Evidence map›Paper›PMID 19887681›Full record

ArticleScience signaling2009

Activation of a bacterial virulence protein by the GTPase RhoA.

Matthias Christen, Lisette H Coye, Jill S Hontz, Doris L LaRock, Richard A Pfuetzner, Megha, Samuel I Miller

Open access · greenAbstract read
In one paragraph

Article in Science signaling, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.5field-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

34 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Review
  3. Molecular biology of the cell · 2025
    Article
  4. Speaking the host language: howMicrobiology (Reading, England) · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. VscF in T3SS1 Helps to Translocate VPA0226 inFrontiers in cellular and infection microbiology · 2021
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. What the SIF Is Happening-The Role of IntracellularFrontiers in cellular and infection microbiology · 2017
    Review
  16. How Bacteria Subvert Animal Cell Structure and Function.Annual review of cell and developmental biology · 2016
    Review
  17. Bacterial Sphingomyelinases and Phospholipases as Virulence Factors.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  18. Article
  19. Modification of Bacterial Effector Proteins Inside Eukaryotic Host Cells.Frontiers in cellular and infection microbiology · 2016
    Review
  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

7 authors at 1 institution in 1 country.

Matthias ChristenDepartment of Immunology, University of Washington, Seattle, WA 98195, USA.
Lisette H Coye
Jill S Hontz
Doris L LaRock
Richard A Pfuetzner
Megha
Samuel I Miller
University of Washington · US

Funding

Variation in Human Innate ImmunityU54AI057141 · NIAID · UNIVERSITY OF WASHINGTON · PI COOKSON, BRAD T · 2003 to 2013
$102.3M
TRAINING IN MOLECULAR AND CELLULAR BIOLOGYT32GM007270 · NIGMS · UNIVERSITY OF WASHINGTON · PI RAIBLE, DAVID W · 1985 to 2020
$21.0M
SALMONELLA PATHOGENICITY ISLAND 2 EFFECTOR PROTEINSR01AI048683 · NIAID · UNIVERSITY OF WASHINGTON · PI MILLER, SAMUEL I · 2001 to 2015
$5.1M
NIAID NIH HHS R01 AI048683NIAID NIH HHS U54 AI057141NIGMS NIH HHS T32 GM007270
6 · The paper itself

Abstract

The Rho family of guanosine triphosphatases (GTPases) are essential eukaryotic signaling molecules that regulate cellular physiology. Virulence factors from various pathogens alter the signaling of GTPases by acting as GTPase activating factors, guanine nucleotide exchange factors, or direct covalent modifiers; however, bacterial virulence factors that sense rather than alter the signaling states of Rho GTPases have not been previously described. Here, we report that the translocated Salmonellae virulence factor SseJ binds to the guanosine triphosphate-bound form of RhoA. This interaction stimulates the lipase activity of SseJ, which results in the esterification of cholesterol in the host cell membrane. Our results suggest that the activation of molecules downstream of GTPases is not exclusive to eukaryotic proteins, and that a bacterial protein has evolved to recognize the activation state of RhoA, which regulates its enzymatic activity as part of the host-pathogen interaction.

Indexed as

Host-Pathogen InteractionsBacterial ProteinsCholesterolEsterificationHumansLipaseProtein BindingrhoA GTP-Binding ProteinSalmonellaSignal TransductionVirulence FactorsBacterial ProteinsCholesterolLipaserhoA GTP-Binding ProteinVirulence Factors

Identifiers

PMID19887681
PMCPMC5096451
OpenAlexW2110492931

What OpenQuestion holds

Textmetadata
LicenceTDM
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.