ArticleMolecular biology of the cell2002
Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 158 citations in OpenAlex.
- The ageing holobiont: crosstalk between telomere dynamics, oxidative stress and the gut microbiome.Biological reviews of the Cambridge Philosophical Society · 2026Review
- Sequence and expression analysis of potential spermatogenesis-specific gene cognates in the Caribbean fruit fly, Anastrepha suspensa.Insect science · 2026Article
- Sequence and expression analysis of the spermatogenesis-specific gene cognates, wampa and Prosα6T, in Drosophila suzukii.Genetica · 2023Article
- Glaesserella parasuis serotype 5 breaches the porcine respiratory epithelial barrier by inducing autophagy and blocking the cell membrane Claudin-1 replenishment.PLoS pathogens · 2022Article
- Serine 408 phosphorylation is a molecular switch that regulates structure and function of the occludin α-helical bundle.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Epithelial Cell Leak Pathway.International journal of molecular sciences · 2021Review
- Epithelial barrier dysfunction and cell migration induction via JNK/cofilin/actin by angubindin-1.Tissue barriers · 2020Article
- Oral Mucosal Epithelial Cells.Frontiers in immunology · 2019Review
- Article
- VCAM-1 induces signals that stimulate ZO-1 serine phosphorylation and reduces ZO-1 localization at lung endothelial cell junctions.Journal of leukocyte biology · 2018Article
- Phosphorylation of tight junction transmembrane proteins: Many sites, much to do.Tissue barriers · 2018Review
- Maresin 1 Maintains the Permeability of Lung Epithelial Cells In Vitro and In Vivo.Inflammation · 2016Article
- On Chip Bioelectric Impedance Spectroscopy Reveals the Effect of P-Glycoprotein Efflux Pumps on the Paracellular Impedance of Tight Junctions at the Blood-Brain Barrier.IEEE transactions on nanobioscience · 2016Article
- A phosphotyrosine switch regulates organic cation transporters.Nature communications · 2016Article
- Dynamic interplay between adhesion surfaces in carcinomas: Cell-cell and cell-matrix crosstalk.World journal of biological chemistry · 2016Review
- c-Jun N-terminal kinase inhibitor SP600125 enhances barrier function and elongation of human pancreatic cancer cell line HPAC in a Ca-switch model.Histochemistry and cell biology · 2015Article
- Proteomic analysis of proteins surrounding occludin and claudin-4 reveals their proximity to signaling and trafficking networks.PloS one · 2015Article
- Differential effects of c-Src and c-Yes on the endocytic vesicle-mediated trafficking events at the Sertoli cell blood-testis barrier: an in vitro study.American journal of physiology. Endocrinology and metabolism · 2014Article
- Colon cancer cells escape 5FU chemotherapy-induced cell death by entering stemness and quiescence associated with the c-Yes/YAP axis.Clinical cancer research : an official journal of the American Association for Cancer Research · 2014Article
- "You Shall Not Pass"-tight junctions of the blood brain barrier.Frontiers in neuroscience · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Occludin is an integral membrane protein that is tyrosine phosphorylated when localized at tight junctions. When Ca(2+) was depleted from the culture medium, occludin tyrosine phosphorylation was diminished from Madin-Darby canine kidney epithelial cells in 2 min. This dephosphorylation was correlated with a significant reduction in transepithelial electrical resistance (TER), indicating a global loss of the tight junction barrier function. Reconstitution of Ca(2+) resulted in a robust tyrosine rephosphorylation of occludin that was temporally associated with an increase in TER. Moreover, we demonstrate in this study that occludin was colocalized with the nonreceptor tyrosine kinase c-Yes at cell junction areas and formed an immunoprecipitable complex with c-Yes in vivo. This complex dissociated when the cells were incubated in medium without Ca(2+) or treated with a c-Yes inhibitor, CGP77675. In the presence of CGP77675 after Ca(2+) repletion, occludin tyrosine phosphorylation was completely abolished and both tight junction formation and the increase of the TER were inhibited. Our study thus provides strong evidence that occludin tyrosine phosphorylation is tightly linked to tight junction formation in epithelial cells, and that the nonreceptor tyrosine kinase c-Yes is involved in the regulation of this process.
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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.