Evidence map›Paper›PMID 10839806›Full record

ArticleThe Journal of experimental medicine2000

Rho family GTPase Cdc42 is essential for the actin-based motility of Shigella in mammalian cells.

T Suzuki, H Mimuro, H Miki, T Takenawa, T Sasaki, H Nakanishi, Y Takai, C Sasakawa

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of experimental medicine, 2000. 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
3.0field-weighted citation impact, top 10% 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, 52 citations in OpenAlex.

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  15. A new paradigm of bacteria-gut interplay brought through the study of Shigella.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2010
    Review
  16. Review
  17. Review
  18. Actin-dependent movement of bacterial pathogens.Nature reviews. Microbiology · 2006
    Review
  19. Article
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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 1 country.

T SuzukiDepartment of Bacteriology, Institute of Medical Science, University of Tokyo, Japan.
H Mimuro
H Miki
T Takenawa
T Sasaki
H Nakanishi
Y Takai
C Sasakawa
Tokyo University of Science · JPJCR Pharmaceuticals (Japan) · JPOsaka University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Shigella, the causative agent of bacillary dysentery, is capable of directing its movement within host cells by exploiting actin dynamics. The VirG protein expressed at one pole of the bacterium can recruit neural Wiskott-Aldrich syndrome protein (N-WASP), a downstream effector of Cdc42. Here, we show that Cdc42 is required for the actin-based motility of Shigella. Microinjection of a dominant active mutant Cdc42, but not Rac1 or RhoA, into Swiss 3T3 cells accelerated Shigella motility. In add-back experiments in Xenopus egg extracts, addition of a guanine nucleotide dissociation inhibitor for the Rho family, RhoGDI, greatly diminished the bacterial motility or actin assembly, which was restored by adding activated Cdc42. In N-WASP-depleted extracts, the bacterial movement almost arrested was restored by adding exogenous N-WASP but not H208D, an N-WASP mutant defective in binding to Cdc42. In pyrene actin assay, Cdc42 enhanced VirG-stimulating actin polymerization by N-WASP-actin-related protein (Arp)2/3 complex. Actually, Cdc42 stimulated actin cloud formation on the surface of bacteria expressing VirG in a solution containing N-WASP, Arp2/3 complex, and G-actin. Immunohistological study of Shigella-infected cells expressing green fluorescent protein-tagged Cdc42 revealed that Cdc42 accumulated by being colocalized with actin cloud at one pole of intracellular bacterium. Furthermore, overexpression of H208D mutant in cells interfered with the actin assembly of infected Shigella and diminished the intra- and intercellular spreading. These results suggest that Cdc42 activity is involved in initiating actin nucleation mediated by VirG-N-WASP-Arp2/3 complex formed on intracellular Shigella.

Indexed as

3T3 CellsActinsAnimalsBacterial Proteinscdc42 GTP-Binding ProteinCOS CellsDNA-Binding ProteinsDogsGuanine Nucleotide Dissociation InhibitorsHumansMammalsMiceMicroinjectionsNerve Tissue ProteinsOvumRabbitsActinsARHGDIA protein, humanBacterial Proteinscdc42 GTP-Binding ProteinDNA-Binding ProteinsGuanine Nucleotide Dissociation InhibitorsNerve Tissue Proteinsrho Guanine Nucleotide Dissociation Inhibitor alpharho-Specific Guanine Nucleotide Dissociation InhibitorsTranscription FactorsvirG protein, Shigella flexneriWASL protein, humanWasl protein, mouseWasl protein, ratWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID10839806
PMCPMC2213524
OpenAlexW2115969925

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.