Evidence map›Paper›PMID 38961085›Full record

ArticleNature communications2024

Flotillin-mediated stabilization of unfolded proteins in bacterial membrane microdomains.

Marta Ukleja, Lara Kricks, Gabriel Torrens, Ilaria Peschiera, Ines Rodrigues-Lopes, Marcin Krupka, Julia García-Fernández, Roberto Melero, Rosa Del Campo, Ana Eulalio and 5 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Mimicking Cellular Membranes With Micropatterned Lipid Bilayers.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. ThebioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Transcriptional and cellular reprogramming inCurrent research in microbial sciences · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Toxic Effects of Butanol in the Plane of the Cell Membrane.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
  14. 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

15 authors.

Marta UklejaDepartment of Microbiology, National Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), Madrid, 28049, Spain.
Lara KricksDepartment of Microbiology, National Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), Madrid, 28049, Spain.
Gabriel TorrensDepartment of Molecular Biology, Umeå University, Umeå, SE-901 87, Sweden.ORCID 0000-0002-0450-1430
Ilaria PeschieraDepartment of Microbiology, National Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), Madrid, 28049, Spain.
Ines Rodrigues-LopesCenter for Neuroscience and Cell Biology (CNC), University of Coimbra, 3004-504, Coimbra, Portugal.ORCID 0000-0003-1527-543X
Marcin KrupkaDepartment of Microbiology, National Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), Madrid, 28049, Spain.
Julia García-FernándezDepartment of Microbiology, National Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), Madrid, 28049, Spain.ORCID 0000-0002-6937-6394
Roberto MeleroDepartment of Structural Biology, National Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), Madrid, 28049, Spain.
Rosa Del CampoInstituto Ramón y Cajal de Investigación Sanitaria (IRYCIS), Ramón y Cajal Hospital, 28034, Madrid, Spain.ORCID 0000-0003-1147-7923
Ana EulalioCenter for Neuroscience and Cell Biology (CNC), University of Coimbra, 3004-504, Coimbra, Portugal.ORCID 0000-0002-7355-0674
André MateusThe Laboratory for Molecular Infection Medicine Sweden (MIMS). Umeå Center for Microbial Research (UCMR). Science for Life Laboratory (SciLifeLab), Umeå, SE-901 87, Sweden.ORCID 0000-0001-6870-0677
María López-BravoDepartment of Microbiology, National Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), Madrid, 28049, Spain.
Ana I RicoDepartment of Microbiology, National Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), Madrid, 28049, Spain.ORCID 0000-0001-6021-3970
Felipe CavaDepartment of Molecular Biology, Umeå University, Umeå, SE-901 87, Sweden.ORCID 0000-0001-5995-718X
Daniel LopezDepartment of Microbiology, National Centre for Biotechnology, Spanish National Research Council (CNB-CSIC), Madrid, 28049, Spain. dlopez@cnb.csic.es.ORCID 0000-0002-8627-3813

Funding

"la Caixa" Foundation (Caixa Foundation) LCF/PR/HR23/52430026Vetenskapsrådet (Swedish Research Council) 521-2014-6652
6 · The paper itself

Abstract

The function of many bacterial processes depends on the formation of functional membrane microdomains (FMMs), which resemble the lipid rafts of eukaryotic cells. However, the mechanism and the biological function of these membrane microdomains remain unclear. Here, we show that FMMs in the pathogen methicillin-resistant Staphylococcus aureus (MRSA) are dedicated to confining and stabilizing proteins unfolded due to cellular stress. The FMM scaffold protein flotillin forms a clamp-shaped oligomer that holds unfolded proteins, stabilizing them and favoring their correct folding. This process does not impose a direct energy cost on the cell and is crucial to survival of ATP-depleted bacteria, and thus to pathogenesis. Consequently, FMM disassembling causes the accumulation of unfolded proteins, which compromise MRSA viability during infection and cause penicillin re-sensitization due to PBP2a unfolding. Thus, our results indicate that FMMs mediate ATP-independent stabilization of unfolded proteins, which is essential for bacterial viability during infection.

Indexed as

Bacterial ProteinsMembrane MicrodomainsMembrane ProteinsMethicillin-Resistant Staphylococcus aureusAdenosine TriphosphateAnimalsHumansMicePenicillin-Binding ProteinsProtein StabilityProtein UnfoldingStaphylococcal InfectionsAdenosine TriphosphateBacterial ProteinsflotillinsMembrane ProteinsPenicillin-Binding Proteins

Identifiers

PMID38961085
PMCPMC11222466

What OpenQuestion holds

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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.