Evidence map›Paper›PMID 29681471›Full record

ArticleStructure (London, England : 1993)2018

Correlative Microscopy of Vitreous Sections Provides Insights into BAR-Domain Organization In Situ.

Tanmay A M Bharat, Patrick C Hoffmann, Wanda Kukulski

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. High-resolution structure determination using high-throughput electron cryo-tomography.Acta crystallographica. Section D, Structural biology · 2022
    Review
  9. Review
  10. iScience · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  15. Article
  16. Review
  17. Article
  18. Mechanisms of negative membrane curvature sensing and generation by ESCRT III subunit Snf7.Protein science : a publication of the Protein Society · 2020
    Article
  19. Article
  20. Investigating eukaryotic cells with cryo-ET.Molecular biology of the cell · 2020
    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

3 authors.

Tanmay A M BharatSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK; Central Oxford Structural and Molecular Imaging Centre, South Parks Road, Oxford OX1 3RE, UK; Structural Studies Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Patrick C HoffmannCell Biology Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Wanda KukulskiCell Biology Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: kukulski@mrc-lmb.cam.ac.uk.

Funding

Medical Research Council MC_UP_1201/8Wellcome Trust
6 · The paper itself

Abstract

Electron microscopy imaging of macromolecular complexes in their native cellular context is limited by the inherent difficulty to acquire high-resolution tomographic data from thick cells and to specifically identify elusive structures within crowded cellular environments. Here, we combined cryo-fluorescence microscopy with electron cryo-tomography of vitreous sections into a coherent correlative microscopy workflow, ideal for detection and structural analysis of elusive protein assemblies in situ. We used this workflow to address an open question on BAR-domain coating of yeast plasma membrane compartments known as eisosomes. BAR domains can sense or induce membrane curvature, and form scaffold-like membrane coats in vitro. Our results demonstrate that in cells, the BAR protein Pil1 localizes to eisosomes of varying membrane curvature. Sub-tomogram analysis revealed a dense protein coat on curved eisosomes, which was not present on shallow eisosomes, indicating that while BAR domains can assemble at shallow membranes in vivo, scaffold formation is tightly coupled to curvature generation.

Indexed as

Cell MembraneCryoelectron MicroscopyElectron Microscope TomographyPhosphoproteinsProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPhosphoproteinsPIL1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsBAR domainsCEMOVIScorrelative microscopycryo-CLEMcryo-EMeisosomeselectron cryo-tomographyvitreous sections

Identifiers

PMID29681471
PMCPMC5992340

What OpenQuestion holds

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Registered trials

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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.