ArticlePLoS pathogens2014
A gatekeeper chaperone complex directs translocator secretion during type three secretion.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Class II chaperones: indispensable components of the Gram-negative bacterial T3SS as guardians of translocators.Archives of microbiology · 2026Review
- Calcium controls type III secretion switch through an SctV-SctW interplay.Frontiers in microbiology · 2026Article
- On the role of the sorting platform in hierarchical type III secretion regulation in enteropathogenicJournal of bacteriology · 2025Article
- Crystallographic Fragment Screening on theACS omega · 2023Article
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Direct interaction of a chaperone-bound type III secretion substrate with the export gate.Nature communications · 2022Article
- Structural and Functional Analysis of SsaV Cytoplasmic Domain and Variable Linker States in the Context of the InvA-SsaV Chimeric Protein.Microbiology spectrum · 2021Article
- Structure of the cytoplasmic domain of SctV (SsaV) from the Salmonella SPI-2 injectisome and implications for a pH sensing mechanism.Journal of structural biology · 2021Article
- α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles.International journal of molecular sciences · 2021Review
- The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019Review
- Insight into microtubule nucleation from tubulin-capping proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Novel insights into the mechanism of SepL-mediated control of effector secretion in enteropathogenic Escherichia coli.MicrobiologyOpen · 2018Article
- Hierarchical protein targeting and secretion is controlled by an affinity switch in the type III secretion system of enteropathogenicThe EMBO journal · 2017Article
- Regulation of Type III Secretion of Translocon and Effector Proteins by the EsaB/EsaL/EsaM Complex in Edwardsiella tarda.Infection and immunity · 2017Article
- Assembly, structure, function and regulation of type III secretion systems.Nature reviews. Microbiology · 2017Review
- Steps for Shigella Gatekeeper Protein MxiC Function in Hierarchical Type III Secretion Regulation.The Journal of biological chemistry · 2017Article
- MxiA, MxiC and IpaD Regulate Substrate Selection and Secretion Mode in the T3SS of Shigella flexneri.PloS one · 2016Article
- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
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2 authors.
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Abstract
Many Gram-negative bacteria use Type Three Secretion Systems (T3SS) to deliver effector proteins into host cells. These protein delivery machines are composed of cytosolic components that recognize substrates and generate the force needed for translocation, the secretion conduit, formed by a needle complex and associated membrane spanning basal body, and translocators that form the pore in the target cell. A defined order of secretion in which needle component proteins are secreted first, followed by translocators, and finally effectors, is necessary for this system to be effective. While the secreted effectors vary significantly between organisms, the ∼20 individual protein components that form the T3SS are conserved in many pathogenic bacteria. One such conserved protein, referred to as either a plug or gatekeeper, is necessary to prevent unregulated effector release and to allow efficient translocator secretion. The mechanism by which translocator secretion is promoted while effector release is inhibited by gatekeepers is unknown. We present the structure of the Chlamydial gatekeeper, CopN, bound to a translocator-specific chaperone. The structure identifies a previously unknown interface between gatekeepers and translocator chaperones and reveals that in the gatekeeper-chaperone complex the canonical translocator-binding groove is free to bind translocators. Structure-based mutagenesis of the homologous complex in Shigella reveals that the gatekeeper-chaperone-translocator complex is essential for translocator secretion and for the ordered secretion of translocators prior to effectors.
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