Evidence map›Paper›PMID 31992581›Full record

ArticleScience signaling2020

Antibodies recognizing the C terminus of PP2A catalytic subunit are unsuitable for evaluating PP2A activity and holoenzyme composition.

Ingrid E Frohner, Ingrid Mudrak, Stephanie Kronlachner, Stefan Schüchner, Egon Ogris

Abstract read
PubMed Publisher
In one paragraph

Article in Science signaling, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.0field-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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Renal ATCirculation research · 2022
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Ingrid E FrohnerCenter for Medical Biochemistry, Max Perutz Labs, Vienna BioCenter, Medical University of Vienna, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria.ORCID 0000-0002-0200-449X
Ingrid MudrakCenter for Medical Biochemistry, Max Perutz Labs, Vienna BioCenter, Medical University of Vienna, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria.
Stephanie KronlachnerCenter for Medical Biochemistry, Max Perutz Labs, Vienna BioCenter, Medical University of Vienna, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria.
Stefan SchüchnerCenter for Medical Biochemistry, Max Perutz Labs, Vienna BioCenter, Medical University of Vienna, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria.ORCID 0000-0003-3931-822X
Egon OgrisCenter for Medical Biochemistry, Max Perutz Labs, Vienna BioCenter, Medical University of Vienna, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria. egon.ogris@meduniwien.ac.at.ORCID 0000-0001-5950-9264
Max Perutz Labs · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The methyl-esterification of the C-terminal leucine of the protein phosphatase 2A (PP2A) catalytic (C) subunit is essential for the assembly of specific trimeric PP2A holoenzymes, and this region of the C subunit also contains two threonine and tyrosine phosphorylation sites. Most commercial antibodies-including the monoclonal antibody 1D6 that is part of a frequently used, commercial phosphatase assay kit-are directed toward the C terminus of the C subunit, raising questions as to their ability to recognize methylated and phosphorylated forms of the enzyme. Here, we tested several PP2A C antibodies, including monoclonal antibodies 1D6, 7A6, G-4, and 52F8 and the polyclonal antibody 2038 for their ability to specifically detect PP2A in its various modified forms, as well as to coprecipitate regulatory subunits. The tested antibodies preferentially recognized the nonmethylated form of the enzyme, and they did not coimmunoprecipitate trimeric holoenzymes containing the regulatory subunits B or B', an issue that precludes their use to monitor PP2A holoenzyme activity. Furthermore, some of the antibodies also recognized the phosphatase PP4, demonstrating a lack of specificity for PP2A. Together, these findings suggest that reinterpretation of the data generated by using these reagents is required.

Indexed as

Protein MultimerizationProtein Phosphatase 2AnimalsAntibodiesCell LineHEK293 CellsHoloenzymesHumansMiceRabbitsAntibodiesHoloenzymesPPP2CA protein, mouseProtein Phosphatase 2

Identifiers

PMID31992581
OpenAlexW3003646137

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.