Evidence map›Paper›PMID 24692547›Full record

ArticleThe Journal of biological chemistry2014

Structural and thermodynamic characterization of cadherin·β-catenin·α-catenin complex formation.

Sabine Pokutta, Hee-Jung Choi, Goran Ahlsen, Scott D Hansen, William I Weis

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Hereditary Diffuse Gastric Cancer: A 2022 Update.Journal of personalized medicine · 2022
    Review
  8. Article
  9. Article
  10. Activated nanoscale actin-binding domain motion in the catenin-cadherin complex revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. The adhesion modulation domain ofMolecular biology of the cell · 2019
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  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

5 authors at 4 institutions in 2 countries.

Sabine PokuttaFrom the Departments of Structural Biology and Molecular and Cellular Physiology, Stanford University, Stanford, California 94305.
Hee-Jung Choi
Goran Ahlsen
Scott D Hansen
William I Weis
Stanford University · USHoward Hughes Medical Institute · USSeoul National University · KRUniversity of California, San Francisco · US

Funding

Assemby , dynamics and evolution of cell-cell and cell-matrix adhesionsU01GM094663 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI WEIS, WILLIAM I · 2010 to 2014
$6.4M
CATENINS, CADHERINS AND THEIR INTERACTIONSR01GM056169 · NIGMS · STANFORD UNIVERSITY · PI WEIS, WILLIAM I · 1997 to 2012
$5.0M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM056169NIGMS NIH HHS R01 GM56169NIGMS NIH HHS U01 GM094663
6 · The paper itself

Abstract

The classical cadherin·β-catenin·α-catenin complex mediates homophilic cell-cell adhesion and mechanically couples the actin cytoskeletons of adjacent cells. Although α-catenin binds to β-catenin and to F-actin, β-catenin significantly weakens the affinity of α-catenin for F-actin. Moreover, α-catenin self-associates into homodimers that block β-catenin binding. We investigated quantitatively and structurally αE- and αN-catenin dimer formation, their interaction with β-catenin and the cadherin·β-catenin complex, and the effect of the α-catenin actin-binding domain on β-catenin association. The two α-catenin variants differ in their self-association properties: at physiological temperatures, αE-catenin homodimerizes 10× more weakly than does αN-catenin but is kinetically trapped in its oligomeric state. Both αE- and αN-catenin bind to β-catenin with a Kd of 20 nM, and this affinity is increased by an order of magnitude when cadherin is bound to β-catenin. We describe the crystal structure of a complex representing the full β-catenin·αN-catenin interface. A three-dimensional model of the cadherin·β-catenin·α-catenin complex based on these new structural data suggests mechanisms for the enhanced stability of the ternary complex. The C-terminal actin-binding domain of α-catenin has no influence on the interactions with β-catenin, arguing against models in which β-catenin weakens actin binding by stabilizing inhibitory intramolecular interactions between the actin-binding domain and the rest of α-catenin.

Indexed as

alpha CateninAnimalsbeta CateninCadherinsCrystallography, X-RayMiceMultiprotein ComplexesProtein Structure, QuaternaryThermodynamicsalpha Cateninbeta CateninCadherinsMultiprotein ComplexesAnalytical UltracentrifugationCadherinsCell AdhesionIsothermal Titration CalorimetryX-ray Crystallographyα-Cateninβ-Catenin

Identifiers

PMID24692547
PMCPMC4036364
OpenAlexW1493497001

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.