Evidence map›Paper›PMID 23752926›Full record

ArticleCell research2013

Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation.

Nathan Wlodarchak, Feng Guo, Kenneth A Satyshur, Li Jiang, Philip D Jeffrey, Tingwan Sun, Vitali Stanevich, Marc C Mumby, Yongna Xing

Open access · hybridAbstract read
In one paragraph

Article in Cell research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 77 citations in OpenAlex.

  1. Metabotropic signaling downstream of GABANPJ Parkinson's disease · 2026
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  5. Targeting PP2A in cancer: an underrated option.Journal of experimental & clinical cancer research : CR · 2025
    Review
  6. Article
  7. Saturated fatty acids stimulate cytokine production in tanycytes via the PP2Ac-dependent signaling pathway.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2024
    Article
  8. Article
  9. Quantum-based modeling implies that bidentate ArgFrontiers in cell and developmental biology · 2023
    Article
  10. Review
  11. Article
  12. Postmitotic G1 phase survivin drives mitogen-independent cell division of B lymphocytes.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Cryo-EM structure of the Hippo signaling integrator human STRIPAK.Nature structural & molecular biology · 2021
    Article
  20. PP2A Phosphatase as an Emerging Viral Host Factor.Frontiers in cellular and infection microbiology · 2021
    Review
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

9 authors at 3 institutions in 1 country.

Nathan WlodarchakMcArdle Laboratory, Department of Oncology, University of Wisconsin-Madison, School of Medicine and Public Health, Madison, WI, USA.
Feng Guo
Kenneth A Satyshur
Li Jiang
Philip D Jeffrey
Tingwan Sun
Vitali Stanevich
Marc C Mumby
Yongna Xing
University of Wisconsin–Madison · USThe University of Texas Southwestern Medical Center · USPrinceton University · US

Funding

Training in Cancer Biology Training GrantT32CA009135 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI SUGDEN, WILLIAM M. · 1985 to 2024
$10.4M
Structural and Biochemical Insights into PP2A Holoenzyme BiogenesisR01GM096060 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI XING, YONGNA · 2012 to 2016
$1.7M
Cell cycle regulation by protein phosphatase 2AR01GM086560 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MUMBY, MARC C. · 2009 to 2012
$1.2M
NCI NIH HHS T32 CA009135NIGMS NIH HHS GM86560NIGMS NIH HHS R01 GM086560NIGMS NIH HHS R01 GM096060NIGMS NIH HHS R01 GM096060-01
6 · The paper itself

Abstract

The B″/PR72 family of protein phosphatase 2A (PP2A) is an important PP2A family involved in diverse cellular processes, and uniquely regulated by calcium binding to the regulatory subunit. The PR70 subunit in this family interacts with cell division control 6 (Cdc6), a cell cycle regulator important for control of DNA replication. Here, we report crystal structures of the isolated PR72 and the trimeric PR70 holoenzyme at a resolution of 2.1 and 2.4 Å, respectively, and in vitro characterization of Cdc6 dephosphorylation. The holoenzyme structure reveals that one of the PR70 calcium-binding motifs directly contacts the scaffold subunit, resulting in the most compact scaffold subunit conformation among all PP2A holoenzymes. PR70 also binds distinctively to the catalytic subunit near the active site, which is required for PR70 to enhance phosphatase activity toward Cdc6. Our studies provide a structural basis for unique regulation of B″/PR72 holoenzymes by calcium ions, and suggest the mechanisms for precise control of substrate specificity among PP2A holoenzymes.

Indexed as

AnimalsCalciumCell Cycle ProteinsCrystallography, X-RayHoloenzymesHumansPhosphorylationProtein Phosphatase 2Protein SubunitsSubstrate SpecificityCalciumCell Cycle ProteinsHoloenzymesProtein Phosphatase 2Protein Subunits

Identifiers

PMID23752926
PMCPMC3698643
OpenAlexW2110138808

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.