ArticleThe Journal of biological chemistry2010
Involvement of the interaction of afadin with ZO-1 in the formation of tight junctions in Madin-Darby canine kidney cells.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers, 1 of them a synthesis that pooled it.
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Who cites it
81 citing papers in PubMed, 1 synthesis or guideline pooled it, 128 citations in OpenAlex.
- Adherens, tight, and gap junctions in ependymal cells: A systematic review of their contribution to CSF-brain barrier.Frontiers in neurology · 2023Pooled it
- Tight junction structure, assembly and (dys)function.Nature reviews. Molecular cell biology · 2026Review
- Hydroxycarboxylic acid receptor 2 (GPR109A) and retinopathies: pathways and prospects.Frontiers in medicine · 2026Review
- Context-dependent interactions among afadin, ZO-1, and actin filaments.Cell structure and function · 2025Article
- A key role of Canoe's intrinsically disordered region in linking cell junctions to the cytoskeleton.The Journal of cell biology · 2025Article
- Interactive Role of the DHPR βBiomolecules · 2025Article
- α-catenin phosphorylation is actomyosin-sensitive and required for epithelial barrier functions through Afadin.bioRxiv : the preprint server for biology · 2025Article
- Proximity proteomics provides a new resource for exploring the function of Afadin and the complexity of cell-cell adherens junctions.Biology open · 2025Article
- Proximity proteomics provides a new resource for exploring the function of Afadin and the complexity of cell-cell adherens junctions.bioRxiv : the preprint server for biology · 2024Article
- Japanese encephalitis virus-induced DNA methylation contributes to blood-brain barrier permeability by modulating tight junction protein expression.Journal of neuroinflammation · 2024Article
- Mechanosensitive recruitment of Vinculin maintains junction integrity and barrier function at epithelial tricellular junctions.Current biology : CB · 2024Article
- Tight junction membrane proteins regulate the mechanical resistance of the apical junctional complex.The Journal of cell biology · 2024Article
- Nectins and Nectin-like molecules drive vascular development and barrier function.Angiogenesis · 2023Review
- Polychaetoid/ZO-1 strengthens cell junctions under tension while localizing differently than core adherens junction proteins.Molecular biology of the cell · 2023Article
- Exploring the evolution and function of Canoe’s intrinsically disordered region in linking cell-cell junctions to the cytoskeleton during embryonic morphogenesis.bioRxiv : the preprint server for biology · 2023Article
- Polychaetoid/ZO-1 strengthens cell junctions under tension while localizing differently than core adherens junction proteins.bioRxiv : the preprint server for biology · 2023Article
- Article
- Transgenic animal models to explore and modulate the blood brain and blood retinal barriers of the CNS.Fluids and barriers of the CNS · 2022Review
- Epithelial integrity, junctional complexes, and biomarkers associated with intestinal functions.Tissue barriers · 2022Review
- IRF6 Regulates the Delivery of E-Cadherin to the Plasma Membrane.The Journal of investigative dermatology · 2022Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tight junctions (TJs) and adherens junctions (AJs) are major junctional apparatuses in epithelial cells. Claudins and junctional adhesion molecules (JAMs) are major cell adhesion molecules (CAMs) at TJs, whereas cadherins and nectins are major CAMs at AJs. Claudins and JAMs are associated with ZO proteins, whereas cadherins are associated with beta- and alpha-catenins, and nectins are associated with afadin. We previously showed that nectins first form cell-cell adhesions where the cadherin-catenin complex is recruited to form AJs, followed by the recruitment of the JAM-ZO and claudin-ZO complexes to the apical side of AJs to form TJs. It is not fully understood how TJ components are recruited to the apical side of AJs. We studied the roles of afadin and ZO-1 in the formation of TJs in Madin-Darby canine kidney (MDCK) cells. Before the formation of TJs, ZO-1 interacted with afadin through the two proline-rich regions of afadin and the SH3 domain of ZO-1. During and after the formation of TJs, ZO-1 dissociated from afadin and associated with JAM-A. Knockdown of afadin impaired the formation of both AJs and TJs in MDCK cells, whereas knockdown of ZO-1 impaired the formation of TJs, but not AJs. Re-expression of full-length afadin restored the formation of both AJs and TJs in afadin-knockdown MDCK cells, whereas re-expression of afadin-DeltaPR1-2, which is incapable of binding to ZO-1, restored the formation of AJs, but not TJs. These results indicate that the transient interaction of afadin with ZO-1 is necessary for the formation of TJs in MDCK cells.
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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.