Evidence map›Paper›PMID 24596249›Full record

ArticleThe EMBO journal2014

Molecular functions of the TLE tetramerization domain in Wnt target gene repression.

Jayanth V Chodaparambil, Kira T Pate, Margretta R D Hepler, Becky P Tsai, Uma M Muthurajan, Karolin Luger, Marian L Waterman, William I Weis

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
15.4field-weighted citation impact, top 1% 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

69 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

9 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

8 authors at 3 institutions in 1 country.

Jayanth V ChodaparambilDepartments of Structural Biology and Molecular & Cellular Physiology, Stanford University School of Medicine, Stanford, CA, USA.
Kira T Pate
Margretta R D Hepler
Becky P Tsai
Uma M Muthurajan
Karolin Luger
Marian L Waterman
William I Weis
Colorado State University · USUniversity of California, Irvine · USStanford University · US

Funding

Univ.of Calif., Irvine Cancer Center Support GrantP30CA062203 · NCI · UNIVERSITY OF CALIFORNIA-IRVINE · PI Christine Hui · 1994 to 2026
$57.9M
project 3P01GM088409 · NIGMS · COLORADO STATE UNIVERSITY · PI NYBORG, JENNIFER K. · 2010 to 2014
$7.3M
CATENINS, CADHERINS AND THEIR INTERACTIONSR01GM056169 · NIGMS · STANFORD UNIVERSITY · PI WEIS, WILLIAM I · 1997 to 2012
$5.0M
LEF/TCF Expression in Colon CancerR01CA096878 · NCI · UNIVERSITY OF CALIFORNIA-IRVINE · PI WATERMAN, MARIAN L · 2003 to 2012
$2.7M
Wnt Signaling in Colon CancerR01CA108697 · NCI · UNIVERSITY OF CALIFORNIA-IRVINE · PI WATERMAN, MARIAN L · 2005 to 2015
$2.7M
Molecular Mechanisms of Wnt Signal TransductionR01GM119156 · NIGMS · STANFORD UNIVERSITY · PI WEIS, WILLIAM I · 2016 to 2019
$1.3M
Howard Hughes Medical InstituteNCI NIH HHS CA096878NCI NIH HHS CA108697NCI NIH HHS P30 CA062203NCI NIH HHS P30CA062203NCI NIH HHS R01 CA096878NCI NIH HHS R01 CA108697NIGMS NIH HHS GM56169NIGMS NIH HHS P01 GM088409NIGMS NIH HHS P01-GM088409NIGMS NIH HHS R01 GM056169NIGMS NIH HHS R01 GM119156
6 · The paper itself

Abstract

Wnt signaling activates target genes by promoting association of the co-activator β-catenin with TCF/LEF transcription factors. In the absence of β-catenin, target genes are silenced by TCF-mediated recruitment of TLE/Groucho proteins, but the molecular basis for TLE/TCF-dependent repression is unclear. We describe the unusual three-dimensional structure of the N-terminal Q domain of TLE1 that mediates tetramerization and binds to TCFs. We find that differences in repression potential of TCF/LEFs correlates with their affinities for TLE-Q, rather than direct competition between β-catenin and TLE for TCFs as part of an activation-repression switch. Structure-based mutation of the TLE tetramer interface shows that dimers cannot mediate repression, even though they bind to TCFs with the same affinity as tetramers. Furthermore, the TLE Q tetramer, not the dimer, binds to chromatin, specifically to K20 methylated histone H4 tails, suggesting that the TCF/TLE tetramer complex promotes structural transitions of chromatin to mediate repression.

Indexed as

Gene Expression RegulationModels, MolecularSignal TransductionAnimalsBasic Helix-Loop-Helix Proteinsbeta CateninCell LineChlorocebus aethiopsChromatinCo-Repressor ProteinsCOS CellsCrystallographyHistonesHumansMethylationMiceBasic Helix-Loop-Helix Proteinsbeta CateninChromatinCo-Repressor ProteinsHistonesRepressor ProteinsTCF3 protein, humanTCF Transcription FactorsTLE1 protein, humanWnt Proteins

Identifiers

PMID24596249
PMCPMC4000089
OpenAlexW2034932027

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.