Evidence map›Paper›PMID 36892778›Full record

ReviewJournal of microbiology (Seoul, Korea)2023

Envelope-Stress Sensing Mechanism of Rcs and Cpx Signaling Pathways in Gram-Negative Bacteria.

Seung-Hyun Cho, Kilian Dekoninck, Jean-Francois Collet

Open access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Journal of microbiology (Seoul, Korea), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
11.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. The mecillinam resistome inAntimicrobial agents and chemotherapy · 2026
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  11. Anti-infective compounds forSustainable microbiology · 2026
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. The Environment-Dependent Regulatory Landscape of thebioRxiv : the preprint server for biology · 2025
    Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 2 countries.

Seung-Hyun ChoWELBIO-Walloon Excellence in Life Sciences and Biotechnology, 1200, Brussels, Belgium. seung.cho@uclouvain.be.
Kilian DekoninckWELBIO-Walloon Excellence in Life Sciences and Biotechnology, 1200, Brussels, Belgium.
Jean-Francois ColletWELBIO-Walloon Excellence in Life Sciences and Biotechnology, 1200, Brussels, Belgium.
de Duve Institute · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The global public health burden of bacterial antimicrobial resistance (AMR) is intensified by Gram-negative bacteria, which have an additional membrane, the outer membrane (OM), outside of the peptidoglycan (PG) cell wall. Bacterial two-component systems (TCSs) aid in maintaining envelope integrity through a phosphorylation cascade by controlling gene expression through sensor kinases and response regulators. In Escherichia coli, the major TCSs defending cells from envelope stress and adaptation are Rcs and Cpx, which are aided by OM lipoproteins RcsF and NlpE as sensors, respectively. In this review, we focus on these two OM sensors. β-Barrel assembly machinery (BAM) inserts transmembrane OM proteins (OMPs) into the OM. BAM co-assembles RcsF, the Rcs sensor, with OMPs, forming the RcsF-OMP complex. Researchers have presented two models for stress sensing in the Rcs pathway. The first model suggests that LPS perturbation stress disassembles the RcsF-OMP complex, freeing RcsF to activate Rcs. The second model proposes that BAM cannot assemble RcsF into OMPs when the OM or PG is under specific stresses, and thus, the unassembled RcsF activates Rcs. These two models may not be mutually exclusive. Here, we evaluate these two models critically in order to elucidate the stress sensing mechanism. NlpE, the Cpx sensor, has an N-terminal (NTD) and a C-terminal domain (CTD). A defect in lipoprotein trafficking results in NlpE retention in the inner membrane, provoking the Cpx response. Signaling requires the NlpE NTD, but not the NlpE CTD; however, OM-anchored NlpE senses adherence to a hydrophobic surface, with the NlpE CTD playing a key role in this function.

Indexed as

Escherichia coli ProteinsBacterial Outer Membrane ProteinsCell MembraneEscherichia coliLipoproteinsSignal TransductionBacterial Outer Membrane ProteinsEscherichia coli ProteinsLipoproteinsNlpE protein, E colircsF protein, E coliBAMBamACpxEnvelope stress responseNlpERcsRcsFTwo-component system (TCS)

Identifiers

PMID36892778
OpenAlexW4323653456

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.