ArticleNature communications2024
The Shigella kinase effector OspG modulates host ubiquitin signaling to escape septin-cage entrapment.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Cell-autonomous immunity as an integrated immune network against bacterial and viral pathogens.Nature microbiology · 2026Review
- Septin crosstalk with microtubules and actin is regulated by a GSK3-dependent phosphoswitch.bioRxiv : the preprint server for biology · 2026Article
- Profiling Selectivity for theBiochemistry · 2026Article
- Shigella flexneri evades septin-mediated cell-autonomous immunity via protein ADP-riboxanation.Nature communications · 2026Article
- Modulation of host functions by bacterial serine/threonine protein kinase effector proteins.The Journal of biological chemistry · 2025Review
- Molecular mechanisms of co-infections.EMBO reports · 2025Review
- Shigella effector IpaH1.4 subverts host E3 ligase RNF213 to evade antibacterial immunity.Nature communications · 2025Article
- Review
- The great escape: a Shigella effector unlocks the septin cage.Nature communications · 2024Article
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14 authors.
Funding
Abstract
Shigella flexneri is a Gram-negative bacterium causing severe bloody dysentery. Its pathogenesis is largely dictated by a plasmid-encoded type III secretion system (T3SS) and its associated effectors. Among these, the effector OspG has been shown to bind to the ubiquitin conjugation machinery (E2~Ub) to activate its kinase activity. However, the cellular targets of OspG remain elusive despite years of extensive efforts. Here we show by unbiased phosphoproteomics that a major target of OspG is CAND1, a regulatory protein controlling the assembly of cullin-RING ubiquitin ligases (CRLs). CAND1 phosphorylation weakens its interaction with cullins, which is expected to impact a large panel of CRL E3s. Indeed, global ubiquitome profiling reveals marked changes in the ubiquitination landscape when OspG is introduced. Notably, OspG promotes ubiquitination of a class of cytoskeletal proteins called septins, thereby inhibiting formation of cage-like structures encircling cytosolic bacteria. Overall, we demonstrate that pathogens have evolved an elaborate strategy to modulate host ubiquitin signaling to evade septin-cage entrapment.
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