Evidence map›Paper›PMID 29540681›Full record

ArticleNature communications2018

Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli.

Patrice Rassam, Kathleen R Long, Renata Kaminska, David J Williams, Grigorios Papadakos, Christoph G Baumann, Colin Kleanthous

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
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  7. Tunable force transduction through theProceedings of the National Academy of Sciences of the United States of America · 2023
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  14. Phase separation in the outer membrane ofProceedings of the National Academy of Sciences of the United States of America · 2021
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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

7 authors at 6 institutions in 2 countries.

Patrice RassamDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.ORCID http://orcid.org/0000-0002-8630-0957
Kathleen R LongDepartment of Biology, University of York, York, YO10 5DD, UK.
Renata KaminskaDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
David J WilliamsDepartment of Biology, University of York, York, YO10 5DD, UK.ORCID http://orcid.org/0000-0003-4033-0867
Grigorios PapadakosDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.ORCID http://orcid.org/0000-0002-8666-0880
Christoph G BaumannDepartment of Biology, University of York, York, YO10 5DD, UK. christoph.baumann@york.ac.uk.ORCID http://orcid.org/0000-0002-8818-972X
Colin KleanthousDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. colin.kleanthous@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0002-3273-0302
University of Oxford · GBCentre National de la Recherche Scientifique · FRRoslin Institute · GBUniversity of Dundee · GBUniversity of York · GBWellcome Sanger Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gram-negative bacteria depend on energised protein complexes that connect the two membranes of the cell envelope. However, β-barrel outer-membrane proteins (OMPs) and α-helical inner-membrane proteins (IMPs) display quite different organisation. OMPs cluster into islands that restrict their lateral mobility, while IMPs generally diffuse throughout the cell. Here, using live cell imaging of Escherichia coli, we demonstrate that when transient, energy-dependent transmembrane connections are formed, IMPs become subjugated by the inherent organisation of OMPs and that such connections impact IMP function. We show that while establishing a translocon for import, the colicin ColE9 sequesters the IMPs of the proton motive force (PMF)-linked Tol-Pal complex into islands mirroring those of colicin-bound OMPs. Through this imposed organisation, the bacteriocin subverts the outer-membrane stabilising role of Tol-Pal, blocking its recruitment to cell division sites and slowing membrane constriction. The ordering of IMPs by OMPs via an energised inter-membrane bridge represents an emerging functional paradigm in cell envelope biology.

Indexed as

Bacterial Outer Membrane ProteinsCell MembraneEscherichia coliEscherichia coli ProteinsProtein BindingProtein TransportBacterial Outer Membrane ProteinsEscherichia coli Proteins

Identifiers

PMID29540681
PMCPMC5852019
OpenAlexW2794328716

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.