ArticleThe Journal of cell biology1999
Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 452 papers, 1 of them a synthesis that pooled it.
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Who cites it
452 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,122 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
- Targeting claudins in cancer.Nature reviews. Drug discovery · 2026Review
- Quantitative phosphoproteomic approach to unveil potential protein biomarkers linked to high meat quality in ducks.Poultry science · 2026Article
- Protective effects of PRELP protein in a mouse model of pulmonary fibrosis.Respiratory research · 2026Article
- A direct interaction of JAM-C with the tight junction scaffold protein ZO-2.Scientific reports · 2026Article
- ZO-1 shuttles between apical junctional complexes and podosomes by riding ERK activation waves.Nature communications · 2026Article
- CLDN7: Epithelial gatekeeper from physiology to pathology‑roles in cancer and epithelial‑related diseases (Review).International journal of molecular medicine · 2026Review
- Claudin proteins as emerging therapeutic targets for solid tumours.Nature reviews. Cancer · 2026Review
- Cerebrovascular claudin-5 isoform expression correlates with worsened stroke outcomes following thromboembolic stroke.Fluids and barriers of the CNS · 2026Article
- Article
- An epithelial morphogenetic program for maximal urine concentration.Nature communications · 2026Article
- An integrative coding and non-coding SNPs analysis of theFrontiers in oncology · 2026Article
- Dietary Flavonoids as Cross-System Modulators of Hypertension and Intestinal Permeability.Molecules (Basel, Switzerland) · 2025Review
- Exploring claudin proteins: from sequence motifs to their impact on tight junction-mediated signaling pathways.Amino acids · 2025Review
- Claudin Proteins: Their Potential Role in Obesity and Adipose Tissue Signaling, Physiology and Disease.Nutrients · 2025Review
- PEAK1 maintains tight junctions in intestinal epithelial cells and resists colitis by inhibiting autophagy-mediated ZO-1 degradation.Nature communications · 2025Article
- The SARS-CoV-2 envelope PDZ binding motif acts as a virulence factor disrupting host's epithelial cell-cell junctions.Cellular & molecular biology letters · 2025Article
- Deficiency in N-cadherin-Akt3 signaling impairs the blood-brain barrier.Cell reports · 2025Article
- Contact and communication: ZO-2 and the Hippo pathway.The FEBS journal · 2025Article
- Novel genetic determinants contribute to hearing loss in a central European cohort with enlarged vestibular aqueduct.Molecular medicine (Cambridge, Mass.) · 2025Article
392 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ZO-1, ZO-2, and ZO-3, which contain three PDZ domains (PDZ1 to -3), are concentrated at tight junctions (TJs) in epithelial cells. TJ strands are mainly composed of two distinct types of four-transmembrane proteins, occludin, and claudins, between which occludin was reported to directly bind to ZO-1/ZO-2/ZO-3. However, in occludin-deficient intestinal epithelial cells, ZO-1/ZO-2/ZO-3 were still recruited to TJs. We then examined the possible interactions between ZO-1/ZO-2/ZO-3 and claudins. ZO-1, ZO-2, and ZO-3 bound to the COOH-terminal YV sequence of claudin-1 to -8 through their PDZ1 domains in vitro. Then, claudin-1 or -2 was transfected into L fibroblasts, which express ZO-1 but not ZO-2 or ZO-3. Claudin-1 and -2 were concentrated at cell-cell borders in an elaborate network pattern, to which endogenous ZO-1 was recruited. When ZO-2 or ZO-3 were further transfected, both were recruited to the claudin-based networks together with endogenous ZO-1. Detailed analyses showed that ZO-2 and ZO-3 are recruited to the claudin-based networks through PDZ2 (ZO-2 or ZO-3)/PDZ2 (endogenous ZO-1) and PDZ1 (ZO-2 or ZO-3)/COOH-terminal YV (claudins) interactions. In good agreement, PDZ1 and PDZ2 domains of ZO-1/ZO-2/ZO-3 were also recruited to claudin-based TJs, when introduced into cultured epithelial cells. The possible molecular architecture of TJ plaque structures is discussed.
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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.