Evidence map›Paper›PMID 19614667›Full record

ArticleCellular microbiology2009

Ubiquitination of the bacterial inositol phosphatase, SopB, regulates its biological activity at the plasma membrane.

Leigh A Knodler, Seth Winfree, Dan Drecktrah, Robin Ireland, Olivia Steele-Mortimer

Open access · bronzeAbstract read
In one paragraph

Article in Cellular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

49 citing papers in PubMed, 73 citations in OpenAlex.

  1. Molecular strategies ofFrontiers in cellular and infection microbiology · 2026
    Review
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  5. Review
  6. Cells · 2022
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  7. Article
  8. Review
  9. Article
  10. Article
  11. Ubiquitination ofmBio · 2019
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Methods to Illuminate the Role ofFrontiers in cellular and infection microbiology · 2017
    Review
  20. Predictable, Tunable Protein Production inFrontiers in cellular and infection microbiology · 2017
    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

5 authors at 1 institution in 1 country.

Leigh A KnodlerLaboratory of Intracellular Parasites, Rocky Mountain Laboratories, NIAID, NIH, Hamilton, MT 59840, USA. lknodler@niaid.nih.gov
Seth Winfree
Dan Drecktrah
Robin Ireland
Olivia Steele-Mortimer
Rocky Mountain Research (United States) · US

Funding

The Salmonella-Containing VacuoleZIAAI000909 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI STEELE-MORTIMER, OLIVIA · 2009 to 2025
$12.9M
Salmonella-Host Cell InteractionsZIAAI001111 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI STEELE-MORTIMER, OLIVIA · 2009 to 2018
$5.6M
Host Responses: Salmonella Enterica Serovar TyphimuriumZ01AI000909 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI STEELE-MORTIMER, OLIVIA · 2002 to 2008
$3.1M
Intramural NIH HHS Z01 AI000909
6 · The paper itself

Abstract

The Salmonella type III effector, SopB, is an inositol polyphosphate phosphatase that modulates host cell phospholipids at the plasma membrane and the nascent Salmonella-containing vacuole (SCV). Translocated SopB persists for many hours after infection and is ubiquitinated but the significance of this covalent modification has not been investigated. Here we identify by mass spectrometry six lysine residues of SopB that are mono-ubiquitinated. Substitution of these six lysine residues with arginine, SopB-K(6)R, almost completely eliminated SopB ubiquitination. We found that ubiquitination does not affect SopB stability or membrane association, or SopB-dependent events in SCV biogenesis. However, two spatially and temporally distinct events are dependent on ubiquitination, downregulation of SopB activity at the plasma membrane and prolonged retention of SopB on the SCV. Activation of the mammalian pro-survival kinase Akt/PKB, a downstream target of SopB, was intensified and prolonged after infection with the SopB-K(6)R mutant. At later times, fewer SCV were decorated with SopB-K(6)R compared with SopB. Instead SopB-K(6)R was present as discrete vesicles spread diffusely throughout the cell. Altogether, our data show that ubiquitination of SopB is not related to its intracellular stability but rather regulates its enzymatic activity at the plasma membrane and intracellular localization.

Indexed as

Amino Acid SubstitutionBacterial ProteinsCell MembraneHeLa CellsHumansLysineMutagenesis, Site-DirectedProtein StabilitySalmonellaUbiquitinationVirulence FactorsBacterial ProteinsLysineSopB protein, SalmonellaVirulence Factors

Identifiers

PMID19614667
PMCPMC2762020
OpenAlexW2018884783

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.