Evidence map›Paper›PMID 20808760›Full record

ArticlePLoS biology2010

Tyrosine-phosphorylated caveolin-1 blocks bacterial uptake by inducing Vav2-RhoA-mediated cytoskeletal rearrangements.

Jan Peter Boettcher, Marieluise Kirchner, Yuri Churin, Alexis Kaushansky, Malvika Pompaiah, Hans Thorn, Volker Brinkmann, Gavin Macbeath, Thomas F Meyer

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Exosomal transmission of viruses, a two-edged biological sword.Cell communication and signaling : CCS · 2023
    Review
  4. Article
  5. Review
  6. Unidirectional Regulation of Vimentin Intermediate Filaments to Caveolin-1.International journal of molecular sciences · 2020
    Article
  7. Caveolae as Potential Hijackable Gates in Cell Communication.Frontiers in cell and developmental biology · 2020
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Caveolae as plasma membrane sensors, protectors and organizers.Nature reviews. Molecular cell biology · 2013
    Review
  19. Article
  20. 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

9 authors at 3 institutions in 2 countries.

Jan Peter BoettcherDepartment of Molecular Biology, Max Planck Institute for Infection Biology, Berlin, Germany.
Marieluise Kirchner
Yuri Churin
Alexis Kaushansky
Malvika Pompaiah
Hans Thorn
Volker Brinkmann
Gavin Macbeath
Thomas F Meyer
Max Planck Institute for Infection Biology · DEMax Planck Society · DEHarvard University · US

Funding

Quantitative Interaction Networks for Tyrosine-Phosphorylated ProteinsR33CA128726 · NCI · HARVARD UNIVERSITY · PI MACBEATH, GAVIN · 2007 to 2009
$1.2M
NCI NIH HHS R33 CA128726
6 · The paper itself

Abstract

Certain bacterial adhesins appear to promote a pathogen's extracellular lifestyle rather than its entry into host cells. However, little is known about the stimuli elicited upon such pathogen host-cell interactions. Here, we report that type IV pili (Tfp)-producing Neisseria gonorrhoeae (P(+)GC) induces an immediate recruitment of caveolin-1 (Cav1) in the host cell, which subsequently prevents bacterial internalization by triggering cytoskeletal rearrangements via downstream phosphotyrosine signaling. A broad and unbiased analysis of potential interaction partners for tyrosine-phosphorylated Cav1 revealed a direct interaction with the Rho-family guanine nucleotide exchange factor Vav2. Both Vav2 and its substrate, the small GTPase RhoA, were found to play a direct role in the Cav1-mediated prevention of bacterial uptake. Our findings, which have been extended to enteropathogenic Escherichia coli, highlight how Tfp-producing bacteria avoid host cell uptake. Further, our data establish a mechanistic link between Cav1 phosphorylation and pathogen-induced cytoskeleton reorganization and advance our understanding of caveolin function.

Indexed as

Gene Expression RegulationSignal TransductionCaveolin 1Cell Line, TumorCytoskeletonEpithelial CellsFimbriae, BacterialHost-Pathogen InteractionsHumansNeisseria gonorrhoeaePhosphorylationProto-Oncogene Proteins c-vavrhoA GTP-Binding ProteinTyrosineCaveolin 1Proto-Oncogene Proteins c-vavrhoA GTP-Binding ProteinRHOA protein, humanTyrosineVAV2 protein, human

Identifiers

PMID20808760
PMCPMC2927421
OpenAlexW2032235753

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.