ArticleProceedings of the National Academy of Sciences of the United States of America2014
Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins.
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 89 papers.
What it found
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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.
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Who cites it
89 citing papers in PubMed, 126 citations in OpenAlex.
- Structural and functional insights into the Rcs phosphorelay.bioRxiv : the preprint server for biology · 2026Article
- Structures of folding intermediates on BAM show diverse substrates fold by a conserved mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2026Review
- AGPAT1 is a novel Chikungunya virus receptor on human cells.Journal of virology · 2026Article
- Liganded LolCDE structures reveal a common substrate-LolE interaction guiding bacterial lipoprotein transport.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Effects of Lipopolysaccharide Core Modulation on Outer Membrane Protein Function and Virulence in Pectobacterium carotovorum.Molecular plant pathology · 2026Article
- Modulation of bacterial cell size and growth rate via activation of a cell envelope stress response.mBio · 2025Article
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
- Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota.Nature microbiology · 2025Article
- Complex interplay between gene deletions and the environment uncovers cellular roles for genes of unknown function inmSystems · 2025Article
- Surface lipoprotein sorting by crosstalk between Lpt and Lol pathways in gram-negative bacteria.Nature communications · 2025Article
- Breaking Barriers: Exploiting Envelope Biogenesis and Stress Responses to Develop Novel Antimicrobial Strategies in Gram-Negative Bacteria.Pathogens (Basel, Switzerland) · 2024Review
- Molecular insights into the initiation step of the Rcs signaling pathway.Structure (London, England : 1993) · 2024Article
- Signaling through theJournal of bacteriology · 2024Article
- ATP-independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next-generation therapeutics.Protein science : a publication of the Protein Society · 2024Review
- Components Subcellular Localization: Cell Surface Exposure.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Components Subcellular Localization: Cell Surface Exposure.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Altering Escherichia coli envelope integrity by mimicking the lipoprotein RcsF.Archives of microbiology · 2023Article
- TamAB is regulated by PhoPQ and functions in outer membrane homeostasis duringJournal of bacteriology · 2023Article
- NlpE Is an OmpA-Associated Outer Membrane Sensor of the Cpx Envelope Stress Response.Journal of bacteriology · 2023Article
29 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
RcsF (regulator of capsule synthesis) is an outer membrane (OM) lipoprotein that functions to sense defects such as changes in LPS. However, LPS is found in the outer leaflet, and RcsF was thought to be tethered to the inner leaflet by its lipidated N terminus, raising the question of how it monitors LPS. We show that RcsF has a transmembrane topology with the lipidated N terminus on the cell surface and the C-terminal signaling domain in the periplasm. Strikingly, the short, unstructured, charged transmembrane domain is threaded through the lumen of β-barrel OM proteins where it is protected from the hydrophobic membrane interior. We present evidence that these unusual complexes, which contain one protein inside another, are formed by the Bam complex that assembles all β-barrel proteins in the OM. The ability of the Bam complex to expose lipoproteins at the cell surface underscores the mechanistic versatility of the β-barrel assembly machine.
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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.