ArticleNature communications2022
Direct interaction of a chaperone-bound type III secretion substrate with the export gate.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Function and Global Regulation of Type III Secretion System and Flagella in Entomopathogenic Nematode Symbiotic Bacteria.International journal of molecular sciences · 2024Article
- The impact of AI-based modeling on the accuracy of protein assembly prediction: Insights from CASP15.Proteins · 2023Article
- The Impact of AI-Based Modeling on the Accuracy of Protein Assembly Prediction: Insights from CASP15.bioRxiv : the preprint server for biology · 2023Article
- Virulence-associated type III secretion systems in Gram-negative bacteria.Microbiology (Reading, England) · 2023Review
- The type III secretion chaperone SctY may shield the hydrophobic export gate-binding C-terminus of its substrate SctX.Acta crystallographica. Section D, Structural biology · 2023Article
- Crystals of SctV from different species reveal variable symmetry for the cytosolic domain of the type III secretion system export gate.Acta crystallographica. Section F, Structural biology communications · 2022Article
- The NEL Family of Bacterial E3 Ubiquitin Ligases.International journal of molecular sciences · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several gram-negative bacteria employ type III secretion systems (T3SS) to inject effector proteins into eukaryotic host cells directly from the bacterial cytoplasm. The export gate SctV (YscV in Yersinia) binds substrate:chaperone complexes such as YscX:YscY, which are essential for formation of a functional T3SS. Here, we present structures of the YscX:YscY complex alone and bound to nonameric YscV. YscX binds its chaperone YscY at two distinct sites, resembling the heterotrimeric complex of the T3SS needle subunit with its chaperone and co-chaperone. In the ternary complex the YscX N-terminus, which mediates YscX secretion, occupies a binding site within one YscV that is also used by flagellar chaperones, suggesting the interaction's importance for substrate recognition. The YscX C-terminus inserts between protomers of the YscV ring where the stalk protein binds to couple YscV to the T3SS ATPase. This primary YscV-YscX interaction is essential for the formation of a secretion-competent T3SS.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.