Evidence map›Paper›PMID 11060018›Full record

ArticleThe EMBO journal2000

Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo.

J Wu, T Tolstykh, J Lee, K Boyd, J B Stock, J R Broach

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

85 citing papers in PubMed, 187 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. STRIPAK, a fundamental signaling hub of eukaryotic development.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  6. The protein methylation network in yeast: A landmark in completeness for a eukaryotic post-translational modification.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. PP2A Functions during Mitosis and Cytokinesis in Yeasts.International journal of molecular sciences · 2019
    Review
  18. Article
  19. Review
  20. Article

25 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

J WuDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
T Tolstykh
J Lee
K Boyd
J B Stock
J R Broach
Princeton University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
VIRAL AND CELLULAR ONCOGENES--MECHANISM OF ACTIONP01CA041086 · NCI · PRINCETON UNIVERSITY · PI WIESCHAUS, ERIC F · 1986 to 2005
$9.4M
NCI NIH HHS CA41086NCI NIH HHS P01 CA041086NIGMS NIH HHS GM07388NIGMS NIH HHS T32 GM007388
6 · The paper itself

Abstract

The phosphoprotein phosphatase 2A (PP2A) catalytic subunit contains a methyl ester on its C-terminus, which in mammalian cells is added by a specific carboxyl methyltransferase and removed by a specific carboxyl methylesterase. We have identified genes in yeast that show significant homology to human carboxyl methyltransferase and methylesterase. Extracts of wild-type yeast cells contain carboxyl methyltransferase activity, while extracts of strains deleted for one of the methyltransferase genes, PPM1, lack all activity. Mutation of PPM1 partially disrupts the PP2A holoenzyme in vivo and ppm1 mutations exhibit synthetic lethality with mutations in genes encoding the B or B' regulatory subunit. Inactivation of PPM1 or overexpression of PPE1, the yeast gene homologous to bovine methylesterase, yields phenotypes similar to those observed after inactivation of either regulatory subunit. These phenotypes can be reversed by overexpression of the B regulatory subunit. These results demonstrate that Ppm1 is the sole PP2A methyltransferase in yeast and that its activity is required for the integrity of the PP2A holoenzyme.

Indexed as

Saccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsAmino Acid SequenceAnimalsCattleCell Cycle ProteinsDNA, ComplementaryDrug Resistance, MicrobialFungal ProteinsGene ExpressionGenes, FungalHumansMethylationMolecular Sequence DataMutationPhenotypeCDC55 protein, S cerevisiaeCell Cycle ProteinsDNA, ComplementaryFungal ProteinsPhosphoprotein Phosphatasesppe1 protein, S pombeProtein MethyltransferasesProtein Phosphatase 2protein-S-isoprenylcysteine O-methyltransferaseProtein SubunitsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsSirolimus

Identifiers

PMID11060018
PMCPMC305778
OpenAlexW2104338484

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.