Evidence map›Paper›PMID 10191253›Full record

ArticleThe Biochemical journal1999

Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Balpha subunit.

J C Bryant, R S Westphal, B E Wadzinski

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing 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

82 citing papers in PubMed, 174 citations in OpenAlex.

  1. Article
  2. Article
  3. Posttranslational Modifications ofPharmacological reviews · 2024
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Potential Role and Clinical Value of PPP2CA in Hepatocellular Carcinoma.Journal of clinical and translational hepatology · 2021
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. UBE3A-mediated PTPA ubiquitination and degradation regulate PP2A activity and dendritic spine morphology.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. Article
  20. Review

22 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

3 authors at 1 institution in 1 country.

J C BryantDepartment of Pharmacology, Room 424 MRB1, Vanderbilt University Medical Center, Nashville, TN 37232-6600, USA.
R S Westphal
B E Wadzinski
Vanderbilt University Medical Center · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
Vanderbilt Diabetes Research CenterP30DK020593 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI OWEN P MCGUINNESS · 2012 to 2026
$29.3M
TRANSGENIC MOUSE/ ES CELL SHARES RESOURCESP60DK020593 · NIDDK · VANDERBILT UNIVERSITY · PI MCGUINNESS, OWEN P · 1986 to 2011
$28.1M
Structure and function of protein kinase/PP2A complexesR01GM051366 · NIGMS · VANDERBILT UNIVERSITY · PI WADZINSKI, BRIAN E · 1994 to 2011
$2.9M
Structure and function of protein kinase/PP2A complexesR56GM051366 · NIGMS · VANDERBILT UNIVERSITY · PI WADZINSKI, BRIAN E · 2007 to 2007
$349k
NCI NIH HHS CA68485NIDDK NIH HHS DK20593NIGMS NIH HHS GM51366
6 · The paper itself

Abstract

Methylation of the C-terminal leucine residue (Leu309) of protein serine/threonine phosphatase 2A catalytic subunit (PP2AC) is known to regulate catalytic activity in vitro, but the functional consequence(s) of this post-translational modification in the context of the cell remain unclear. Alkali-induced demethylation of PP2AC in purified PP2A heterotrimer (ABalphaC), but not in purified PP2A heterodimer (AC), indicated that a larger fraction of PP2AC is carboxymethylated in ABalphaC than in AC. To explore the role of Leu309 in PP2A holoenzyme assembly, epitope-tagged PP2A catalytic subunit (HA-PP2A) and a mutant of HA-PP2A containing an alanine residue in place of Leu309 (HA-PP2A-L309A) were transiently expressed in COS cells. Both recombinant proteins exhibited serine/threonine phosphatase activity when immunoisolated from COS cell extracts. HA-PP2A, but not HA-PP2A-L309A, was carboxymethylated in vitro. A chromatographic analysis of cell extracts indicated that most endogenous PP2AC and HA-PP2A were co-eluted with the A and Balpha regulatory subunits of PP2A, whereas most HA-PP2A-L309A seemed to elute with the A subunit as a smaller complex or, alternatively, as free catalytic (C) subunit. The A subunit co-immunoisolated with both tagged proteins; however, substantially less Balpha subunit co-immunoisolated with HA-PP2A-L309A than with HA-PP2A. These results demonstrate that the reversibly methylated C-terminal leucine residue of PP2AC is important for Balpha regulatory subunit binding. Furthermore, the results provide evidence for an interrelationship between PP2AC carboxymethylation and PP2A holoenzyme assembly.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCatalytic DomainCOS CellsDNA PrimersLeucineMethylationMutagenesis, Site-DirectedPhosphoprotein PhosphatasesProtein BindingProtein Phosphatase 2DNA PrimersLeucinePhosphoprotein PhosphatasesProtein Phosphatase 2

Identifiers

PMID10191253
PMCPMC1220151
OpenAlexW2026508325

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.