Evidence map›Paper›PMID 23292143›Full record

ArticleNature structural & molecular biology2013

Dimer asymmetry defines α-catenin interactions.

Erumbi S Rangarajan, Tina Izard

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

75 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Binding asymmetry and conformational studies of the AtGSDA dimer.Computational and structural biotechnology journal · 2023
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Sorting of cadherin-catenin-associated proteins into individual clusters.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. 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

15 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

2 authors at 1 institution in 1 country.

Erumbi S RangarajanDepartment of Cancer Biology, Scripps Research Institute, Jupiter, Florida, USA.
Tina Izard
Scripps Research Institute · US

Funding

Mechanisms Directing Adherens Junctions and Actin Network InteractionsR01GM094483 · NIGMS · SCRIPPS FLORIDA · PI IZARD, TINA · 2011 to 2019
$3.2M
STRUCTURAL DYNAMICS OF VINCULIN IN ADHESION JUNCTIONSR01GM071596 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI IZARD, TINA · 2004 to 2012
$3.1M
NIGMS NIH HHS GM071596NIGMS NIH HHS GM094483NIGMS NIH HHS R01 GM071596NIGMS NIH HHS R01 GM094483
6 · The paper itself

Abstract

The F-actin-binding cytoskeletal protein α-catenin interacts with β-catenin-cadherin complexes and stabilizes cell-cell junctions. The β-catenin-α-catenin complex cannot bind F-actin, whereas interactions of α-catenin with the cytoskeletal protein vinculin appear to be necessary to stabilize adherens junctions. Here we report the crystal structure of nearly full-length human α-catenin at 3.7-Å resolution. α-catenin forms an asymmetric dimer where the four-helix bundle domains of each subunit engage in distinct intermolecular interactions. This results in a left handshake-like dimer, wherein the two subunits have remarkably different conformations. The crystal structure explains why dimeric α-catenin has a higher affinity for F-actin than does monomeric α-catenin, why the β-catenin-α-catenin complex does not bind F-actin, how activated vinculin links the cadherin-catenin complex to the cytoskeleton and why α-catenin but not inactive vinculin can bind F-actin.

Indexed as

Models, MolecularProtein ConformationActinsAdherens Junctionsalpha CateninChromatography, GelCrystallography, X-RayDimerizationElectrophoretic Mobility Shift AssayHumansImmunoblottingVinculinX-Ray DiffractionActinsalpha CateninVinculin

Identifiers

PMID23292143
PMCPMC3805043
OpenAlexW2052492533

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.