ArticleProceedings of the National Academy of Sciences of the United States of America2014
The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 46 citations in OpenAlex.
- Targeting Type III Secretion System usingIndian journal of microbiology · 2025Review
- On the role of the sorting platform in hierarchical type III secretion regulation in enteropathogenicJournal of bacteriology · 2025Article
- Infection biology ofEcoSal Plus · 2024Review
- Salmonella Typhimurium exploits host polyamines for assembly of the type 3 secretion machinery.PLoS biology · 2024Article
- Robustness and the evolution of length control strategies in the T3SS and flagellar hook.Biophysical journal · 2021Article
- Type three secretion system in Salmonella Typhimurium: the key to infection.Genes & genomics · 2020Review
- T3S injectisome needle complex structures in four distinct states reveal the basis of membrane coupling and assembly.Nature microbiology · 2019Article
- A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion.PLoS biology · 2019Article
- Chaperone-mediated secretion switching from early to middle substrates in the type III secretion system encoded byThe Journal of biological chemistry · 2019Article
- The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells.EcoSal Plus · 2019Review
- Article
- Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells.FEMS microbiology letters · 2018Review
- A protein secreted by theeLife · 2018Article
- Protein-Injection Machines in Bacteria.Cell · 2018Review
- The inner-rod component of Shigella flexneri type 3 secretion system, MxiI, is involved in the transmission of the secretion activation signal by its interaction with MxiC.MicrobiologyOpen · 2018Article
- Assembly, structure, function and regulation of type III secretion systems.Nature reviews. Microbiology · 2017Review
- Recombinant Salmonella expressing SspH2-EscI fusion protein limits its colonization in mice.BMC immunology · 2017Article
- An Interaction between the Inner Rod Protein YscI and the Needle Protein YscF Is Required to Assemble the Needle Structure of theThe Journal of biological chemistry · 2017Article
- Characterization of the Ruler Protein Interaction Interface on the Substrate Specificity Switch Protein in theThe Journal of biological chemistry · 2017Article
- Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus.PLoS pathogens · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Type III secretion machines are essential for the biology of many bacteria that are pathogenic or symbiotic for animals, plants, or insects. They exert their function by delivering bacterial effector proteins into target eukaryotic cells. The core component of these machines is the needle complex, a multiprotein structure that spans the bacterial envelope and serves as a conduit for proteins that transit this secretion pathway. The needle complex is composed of a multiring base embedded in the bacterial envelope and a filament-like structure, the needle, that projects from the bacterial surface and is linked to the base by the inner rod. Assembly of the needle complex proceeds in a step-wise fashion that is initiated by the assembly of the base and is followed by the export of the building subunits for the needle and inner rod substructures. Once assembled, the needle complex reprograms its specificity and becomes competent for the secretion of effector proteins. Here through genetic, biochemical, and electron microscopy analyses of the Salmonella inner rod protein subunit PrgJ we present evidence that the assembly of the inner rod dictates the timing of substrate switching and needle length. Furthermore, the identification of mutations in PrgJ that specifically alter the hierarchy of protein secretion provides additional support for a complex role of the inner rod substructure in type III secretion.
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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.