Evidence map›Paper›PMID 27998540›Full record

ArticleStructure (London, England : 1993)2016

Expanding the PP2A Interactome by Defining a B56-Specific SLiM.

Xinru Wang, Rakhi Bajaj, Mathieu Bollen, Wolfgang Peti, Rebecca Page

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

101 citing papers in PubMed, 157 citations in OpenAlex.

  1. Article
  2. Liprin-α family proteins and their cellular functions.The Journal of biological chemistry · 2026
    Review
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  6. Targeting PP2A in cancer: an underrated option.Journal of experimental & clinical cancer research : CR · 2025
    Review
  7. Review
  8. Houge-Janssens syndrome.European journal of human genetics : EJHG · 2025
    Review
  9. Article
  10. Fuzziness in enzymatic catalysis.Current opinion in structural biology · 2025
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. A protein phosphatase 1 specificProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article

41 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

5 authors at 2 institutions in 2 countries.

Xinru WangDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02912, USA.
Rakhi BajajDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02912, USA.
Mathieu BollenLaboratory of Biosignaling & Therapeutics, Department of Cellular and Molecular Medicine, KU Leuven, 3000 Leuven, Belgium.
Wolfgang PetiDepartment of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA; Department Chemistry, Brown University, Providence, RI 02912, USA.
Rebecca PageDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02912, USA. Electronic address: rebecca_page@brown.edu.
Brown University · USKU Leuven · BE

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
The Regulation of PP1 in the NucleusR01GM098482 · NIGMS · UNIVERSITY OF ARIZONA · PI PAGE, REBECCA · 2011 to 2019
$2.8M
Supplement for "Serine/Threonine Phosphatases in Neurological Diseases"R01NS091336 · NINDS · UNIVERSITY OF ARIZONA · PI PAGE, REBECCA, PETI, WOLFGANG · 2015 to 2019
$1.8M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM098482NINDS NIH HHS R01 NS091336
6 · The paper itself

Abstract

Specific interactions between proteins govern essential physiological processes including signaling. Many enzymes, especially the family of serine/threonine phosphatases (PSPs: PP1, PP2A, and PP2B/calcineurin/CN), recruit substrates and regulatory proteins by binding short linear motifs (SLiMs), short sequences found within intrinsically disordered regions that mediate specific protein-protein interactions. While tremendous progress had been made in identifying where and how SLiMs bind PSPs, especially PP1 and CN, essentially nothing is known about how SLiMs bind PP2A, a validated cancer drug target. Here we describe three structures of a PP2A-SLiM interaction (B56:pS-RepoMan, B56:pS-BubR1, and B56:pSpS-BubR1), show that this PP2A-specific SLiM is defined as LSPIxE, and then use these data to discover scores of likely PP2A regulators and substrates. Together, these data provide a powerful approach not only for dissecting PP2A interaction networks in cells but also for targeting PP2A diseases, such as cancer.

Indexed as

Amino Acid MotifsBinding SitesCarrier ProteinsCell Cycle ProteinsCrystallography, X-RayHumansModels, MolecularNuclear ProteinsPhosphorylationProtein BindingProtein Phosphatase 2Protein Serine-Threonine KinasesSerineBUB1 protein, humanCarrier ProteinsCDCA2 protein, humanCell Cycle ProteinsNuclear ProteinsPPP2R5A protein, humanProtein Phosphatase 2Protein Serine-Threonine KinasesSerineB56BubR1mitosisNMR spectroscopyphosphorylationPP2ARepoMansmall linear motif (SLiM)X-ray crystallography

Identifiers

PMID27998540
PMCPMC5180209
OpenAlexW2539509011

What OpenQuestion holds

Textmetadata
LicenceTDM
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.