Evidence map›Paper›PMID 21779406›Full record

ArticlePloS one2011

Activation of Akt by the bacterial inositol phosphatase, SopB, is wortmannin insensitive.

Kendal G Cooper, Seth Winfree, Preeti Malik-Kale, Carrie Jolly, Robin Ireland, Leigh A Knodler, Olivia Steele-Mortimer

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Infection biology ofEcoSal Plus · 2024
    Review
  7. Article
  8. Article
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  10. Modification of phosphoinositides by theFrontiers in cellular and infection microbiology · 2022
    Review
  11. Journal of immunology research · 2022
    Article
  12. Review
  13. Review
  14. Frontiers in cellular and infection microbiology · 2019
    Article
  15. Review
  16. Article
  17. Article
  18. MYO6 is targeted byProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  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

7 authors at 1 institution in 1 country.

Kendal G CooperLaboratory of Intracellular Parasites, National Institutes of Allergy and Infectious Disease, National Institutes of Health, Rocky Mountain Laboratories, Hamilton, Montana, United States of America.
Seth Winfree
Preeti Malik-Kale
Carrie Jolly
Robin Ireland
Leigh A Knodler
Olivia Steele-Mortimer
National Institutes of Health · US

Funding

Salmonella-Host Cell InteractionsZIAAI001111 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI STEELE-MORTIMER, OLIVIA · 2009 to 2018
$5.6M
Intramural NIH HHS
6 · The paper itself

Abstract

Salmonella enterica uses effector proteins translocated by a Type III Secretion System to invade epithelial cells. One of the invasion-associated effectors, SopB, is an inositol phosphatase that mediates sustained activation of the pro-survival kinase Akt in infected cells. Canonical activation of Akt involves membrane translocation and phosphorylation and is dependent on phosphatidyl inositide 3 kinase (PI3K). Here we have investigated these two distinct processes in Salmonella infected HeLa cells. Firstly, we found that SopB-dependent membrane translocation and phosphorylation of Akt are insensitive to the PI3K inhibitor wortmannin. Similarly, depletion of the PI3K regulatory subunits p85α and p85ß by RNAi had no inhibitory effect on SopB-dependent Akt phosphorylation. Nevertheless, SopB-dependent phosphorylation does depend on the Akt kinases, PDK1 and rictor-mTOR. Membrane translocation assays revealed a dependence on SopB for Akt recruitment to Salmonella ruffles and suggest that this is mediated by phosphoinositide (3,4) P(2) rather than phosphoinositide (3,4,5) P(3). Altogether these data demonstrate that Salmonella activates Akt via a wortmannin insensitive mechanism that is likely a class I PI3K-independent process that incorporates some essential elements of the canonical pathway.

Indexed as

AndrostadienesBacterial ProteinsPhosphatidylinositol 3-KinasePhosphoinositide-3 Kinase InhibitorsProtein Kinase InhibitorsProto-Oncogene Proteins c-aktSalmonella entericaWortmanninAndrostadienesBacterial ProteinsPhosphatidylinositol 3-KinasePhosphoinositide-3 Kinase InhibitorsProtein Kinase InhibitorsProto-Oncogene Proteins c-aktSopB protein, SalmonellaWortmannin

Identifiers

PMID21779406
PMCPMC3136525
OpenAlexW2032928756

What OpenQuestion holds

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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.