Evidence map›Paper›PMID 18397887›Full record

ArticleThe Journal of biological chemistry2008

Protein phosphatase 2A is targeted to cell division control protein 6 by a calcium-binding regulatory subunit.

Anthony J Davis, Zhen Yan, Bobbie Martinez, Marc C Mumby

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

29 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Targeting PP2A in cancer: an underrated option.Journal of experimental & clinical cancer research : CR · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Fine mapping of a QTL locus (Molecular breeding : new strategies in plant improvement · 2021
    Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. A PP2A-mediated feedback mechanism controls CaFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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

4 authors at 2 institutions in 1 country.

Anthony J DavisDepartment of Pharmacology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-9041, USA.
Zhen Yan
Bobbie Martinez
Marc C Mumby
The University of Texas Southwestern Medical Center · USDuke Medical Center · US

Funding

MECHANISMS OF DRUG ACTION AND DISPOSITIONT32GM007062 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MANGELSDORF, DAVID J · 1985 to 2020
$7.4M
REGULATION OF PROTEIN DEPHOSPHROYLATIONR01GM049505 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI MUMBY, MARC C. · 1994 to 2005
$1.8M
NIGMS NIH HHS GM49505NIGMS NIH HHS R01 GM049505NIGMS NIH HHS T32 GM007062NIGMS NIH HHS T32 GM07062
6 · The paper itself

Abstract

The cell division control protein 6 (Cdc6) is essential for formation of pre-replication complexes at origins of DNA replication. Phosphorylation of Cdc6 by cyclin-dependent kinases inhibits ubiquitination of Cdc6 by APC/C(cdh1) and degradation by the proteasome. Experiments described here show that the PR70 member of the PPP2R3 family of regulatory subunits targets protein phosphatase 2A (PP2A) to Cdc6. Interaction with Cdc6 is mediated by residues within the C terminus of PR70, whereas interaction with PP2A requires N-terminal sequences conserved within the PPP2R3 family. Two functional EF-hand calcium-binding motifs mediate a calcium-enhanced interaction of PR70 with PP2A. Calcium has no effect on the interaction of PR70 with Cdc6 but enhances the association of PP2A with Cdc6 through its effects on PR70. Knockdown of PR70 by RNA interference results in an accumulation of endogenous and expressed Cdc6 protein that is dependent on the cyclin-dependent protein kinase phosphorylation sites on Cdc6. Knockdown of PR70 also causes G(1) arrest, suggesting that PR70 function is critical for progression into S phase. These observations indicate that PP2A can be targeted in a calcium-regulated manner to Cdc6 via the PR70 subunit, where it plays a role in regulating protein phosphorylation and stability.

Indexed as

Amino Acid MotifsAnimalsAntigens, CDCadherinsCalciumCell Cycle ProteinsChlorocebus aethiopsCOS CellsDNA ReplicationG1 PhaseHeLa CellsHumansNuclear ProteinsPhosphorylationProteasome Endopeptidase ComplexProtein Phosphatase 2Antigens, CDCadherinsCalciumCDC6 protein, humanCDH1 protein, humanCell Cycle ProteinsNuclear ProteinsProteasome Endopeptidase ComplexProtein Phosphatase 2Protein Subunits

Identifiers

PMID18397887
PMCPMC2414307
OpenAlexW2040038307

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.