Evidence map›Paper›PMID 31625226›Full record

ReviewAngewandte Chemie (International ed. in English)2019

Phosphorylation Reduces the Mechanical Stability of the α-Catenin/ β-Catenin Complex.

Shimin Le, Miao Yu, Jie Yan

Open access · hybridAbstract readReview
In one paragraph

Review in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Force-dependent structural dynamics of the giant nesprin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Implication of protein post translational modifications in gastric cancer.Frontiers in cell and developmental biology · 2025
    Review
  4. Article
  5. Review
  6. Single-molecule force spectroscopy reveals intra- and intermolecular interactions ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
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

3 authors at 1 institution in 1 country.

Shimin LeMechanobiology Institute, National University of Singapore, Singapore, 117411, Singapore.
Miao YuMechanobiology Institute, National University of Singapore, Singapore, 117411, Singapore.
Jie YanMechanobiology Institute, National University of Singapore, Singapore, 117411, Singapore.ORCID 0000-0002-8555-7291
National University of Singapore · SG

Funding

Singapore Ministry of Education Academic Research Fund Tier 3 MOE2016-T3-1-002the Ministry of Education under the Research Centres of Excellence programmethe National Research Foundation, Prime Minister's Office, Singapore, under its NRF Investigatorship Programme NRF-NRFI2016-03
6 · The paper itself

Abstract

The α-catenin/β-catenin complex serves as a critical molecular interface involved in cadherin-catenin-based mechanosensing at the cell-cell adherence junction that plays a critical role in tissue integrity, repair, and embryonic development. This complex is subject to tensile forces due to internal actomyosin contractility and external mechanical micro-environmental perturbation. However, the mechanical stability of this complex has yet to be quantified. Here, we directly quantified the mechanical stability of the α-catenin/β-catenin complex and showed that it has enough mechanical stability to survive for tens to hundreds of seconds within physiological level of forces up to 10 pN. Phosphorylation or phosphotyrosine-mimetic mutations (Y142E or/and T120E) on β-catenin shorten the mechanical lifetime of the complex by tens of fold over the same force range. These results provide insights into the regulation of the α-catenin/β-catenin complex by phosphorylation.

Indexed as

alpha Cateninbeta CateninHumansPhosphorylationalpha Cateninbeta Cateninforcemechanotransductionphosphorylationα-cateninβ-catenin

Identifiers

PMID31625226
PMCPMC6916283
OpenAlexW2980422027

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.