ArticleThe Journal of cell biology1993
The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 179 papers.
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Who cites it
179 citing papers in PubMed.
- Chemically induced specification of retinal ganglion cells from human embryonic and induced pluripotent stem cells.Stem cells translational medicine · 2014Trial
- Junctions, Transporters, and Interactions of Endothelial Cells: Regulation by Ethanol.International journal of molecular sciences · 2026Review
- Context-dependent interactions among afadin, ZO-1, and actin filaments.Cell structure and function · 2025Article
- ZO-1/Tjp1 and ZO-2/Tjp2 deletion in retinal pigment epithelium causes progressive retinal degeneration.iScience · 2025Article
- Functional landscape of mechanistic diversity in 27 claudin family members at tight junctions.Science advances · 2025Article
- Understanding the Blood-Brain Barrier: From Physiology to Pathology.Advances in experimental medicine and biology · 2025Review
- ZO-1 boosts the in vitro self-renewal of pre-haematopoietic stem cells from OCT4-reprogrammed human hair follicle mesenchymal stem cells through cytoskeleton remodeling.Stem cell research & therapy · 2024Article
- Article
- Tight junction membrane proteins regulate the mechanical resistance of the apical junctional complex.The Journal of cell biology · 2024Article
- Association of connexin36 with adherens junctions at mixed synapses and distinguishing electrophysiological features of those at mossy fiber terminals in rat ventral hippocampus.International journal of physiology, pathophysiology and pharmacology · 2024Article
- Autoregulation of the LIM kinases by their PDZ domain.Nature communications · 2023Article
- Review
- The Human PDZome 2.0: Characterization of a New Resource to Test for PDZ Interactions by Yeast Two-Hybrid.Membranes · 2023Article
- Phase separation of an actin nucleator by junctional microtubules regulates epithelial function.Science advances · 2023Article
- Zonula Occludens Proteins Signaling in Inflammation and Tumorigenesis.International journal of biological sciences · 2023Review
- Serum Zonula Occludens-1 and Claudin-5 Levels in Patients with Insomnia Disorder: A Pilot Study.Nature and science of sleep · 2023Article
- Epithelial polarization in the 3D matrix requires MST3 signaling to regulate ZO-1 position.PloS one · 2023Article
- Involvement of membrane palmitoylated protein 2 (MPP2) in the synaptic molecular complex at the mouse cerebellar glomerulus.Histochemistry and cell biology · 2022Article
- Lmo7 recruits myosin II heavy chain to regulate actomyosin contractility and apical domain size in Xenopus ectoderm.Development (Cambridge, England) · 2022Article
- Primary cilia control endothelial permeability by regulating expression and location of junction proteins.Cardiovascular research · 2022Article
119 more citing papers are in PubMed but not listed here.
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6 authors.
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Abstract
We previously identified a 220-kD constitutive protein of the plasma membrane undercoat which colocalizes at the immunofluorescence microscopic level with cadherins and occurs not only in epithelial M., S. Yonemura, A. Nagafuchi, Sa. Tsukita, and Sh. Tsukita. 1991. J. Cell Biol. 115:1449-1462). To clarify the nature and possible functions of this protein, we cloned its full-length cDNA and sequenced it. Unexpectedly, we found mouse 220-kD protein to be highly homologous to rat protein ZO-1, only a part of which had been already sequenced. This relationship was confirmed by immunoblotting with anti-ZO-1 antibody. As protein ZO-1 was originally identified as a component exclusively underlying tight junctions in epithelial cells, where cadherins are not believed to be localized, we analyzed the distribution of cadherins and the 220-kD protein by ultrathin cryosection immunoelectron microscopy. We found that in non-epithelial cells lacking tight junctions cadherins and the 220-kD protein colocalize, whereas in epithelial cells (e.g., intestinal epithelial cells) bearing well-developed tight junctions cadherins and the 220-kD protein are clearly segregated into adherens and tight junctions, respectively. Interestingly, in epithelial cells such as hepatocytes, which tight junctions are not so well developed, the 220-kD protein is detected not only in the tight junction zone but also at adherens junctions. Furthermore, we show in mouse L cells transfected with cDNAs encoding N-, P-, E-cadherins that cadherins interact directly or indirectly with the 220-kD protein. Possible functions of the 220-kD protein (ZO-1) are discussed with special reference to the molecular mechanism for adherens and tight junction formation.
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