ArticleMolecular and cellular biology2007
Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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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.
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Who cites it
45 citing papers in PubMed, 85 citations in OpenAlex.
- PAK2 promotes CTC cluster formation by phosphorylating E-cadherin to enhance cell-cell adhesion in breast cancer.Breast cancer research : BCR · 2025Article
- Maintaining Genome Integrity: Protein Kinases and Phosphatases Orchestrate the Balancing Act of DNA Double-Strand Breaks Repair in Cancer.International journal of molecular sciences · 2023Review
- Transcriptional signatures associated with rubella virus-specific humoral immunity after a third dose of MMR vaccine in women of childbearing age.European journal of immunology · 2021Article
- Rac1-PAK1 regulation of Rab11 cycling promotes junction destabilization.The Journal of cell biology · 2021Article
- Metformin inhibition of colorectal cancer cell migration is associated with rebuilt adherens junctions and FAK downregulation.Journal of cellular physiology · 2020Article
- Regulation of Epithelial-Mesenchymal Plasticity by the E3 Ubiquitin-Ligases in Cancer.Cancers · 2020Review
- Src and Fyn define a new signaling cascade activated by canonical and non-canonical Wnt ligands and required for gene transcription and cell invasion.Cellular and molecular life sciences : CMLS · 2020Article
- Protein Phosphatase 2A: More Than a Passenger in the Regulation of Epithelial Cell-Cell Junctions.Frontiers in cell and developmental biology · 2019Review
- Casein kinase 1α: biological mechanisms and theranostic potential.Cell communication and signaling : CCS · 2018Review
- Review
- The canonical way to make a heart: β-catenin and plakoglobin in heart development and remodeling.Experimental biology and medicine (Maywood, N.J.) · 2017Review
- The β-TrCP-FBXW2-SKP2 axis regulates lung cancer cell growth with FBXW2 acting as a tumour suppressor.Nature communications · 2017Article
- VE-cadherin interacts with cell polarity protein Pals1 to regulate vascular lumen formation.Molecular biology of the cell · 2016Article
- Adherens Junction and E-Cadherin complex regulation by epithelial polarity.Cellular and molecular life sciences : CMLS · 2016Review
- Distinct Signaling Requirements for the Establishment of ESC Pluripotency in Late-Stage EpiSCs.Cell reports · 2016Article
- Molecular signalling in hepatocellular carcinoma: Role of and crosstalk among WNT/ß-catenin, Sonic Hedgehog, Notch and Dickkopf-1.Canadian journal of gastroenterology & hepatology · 2015Review
- α-Catenin phosphorylation promotes intercellular adhesion through a dual-kinase mechanism.Journal of cell science · 2015Article
- Regulation of Endothelial Adherens Junctions by Tyrosine Phosphorylation.Mediators of inflammation · 2015Review
- Cytoskeletal mechanisms regulating vascular endothelial barrier function in response to acute lung injury.Tissue barriers · 2015Article
- Pre-metazoan origins and evolution of the cadherin adhesome.Biology open · 2014Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Cadherins are the most crucial membrane proteins for the formation of tight and compact cell-cell contacts. Cadherin-based cell-cell adhesions are dynamically established and/or disrupted during various physiological and pathological processes. However, the molecular mechanisms that regulate cell-cell contacts are not fully understood. In this paper, we report a novel functional role of casein kinase 1 (CK1) in the regulation of cell-cell contacts. Firstly, we observed that IC261, a specific inhibitor of CK1, stabilizes cadherin-based cell-cell contacts, whereas the overexpression of CK1 disrupts them. CK1 colocalizes with E-cadherin and phosphorylates the cytoplasmic domain of E-cadherin in vitro and in a cell culture system. We show that the major CK1 phosphorylation site of E-cadherin is serine 846, a highly conserved residue between classical cadherins. Constitutively phosphorylated E-cadherin (S846D) is unable to localize at cell-cell contacts and has decreased adhesive activity. Furthermore, phosphorylated E-cadherin (S846D) has weaker interactions with beta-catenin and is internalized more efficiently than wild-type E-cadherin. These data indicate that CK1 is a novel negative regulator of cadherin-based cell-cell contacts.
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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.