Evidence map›Paper›PMID 28039206›Full record

ArticleEMBO reports2017

Endoplasmic reticulum chaperone Gp96 controls actomyosin dynamics and protects against pore-forming toxins.

Francisco Sarmento Mesquita, Cláudia Brito, Maria J Mazon Moya, Jorge Campos Pinheiro, Serge Mostowy, Didier Cabanes, Sandra Sousa

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

22 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Mechanisms protecting host cells against bacterial pore-forming toxins.Cellular and molecular life sciences : CMLS · 2019
    Review
  18. Review
  19. Article
  20. 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

7 authors at 2 institutions in 2 countries.

Francisco Sarmento MesquitaI3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.
Cláudia BritoI3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.
Maria J Mazon MoyaSection of Microbiology, MRC Centre for Molecular Bacteriology and Infection (CMBI), Imperial College London, London, UK.
Jorge Campos PinheiroI3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.
Serge MostowySection of Microbiology, MRC Centre for Molecular Bacteriology and Infection (CMBI), Imperial College London, London, UK.ORCID 0000-0002-7286-6503
Didier CabanesI3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal didier@ibmc.up.pt srsousa@ibmc.up.pt.
Sandra SousaI3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal didier@ibmc.up.pt srsousa@ibmc.up.pt.ORCID 0000-0001-8578-0461
Universidade do Porto · PTImperial College London · GB

Funding

Wellcome TrustWellcome Trust WT097411MA
6 · The paper itself

Abstract

During infection, plasma membrane (PM) blebs protect host cells against bacterial pore-forming toxins (PFTs), but were also proposed to promote pathogen dissemination. However, the details and impact of blebbing regulation during infection remained unclear. Here, we identify the endoplasmic reticulum chaperone Gp96 as a novel regulator of PFT-induced blebbing. Gp96 interacts with non-muscle myosin heavy chain IIA (NMHCIIA) and controls its activity and remodelling, which is required for appropriate coordination of bleb formation and retraction. This mechanism involves NMHCIIA-Gp96 interaction and their recruitment to PM blebs and strongly resembles retraction of uropod-like structures from polarized migrating cells, a process that also promotes NMHCIIA-Gp96 association. Consistently, Gp96 and NMHCIIA not only protect the PM integrity from listeriolysin O (LLO) during infection by Listeria monocytogenes but also affect cytoskeletal organization and cell migration. Finally, we validate the association between Gp96 and NMHCIIA in vivo and show that Gp96 is required to protect hosts from LLO-dependent killing.

Indexed as

ActomyosinAnimalsBacterial ProteinsBacterial ToxinsCell SurvivalHumansListeria monocytogenesMembrane GlycoproteinsMiceMolecular ChaperonesPore Forming Cytotoxic ProteinsZebrafishActomyosinBacterial ProteinsBacterial ToxinsendoplasminMembrane GlycoproteinsMolecular ChaperonesPore Forming Cytotoxic Proteinsactomyosinendoplasmic reticulum chaperoneListeria monocytogenesplasma membrane blebbingpore‐forming toxins

Identifiers

PMID28039206
PMCPMC5286360
OpenAlexW2560903744

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.