Evidence map›Paper›PMID 21504731›Full record

ArticleBiophysical journal2011

A role for septins in the interaction between the Listeria monocytogenes INVASION PROTEIN InlB and the Met receptor.

Serge Mostowy, Sébastien Janel, Claire Forestier, Charles Roduit, Sandor Kasas, Javier Pizarro-Cerdá, Pascale Cossart, Frank Lafont

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
5.1field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 98 citations in OpenAlex.

  1. Pooled it
  2. Mechanically-induced Septin Networks Protect Nuclear Integrity.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. The Roles of Septins in Regulating Fission Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Septins, a cytoskeletal protein family, with emerging role in striated muscle.Journal of muscle research and cell motility · 2021
    Review
  13. Article
  14. Septins in Infections: Focus on Viruses.Pathogens (Basel, Switzerland) · 2021
    Review
  15. How Microbes Use Force To Control Adhesion.Journal of bacteriology · 2020
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Microbiology spectrum · 2018
    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 4 institutions in 2 countries.

Serge MostowyUnité des Interactions Bactéries-Cellules, Institut Pasteur, Paris, France.
Sébastien Janel
Claire Forestier
Charles Roduit
Sandor Kasas
Javier Pizarro-Cerdá
Pascale Cossart
Frank Lafont
Inserm · FRÉcole Polytechnique Fédérale de Lausanne · CHInstitut Pasteur · FRCenter for Infection and Immunity of Lille · FR

Funding

CIHREuropean Research Council 233348Howard Hughes Medical Institute
6 · The paper itself

Abstract

Septins are conserved GTPases that form filaments and are required for cell division. During interphase, septin filaments associate with cellular membrane and cytoskeleton networks, yet the functional significance of these associations have, to our knowledge, remained unknown. We recently discovered that different septins, SEPT2 and SEPT11, regulate the InlB-mediated entry of Listeria monocytogenes into host cells. Here we address the role of SEPT2 and SEPT11 in the InlB-Met interactions underlying Listeria invasion to explore how septins modulate surface receptor function. We observed that differences in InlB-mediated Listeria entry correlated with differences in Met surface expression caused by septin depletion. Using atomic force microscopy on living cells, we show that septin depletion significantly reduced the unbinding force of InlB-Met interaction and the viscosity of membrane tethers at locations where the InlB-Met interaction occurs. Strikingly, the same order of difference was observed for cells in which the actin cytoskeleton was disrupted. Consistent with a proposed role of septins in association with the actin cytoskeleton, we show that cell elasticity is decreased upon septin or actin inactivation. Septins are therefore likely to participate in anchorage of the Met receptor to the actin cytoskeleton, and represent a critical determinant in surface receptor function.

Indexed as

Listeria monocytogenesAnimalsBacterial ProteinsBiomechanical PhenomenaCell MembraneCell ShapeCell SurvivalElasticityHeLa CellsHumansMembrane ProteinsProtein BindingProto-Oncogene Proteins c-metReceptors, Growth FactorSeptinsBacterial ProteinsinlB protein, Listeria monocytogenesMembrane ProteinsMET protein, humanProto-Oncogene Proteins c-metReceptors, Growth FactorSEPTIN11 protein, humanSEPTIN2 protein, humanSeptins

Identifiers

PMID21504731
PMCPMC3077699
OpenAlexW2063622991

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.