ArticleThe Journal of cell biology2017
α-Catenin homodimers are recruited to phosphoinositide-activated membranes to promote adhesion.
Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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.
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.
Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Intact Mass Profiling Reveals Phospho-Proteoforms of the Catenins (85-110 kDa) Regulated by Actomyosin Contractility.Angewandte Chemie (International ed. in English) · 2025Article
- Distinct strategies of epithelial cell barrier disruption by Leptospira interrogans isolated from human patients in Okinawa, Japan.PLoS neglected tropical diseases · 2025Article
- α-Catenin force-sensitive binding and sequestration of LZTS2 leads to cytokinesis failure.The Journal of cell biology · 2025Article
- Actin-dependent α-catenin oligomerization contributes to adherens junction assembly.Nature communications · 2025Article
- Exploring genetic associations in systemic lupus erythematosus through Mendelian randomization: implications for novel biomarkers and therapeutic targets.Clinical rheumatology · 2025Article
- Article
- α-catenin middle- and actin-binding domain unfolding mutants differentially impact epithelial strength and sheet migration.Molecular biology of the cell · 2024Article
- Characterization of early and late events of adherens junction assembly.bioRxiv : the preprint server for biology · 2024Article
- Plakophilin-3 Binds the Membrane and Filamentous Actin without Bundling F-Actin.International journal of molecular sciences · 2023Article
- Distinct inter-domain interactions of dimeric versus monomeric α-catenin link cell junctions to filaments.Communications biology · 2023Article
- α-Catenin links integrin adhesions to F-actin to regulate ECM mechanosensing and rigidity dependence.The Journal of cell biology · 2022Article
- α-catenin switches between a slip and an asymmetric catch bond with F-actin to cooperatively regulate cell junction fluidity.Nature communications · 2022Article
- 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 · 2021Article
- Phosphoinositide-Dependent Signaling in Cancer: A Focus on Phospholipase C Isozymes.International journal of molecular sciences · 2020Review
- Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions.Nature communications · 2018Article
- α-Catenin Structure and Nanoscale Dynamics in Solution and in Complex with F-Actin.Biophysical journal · 2018Article
- Mechanoregulation and pathology of YAP/TAZ via Hippo and non-Hippo mechanisms.Clinical and translational medicine · 2018Review
- αT-catenin: A developmentally dispensable, disease-linked member of the α-catenin family.Tissue barriers · 2018Review
- So far, yet so close: α-Catenin dimers help migrating cells get together.The Journal of cell biology · 2017Article
- Distinct intramolecular interactions regulate autoinhibition of vinculin binding in αT-catenin and αE-catenin.The Journal of biological chemistryArticle
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
A unique feature of α-catenin localized outside the cadherin-catenin complex is its capacity to form homodimers, but the subcellular localization and functions of this form of α-catenin remain incompletely understood. We identified a cadherin-free form of α-catenin that is recruited to the leading edge of migrating cells in a phosphatidylinositol 3-kinase-dependent manner. Surface plasmon resonance analysis shows that α-catenin homodimers, but not monomers, selectively bind phosphatidylinositol-3,4,5-trisphosphate-containing lipid vesicles with high affinity, where three basic residues, K488, K493, and R496, contribute to binding. Chemical-induced dimerization of α-catenin containing a synthetic dimerization domain promotes its accumulation within lamellipodia and elaboration of protrusions with extended filopodia, which are attenuated in the α-catenin
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What OpenQuestion holds
Registered trials
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.