Evidence map›Paper›PMID 20823205›Full record

ArticleInfection and immunity2010

Critical role for the host GTPase-activating protein ARAP2 in InlB-mediated entry of Listeria monocytogenes.

Balramakrishna Gavicherla, Lisa Ritchey, Antonella Gianfelice, Andrey A Kolokoltsov, Robert A Davey, Keith Ireton

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Arf GAPs as Regulators of the Actin Cytoskeleton-An Update.International journal of molecular sciences · 2019
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. 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

6 authors at 3 institutions in 2 countries.

Balramakrishna GavicherlaDepartment of Molecular Biology and Microbiology, College of Medicine, Burnett School of Biomedical Sciences, University of Central Florida, Orlando, Florida, USA.
Lisa Ritchey
Antonella Gianfelice
Andrey A Kolokoltsov
Robert A Davey
Keith Ireton
The University of Texas Medical Branch at Galveston · USUniversity of Central Florida · USUniversity of Otago · NZ

Funding

Receptor Trafficking in Entry of Murine Leukemia VirusesR01AI063513 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI DAVEY, ROBERT A · 2006 to 2011
$1.5M
NIAID NIH HHS 5R01AI063513-02NIAID NIH HHS R01 AI063513
6 · The paper itself

Abstract

The bacterial pathogen Listeria monocytogenes causes food-borne illnesses culminating in gastroenteritis, meningitis, or abortion. Listeria induces its internalization into some mammalian cells through binding of the bacterial surface protein InlB to the host receptor tyrosine kinase Met. Interaction of InlB with the Met receptor elicits host downstream signaling pathways that promote F-actin cytoskeletal changes responsible for pathogen engulfment. Here we show that the mammalian signaling protein ARAP2 plays a critical role in cytoskeletal remodeling and internalization of Listeria. Depletion of ARAP2 through RNA interference (RNAi) caused a marked inhibition of InlB-mediated F-actin rearrangements and bacterial entry. ARAP2 contains multiple functional domains, including a GTPase-activating protein (GAP) domain that antagonizes the GTPase Arf6 and a domain capable of binding the GTPase RhoA. Genetic data indicated roles for both the Arf GAP and RhoA binding domains in Listeria entry. Experiments involving Arf6 RNAi or a constitutively activated allele of Arf6 demonstrated that one of the ways in which ARAP2 promotes bacterial uptake is by restraining the activity of Arf6. Conversely, Rho activity was dispensable for Listeria internalization, suggesting that the RhoA binding domain in ARAP2 acts by engaging a host ligand other than Rho proteins. Collectively, our findings indicate that ARAP2 promotes InlB-mediated entry of Listeria, in part, by antagonizing the host GTPase Arf6.

Indexed as

ADP-Ribosylation Factor 6ADP-Ribosylation FactorsBacterial ProteinsCarrier ProteinsEpithelial CellsGTPase-Activating ProteinsHeLa CellsHost-Pathogen InteractionsHumansListeria monocytogenesMembrane ProteinsPhosphatidylinositol 3-KinasesADP-Ribosylation Factor 6ADP-Ribosylation FactorsARAP2 protein, humanARF6 protein, humanBacterial ProteinsCarrier ProteinsGTPase-Activating ProteinsinlB protein, Listeria monocytogenesMembrane ProteinsPhosphatidylinositol 3-Kinases

Identifiers

PMID20823205
PMCPMC2976330
OpenAlexW2123179262

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.