Eps8 by the NleH effector kinases from enteropathogenicProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- A bacterial kinase phosphorylates OSK1 to suppress stomatal immunity in rice.Nature communications · 2021Article
- Identification of a Family ofmSphere · 2021Article
- The Effect of Interferons on Presentation of Defective Ribosomal Products as HLA Peptides.Molecular & cellular proteomics : MCP · 2021Article
- Molecular Mechanisms That Define Redox Balance Function in Pathogen-Host Interactions-Is There a Role for Dietary Bioactive Polyphenols?International journal of molecular sciences · 2019Review
- Hsp90 Interacts with the Bacterial Effector NleH1.Pathogens (Basel, Switzerland) · 2018Article
- EPEC NleH1 is significantly more effective in reversing colitis and reducing mortality than NleH2 via differential effects on host signaling pathways.Laboratory investigation; a journal of technical methods and pathology · 2018Article
- Cooperative Immune Suppression by Escherichia coli and Shigella Effector Proteins.Infection and immunity · 2018Review
- Bacterial virulence factor inhibits caspase-4/11 activation in intestinal epithelial cells.Mucosal immunology · 2017Article
- Modulation of host signaling in the inflammatory response by enteropathogenic Escherichia coli virulence proteins.Cellular & molecular immunology · 2017Review
- Interference with nuclear factor kappaB signaling pathway by pathogen-encoded proteases: global and selective inhibition.Molecular microbiology · 2016Review
- Structural insight into effector proteins of Gram-negative bacterial pathogens that modulate the phosphoproteome of their host.Protein science : a publication of the Protein Society · 2015Review
- Bacterial serine/threonine protein kinases in host-pathogen interactions.The Journal of biological chemistry · 2014Review
- Contribution of Crk adaptor proteins to host cell and bacteria interactions.BioMed research international · 2014Review
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4 authors at 2 institutions in 1 country.
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Abstract
Enterohemorrhagic Escherichia coli and other attaching/effacing bacterial pathogens cause diarrhea in humans. These pathogens use a type III secretion system to inject virulence proteins (effectors) into host cells, some of which inhibit the innate immune system. The enterohemorrhagic E. coli NleH1 effector prevents the nuclear translocation of RPS3 (ribosomal protein S3) to inhibit its participation as a nuclear "specifier" of NF-κB binding to target gene promoters. NleH1 binds to RPS3 and inhibits its phosphorylation on Ser-209 by IκB kinase-β (IKKβ). However, the precise mechanism of this inhibition is unclear. NleH1 possesses a Ser/Thr protein kinase activity that is essential both for its ability to inhibit the RPS3/NF-κB pathway and for full virulence of the attaching/effacing mouse pathogen Citrobacter rodentium. However, neither RPS3 nor IKKβ is a substrate of NleH1 kinase activity. We therefore screened ∼9,000 human proteins to identify NleH1 kinase substrates and identified CRKL (v-Crk sarcoma virus CT10 oncogene-like protein), a substrate of the BCR/ABL kinase. Knockdown of CRKL abundance prevented NleH1 from inhibiting RPS3 nuclear translocation and NF-κB activity. CRKL residues Tyr-198 and Tyr-207 were required for interaction with NleH1. Lys-159, the kinase-active site of NleH1, was necessary for its interaction with CRKL. We also identified CRKL as an IKKβ interaction partner, mediated by CRKL Tyr-198. We propose that the CRKL interaction with IKKβ recruits NleH1 to the IKKβ complex, where NleH1 then inhibits the RPS3/NF-κB pathway.
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