Evidence map›Paper›PMID 29142072›Full record

ArticleMolecular biology of the cell2018

Salt bridges gate α-catenin activation at intercellular junctions.

Samantha Barrick, Jing Li, Xinyu Kong, Alokananda Ray, Emad Tajkhorshid, Deborah Leckband

Abstract readVideo-Audio Media
In one paragraph

Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

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  4. Single-molecule force spectroscopy reveals intra- and intermolecular interactions ofProceedings of the National Academy of Sciences of the United States of America · 2024
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  5. bioRxiv : the preprint server for biology · 2024
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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

6 authors at 1 institution in 1 country.

Samantha BarrickDepartment of Chemistry, University of Illinois, Urbana, IL 61801.
Jing LiCenter for Biophysics and Quantitative Biology, University of Illinois, Urbana, IL 61801.
Xinyu KongDepartment of Biochemistry, University of Illinois, Urbana, IL 61801.
Alokananda RayDepartment of Biochemistry, University of Illinois, Urbana, IL 61801.
Emad TajkhorshidCenter for Biophysics and Quantitative Biology, University of Illinois, Urbana, IL 61801.
Deborah LeckbandDepartment of Chemistry, University of Illinois, Urbana, IL 61801 leckband@illinois.edu.
University of Illinois Urbana-Champaign · US

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
Cadherin Adhesion and MechanosensingR01GM097443 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI LECKBAND, DEBORAH E · 2012 to 2016
$1.3M
NIGMS NIH HHS P41 GM104601NIGMS NIH HHS R01 GM097443
6 · The paper itself

Abstract

Cadherin complexes transduce force fluctuations at junctions to activate signals that reinforce stressed intercellular contacts. α-Catenin is an identified force transducer within cadherin complexes that is autoinhibited under low tension. Increased force triggers a conformational change that exposes a cryptic site for the actin-binding protein vinculin. This study tested predictions that salt bridges within the force-sensing core modulate α-catenin activation. Studies with a fluorescence resonance energy transfer (FRET)-based α-catenin conformation sensor demonstrated that each of the salt-bridge mutations R551A and D503N enhances α-catenin activation in live cells, but R551A has a greater impact. Under dynamic force loading at reannealing cell-cell junctions, the R551A mutant bound more vinculin than wild-type α-catenin. In vitro binding measurements quantified the impact of the R551A mutation on the free-energy difference between the active and autoinhibited α-catenin conformers. A 2-μs constant-force, steered molecular dynamics simulation of the core force-sensing region suggested how the salt-bridge mutants alter the α-catenin conformation, and identified a novel load-bearing salt bridge. These results reveal key structural features that determine the force-transduction mechanism and the force sensitivity of this crucial nanomachine.

Indexed as

Actinsalpha CateninAnimalsCadherinsCells, CulturedFluorescence Resonance Energy TransferHEK293 CellsHumansIntercellular JunctionsMicrofilament ProteinsMolecular Dynamics SimulationVinculinActinsalpha CateninCadherinsMicrofilament ProteinsVinculin

Identifiers

PMID29142072
PMCPMC5909925
OpenAlexW2770444774

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.