Evidence map›Paper›PMID 22493458›Full record

ArticleThe Journal of biological chemistry2012

The cytoskeletal protein α-catenin unfurls upon binding to vinculin.

Erumbi S Rangarajan, Tina Izard

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. 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
4.6field-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

69 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
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  6. Nanoscale dynamics of the cadherin-catenin complex bound to vinculin revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  9. Characterization of early and late events of adherens junction assembly.bioRxiv : the preprint server for biology · 2024
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  12. Review
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  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. 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

2 authors at 1 institution in 1 country.

Erumbi S RangarajanDepartment of Cancer Biology, The Scripps Research Institute, Jupiter, Florida 33458, 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
NIGMS NIH HHS R01 GM094483
6 · The paper itself

Abstract

Adherens junctions (AJs) are essential for cell-cell contacts, morphogenesis, and the development of all higher eukaryotes. AJs are formed by calcium-dependent homotypic interactions of the ectodomains of single membrane-pass cadherin family receptors. These homotypic interactions in turn promote binding of the intracellular cytoplasmic tail domains of cadherin receptors with β-catenin, a multifunctional protein that plays roles in both transcription and AJs. The cadherin receptor-β-catenin complex binds to the cytoskeletal protein α-catenin, which is essential for both the formation and the stabilization of these junctions. Precisely how α-catenin contributes to the formation and stabilization of AJs is hotly debated, although the latter is thought to involve its interactions with the cytoskeletal protein vinculin. Here we report the crystal structure of the vinculin binding domain (VBD) of α-catenin in complex with the vinculin head domain (Vh1). This structure reveals that α-catenin is in a unique unfurled mode allowing dimer formation when bound to vinculin. Finally, binding studies suggest that vinculin must be in an activated state to bind to α-catenin and that this interaction is stabilized by the formation of a ternary α-catenin-vinculin-F-actin complex, which can be formed via the F-actin binding domain of either protein. We propose a feed-forward model whereby α-catenin-vinculin interactions promote their binding to the actin cytoskeleton to stabilize AJs.

Indexed as

alpha CateninAmino Acid SequenceChromatography, GelChromatography, High Pressure LiquidCrystallizationCytoskeletal ProteinsHumansModels, MolecularMolecular Sequence DataProtein BindingSpectrophotometry, UltravioletVinculinalpha CateninCytoskeletal ProteinsVinculin

Identifiers

PMID22493458
PMCPMC3365723
OpenAlexW2076250658

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.