Evidence map›Paper›PMID 29483609›Full record

ArticleScientific reports2018

Heterogeneous localisation of membrane proteins in Staphylococcus aureus.

Felix Weihs, Katarzyna Wacnik, Robert D Turner, Siân Culley, Ricardo Henriques, Simon J Foster

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. The versatile role of YidC in membrane protein biosynthesis and quality control.Biochimica et biophysica acta. Molecular cell research · 2025
    Review
  2. Bacterial lipid biophysics and membrane organization.Current opinion in microbiology · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Biology · 2021
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. SRRF: Universal live-cell super-resolution microscopy.The international journal of biochemistry & cell biology · 2018
    Article
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

6 authors at 2 institutions in 1 country.

Felix WeihsThe Krebs Institute. Department of Molecular Biology and Microbiology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.
Katarzyna WacnikThe Krebs Institute. Department of Molecular Biology and Microbiology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.
Robert D TurnerThe Krebs Institute. Department of Molecular Biology and Microbiology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.
Siân CulleyQuantitative Imaging and Nanobiophysics Group, MRC Laboratory for Molecular Cell Biology and Department of Cell and Developmental Biology, University College London, Gower Street, London, WC1E 6BT, UK.ORCID 0000-0003-2112-0143
Ricardo HenriquesQuantitative Imaging and Nanobiophysics Group, MRC Laboratory for Molecular Cell Biology and Department of Cell and Developmental Biology, University College London, Gower Street, London, WC1E 6BT, UK.ORCID 0000-0002-2043-5234
Simon J FosterThe Krebs Institute. Department of Molecular Biology and Microbiology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK. s.foster@sheffield.ac.uk.
University of Sheffield · GBThe Francis Crick Institute · GB

Funding

Biotechnology and Biological Sciences Research Council BBL006162/1Biotechnology and Biological Sciences Research Council BB/M022374/1Medical Research Council G1100127Medical Research Council MR/K015753/1Medical Research Council MR/K015826/1Medical Research Council MR/N002679/1Wellcome Trust 203276/Z/16/Z
6 · The paper itself

Abstract

The bacterial cytoplasmic membrane is the interface between the cell and its environment, with multiple membrane proteins serving its many functions. However, how these proteins are organised to permit optimal physiological processes is largely unknown. Based on our initial findings that 2 phospholipid biosynthetic enzymes (PlsY and CdsA) localise heterogeneously in the membrane of the bacterium Staphylococcus aureus, we have analysed the localisation of other key membrane proteins. A range of protein fusions were constructed and used in conjunction with quantitative image analysis. Enzymes involved in phospholipid biosynthesis as well as the lipid raft marker FloT exhibited a heterogeneous localisation pattern. However, the secretion associated SecY protein, was more homogeneously distributed in the membrane. A FRET-based system also identified novel colocalisation between phospholipid biosynthesis enzymes and the respiratory protein CydB revealing a likely larger network of partners. PlsY localisation was found to be dose dependent but not to be affected by membrane lipid composition. Disruption of the activity of the essential cell division organiser FtsZ, using the inhibitor PC190723 led to loss of PlsY localisation, revealing a link to cell division and a possible role for FtsZ in functions not strictly associated with septum formation.

Indexed as

Bacterial ProteinsMembrane ProteinsNucleotidyltransferasesPhospholipidsSEC Translocation ChannelsStaphylococcus aureusBacterial ProteinsMembrane ProteinsNucleotidyltransferasesPhospholipidsSEC Translocation Channels

Identifiers

PMID29483609
PMCPMC5826919
OpenAlexW2806776060

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.