Evidence map›Paper›PMID 16381816›Full record

ArticleMolecular biology of the cell2006

The association of Shiga-like toxin with detergent-resistant membranes is modulated by glucosylceramide and is an essential requirement in the endoplasmic reticulum for a cytotoxic effect.

Daniel C Smith, Daniel J Sillence, Thomas Falguières, Rosemary M Jarvis, Ludger Johannes, J Michael Lord, Frances M Platt, Lynne M Roberts

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. EnterohemorrhagicInternational journal of molecular sciences · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Synthesis of GbAngewandte Chemie (International ed. in English) · 2019
    Article
  16. Protein Toxins That Utilize Gangliosides as Host Receptors.Progress in molecular biology and translational science · 2018
    Review
  17. Article
  18. Review
  19. Review
  20. Blood Groups in Infection and Host Susceptibility.Clinical microbiology reviews · 2015
    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

8 authors at 3 institutions in 2 countries.

Daniel C SmithDepartment of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK.
Daniel J Sillence
Thomas Falguières
Rosemary M Jarvis
Ludger Johannes
J Michael Lord
Frances M Platt
Lynne M Roberts
University of Warwick · GBCentre National de la Recherche Scientifique · FRUniversity of Oxford · GB

Funding

Wellcome Trust 063058/Z/00/Z
6 · The paper itself

Abstract

Receptor-mediated internalization to the endoplasmic reticulum (ER) and subsequent retro-translocation to the cytosol are essential sequential processes required for the productive intoxication of susceptible mammalian cells by Shiga-like toxin-1 (SLTx). Recently, it has been proposed that the observed association of certain ER-directed toxins and viruses with detergent-resistant membranes (DRM) may provide a general mechanism for their retrograde transport to endoplasmic reticulum (ER). Here, we show that DRM recruitment of SLTx bound to its globotriosylceramide (Gb(3)) receptor is mediated by the availability of other glycosphingolipids. Reduction in glucosylceramide (GlcCer) levels led to complete protection against SLTx and a reduced cell surface association of bound toxin with DRM. This reduction still allowed efficient binding and transport of the toxin to the ER. However, toxin sequestration within DRM of the ER was abolished under reduced GlcCer conditions, suggesting that an association of toxin with lipid microdomains or rafts in the ER (where these are defined by detergent insolubility) is essential for a later step leading to or involving retro-translocation of SLTx across the ER membrane. In support of this, we show that a number of ER residents, proteins intimately involved in the process of ER dislocation of misfolded proteins, are present in DRM.

Indexed as

1-DeoxynojirimycinAnimalsCell DeathCell Line, TumorCell MembraneChlorocebus aethiopsDetergentsEndoplasmic ReticulumGlucosylceramidesGlycosphingolipidsHeLa CellsHumansIntracellular MembranesProteasome InhibitorsProtein TransportShiga Toxin 11-DeoxynojirimycinDetergentsglobotriaosylceramideGlucosylceramidesGlycosphingolipidsmigalastatProteasome InhibitorsShiga Toxin 1Trihexosylceramides

Identifiers

PMID16381816
PMCPMC1382325
OpenAlexW2096623610

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.