Evidence map›Paper›PMID 19565571›Full record

ArticleJournal of cellular biochemistry2009

Threonine 393 of beta-catenin regulates interaction with Axin.

Hao Wu, Karen Symes, David C Seldin, Isabel Dominguez

Abstract read
In one paragraph

Article in Journal of cellular biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Review
  3. HGG advances · 2022
    Article
  4. Review
  5. Protein Kinase CK2 in Cancer Energetics.Frontiers in oncology · 2020
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Asymmetric Localization of CK2α DuringHuman genetics & embryology : current research · 2012
    Article
  12. Article
  13. Review
  14. CK2α is essential for embryonic morphogenesis.Molecular and cellular biochemistry · 2011
    Article
  15. Article
  16. Article
  17. 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 1 institution in 1 country.

Hao WuDepartment of Medicine, Boston University School of Medicine, Boston, Massachusetts 02118, USA.
Karen Symes
David C Seldin
Isabel Dominguez
Boston University · US

Funding

Signaling Pathways in Stages of TumorigenesisP01ES011624 · NIEHS · TUFTS UNIVERSITY BOSTON · PI SONENSHEIN, GAIL E. · 2001 to 2012
$11.4M
Multistep Lymphomagenesis/Tumorigenesis in Transgenic Mice: Protein Kinase Ck2R01CA071796 · NCI · BOSTON MEDICAL CENTER · PI SELDIN, DAVID C · 1997 to 2010
$2.8M
CELL MOVEMENT DURING XENOPUS DEVELOPMENT--METASTASISR01CA087375 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SYMES, KAREN · 2000 to 2004
$1.3M
NCI NIH HHS R01 CA071796NCI NIH HHS R01 CA087375NCI NIH HHS R01 CA71796NCI NIH HHS R01 CA 87375NIEHS NIH HHS P01 ES011624
6 · The paper itself

Abstract

CK2 is a regulatory kinase implicated in embryonic development and in cancer. Among the CK2 substrates is beta-catenin, a protein with dual function in Wnt signaling and cell adhesion. Previously, we reported that CK2 activity is required for beta-catenin stability and we identified threonine (T) 393 as a major CK2 phosphorylation site in beta-catenin. However, it is not known whether phosphorylation at T393 increases beta-catenin stability and if so, what is the mechanism. In this study we investigate the molecular mechanism of beta-catenin stabilization through phosphorylation at T393. We found that pseudophosphorylation of beta-catenin at T393 resulted in a stable activated form of beta-catenin with decreased affinity for Axin in vitro. This phosphomimetic mutant also displayed decreased regulation by Axin in vivo in a bioassay in Xenopus laevis embryos. In contrast, the binding of T393 pseudophosphorylated beta-catenin to E-cadherin was unaffected. Further analysis showed that pseudophosphorylation at T393 did not prevent beta-catenin phosphorylation by GSK3beta. Interestingly, we found that in the presence of pseudophophorylated beta-catenin and another activated form of beta-catenin, the recruitment of GSK3beta to Axin is enhanced. These findings indicate that phosphorylation of T393 by CK2 may affect the stability of beta-catenin through decreased binding to Axin. In addition, the increased recruitment of GSK3beta to the destruction complex in the presence of activated beta-catenin mutants could be a feedback mechanism to suppress overactive Wnt signaling.

Indexed as

AnimalsAxin Proteinbeta CateninBinding SitesCadherinsCells, CulturedEmbryo, NonmammalianHumansMutationPhosphorylationRepressor ProteinsSignal TransductionThreonineTranscriptional ActivationTransfectionXenopusaxin1 protein, XenopusAxin Proteinbeta CateninCadherinsRepressor ProteinsThreonineXenopus Proteins

Identifiers

PMID19565571
PMCPMC3398408
OpenAlexW2088251407

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.