Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The force-sensing device region of α-catenin is an intrinsically disordered segment in the absence of intramolecular stabilization of the autoinhibitory form.

Genes to cells : devoted to molecular & cellular mechanisms - 1 May 2018

Hirano Yoshinori, Amano Yu, Yonemura Shigenobu, Hakoshima Toshio

Abstract excerpt

Mechanotransduction by α-catenin facilitates the force-dependent development of adherens junctions (AJs) by recruiting vinculin to reinforce actin anchoring of AJs. The α-catenin mechanotransducing action is facilitated by its force-sensing device region that autoinhibits the vinculin-binding site 1 (VBS1). Here, we report the high-resolution structure of the force-sensing device region of α-catenin, which shows...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Actins
Share to Adherens Junctions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to alpha Catenin

Share to Crystallography, X-Ray

Share to Mechanotransduction, Cellular

Share to Protein Conformation

Share to Protein Folding

Share to Vinculin

Source

Identifiers

PMID: 29542234
DOI: 10.1111/gtc.12578

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The force-sensing device region of α-catenin is an intrinsically disordered segment in the absence of intramolecular stabilization of the autoinhibitory form.PMID 29542234Read ↗

Force-dependent vinculin binding of α-catenin accelerates adherens junction formation.Semantic proximity Read ↗

α-catenin middle- and actin-binding domain unfolding mutants differentially impact epithelial strength and sheet migration.Semantic proximity Read ↗

αE-catenin is an autoinhibited molecule that coactivates vinculin.Semantic proximity Read ↗

Cadherin mechanotransduction in tissue remodeling.Semantic proximity Read ↗

Myosin forces elicit an F-actin structural landscape that mediates mechanosensitive protein recognitionSemantic proximity Read ↗

Sorting of cadherin-catenin-associated proteins into individual clusters.Semantic proximity Read ↗

VASP, zyxin and TES are tension-dependent members of Focal Adherens Junctions independent of the α-catenin-vinculin module.Semantic proximity Read ↗

Vinculin regulates the recruitment and release of core focal adhesion proteins in a force-dependent manner.Semantic proximity Read ↗

α-Catenin Controls the Anisotropy of Force Distribution at Cell-Cell Junctions during Collective Cell Migration.Semantic proximity Read ↗

Cell adhesions link subcellular actomyosin dynamics to tissue scale force production during vertebrate convergent extensionSemantic proximity Read ↗

α-Catenin and vinculin cooperate to promote high E-cadherin-based adhesion strength.Semantic proximity Read ↗

Modeling the assembly of the multiple domains of α-actinin-4 and its role in actin cross-linking.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.