Evidence map›Paper›PMID 25404699›Full record

ArticleJournal of bacteriology2015

Ubiquitin activates patatin-like phospholipases from multiple bacterial species.

David M Anderson, Hiromi Sato, Aaron T Dirck, Jimmy B Feix, Dara W Frank

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

31 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Functional Analysis of Hypothetical Proteins ofBioinformatics and biology insights · 2022
    Article
  8. Perspectives on theToxins · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Observational
  14. Article
  15. Microorganisms · 2019
    Review
  16. Interactions of the effector ExoU fromThe Journal of biological chemistry · 2019
    Article
  17. Role of a patatin-like phospholipase inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. Frontiers in microbiology · 2019
    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

5 authors at 1 institution in 1 country.

David M AndersonDepartments of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin, USA Center for Infectious Disease Research, Medical College of Wisconsin, Milwaukee, Wisconsin, USA.
Hiromi SatoDepartments of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin, USA Center for Infectious Disease Research, Medical College of Wisconsin, Milwaukee, Wisconsin, USA.
Aaron T DirckDepartments of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin, USA.
Jimmy B FeixDepartment of Biophysics, Medical College of Wisconsin, Milwaukee, Wisconsin, USA.
Dara W FrankDepartments of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin, USA Center for Infectious Disease Research, Medical College of Wisconsin, Milwaukee, Wisconsin, USA frankd@mcw.edu.
Medical College of Wisconsin · US

Funding

TR&D Project 3P41EB001980 · NIBIB · MEDICAL COLLEGE OF WISCONSIN · PI KLUG, CANDICE S · 2003 to 2017
$16.3M
Type III effector-cofactor dynamics within the cellular environmentR01AI104922 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI FEIX, JIMMY, FRANK, DARA W. · 2013 to 2021
$3.7M
Mechanism of Activation and Membrane Interactions of Pseudomonas toxin ExoUR01GM114234 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI FEIX, JIMMY · 2015 to 2018
$1.2M
NIAID NIH HHS 1R01 AI104922NIAID NIH HHS R01 AI104922NIBIB NIH HHS P41 EB001980NIGMS NIH HHS R01 GM114234
6 · The paper itself

Abstract

Phospholipase A2 enzymes are ubiquitously distributed throughout the prokaryotic and eukaryotic kingdoms and are utilized in a wide array of cellular processes and physiological and immunological responses. Several patatin-like phospholipase homologs of ExoU from Pseudomonas aeruginosa were selected on the premise that ubiquitin activation of this class of bacterial enzymes was a conserved process. We found that ubiquitin activated all phospholipases tested in both in vitro and in vivo assays via a conserved serine-aspartate catalytic dyad. Ubiquitin chains versus monomeric ubiquitin were superior in inducing catalysis, and ubiquitin-like proteins failed to activate phospholipase activity. Toxicity studies in a prokaryotic dual-expression system grouped the enzymes into high- and low-toxicity classes. Toxicity measured in eukaryotic cells also suggested a two-tiered classification but was not predictive of the severity of cellular damage, suggesting that each enzyme may correspond to unique properties perhaps based on its specific biological function. Additional studies on lipid binding preference suggest that some enzymes in this family may be differentially sensitive to phosphatidyl-4,5-bisphosphate in terms of catalytic activation enhancement and binding affinity. Further analysis of the function and amino acid sequences of this enzyme family may lead to a useful approach to formulating a unifying model of how these phospholipases behave after delivery into the cytoplasmic compartment.

Indexed as

Enzyme ActivatorsPhospholipasesPseudomonas aeruginosaUbiquitinEnzyme ActivatorsPhospholipasesUbiquitin

Identifiers

PMID25404699
PMCPMC4285982
OpenAlexW1982104136

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.