ArticleeLife2022
Recognition of discrete export signals in early flagellar subunits during bacterial type III secretion.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 14 citations in OpenAlex.
- Active removal of inhibitory components drives the flagellar type 3 secretion-specificity switch.mBio · 2026Article
- Structure of the proton-powered secretion motor at the heart of the bacterial flagellum.bioRxiv : the preprint server for biology · 2026Article
- Active removal of inhibitory components drives the flagellar Type III Secretion Specificity Switch.bioRxiv : the preprint server for biology · 2026Article
- The Salmonella pathogenicity island 1 injectisome reprograms host cell translation to evade the inflammatory response.Nature communications · 2025Article
- A β-cap on the FliPQR protein-export channel acts as the cap for initial flagellar rod assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- On the role of the sorting platform in hierarchical type III secretion regulation in enteropathogenicJournal of bacteriology · 2025Article
- FliH and FliI help FlhA bring strict order to flagellar protein export in Salmonella.Communications biology · 2024Article
- Article
- Cytosolic sorting platform complexes shuttle type III secretion system effectors to the injectisome in Yersinia enterocolitica.Nature microbiology · 2024Article
- Salmonella typhimurium targeting with monoclonal antibodies prevents infection in mice.PLoS neglected tropical diseases · 2023Article
- An overview of the structure and function of the flagellar hook FlgE protein.World journal of microbiology & biotechnology · 2023Review
- Targeting early proximal-rod component substrate FlgB to FlhB for flagellar-type III secretion in Salmonella.PLoS genetics · 2022Article
- Recognition of discrete export signals in early flagellar subunits during bacterial type III secretion.eLife · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Type III Secretion Systems (T3SS) deliver subunits from the bacterial cytosol to nascent cell surface flagella. Early flagellar subunits that form the rod and hook substructures are unchaperoned and contain their own export signals. A gate recognition motif (GRM) docks them at the FlhBc component of the FlhAB-FliPQR export gate, but the gate must then be opened and subunits must be unfolded to pass through the flagellar channel. This induced us to seek further signals on the subunits. Here, we identify a second signal at the extreme N-terminus of flagellar rod and hook subunits and determine that key to the signal is its hydrophobicity. We show that the two export signal elements are recognised separately and sequentially, as the N-terminal signal is recognised by the flagellar export machinery only after subunits have docked at FlhB
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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.