ArticleThe Journal of cell biology1991
A 220-kD undercoat-constitutive protein: its specific localization at cadherin-based cell-cell adhesion sites.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.
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Who cites it
92 citing papers in PubMed, 235 citations in OpenAlex.
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- Angulin-1 seals tricellular contacts independently of tricellulin and claudins.The Journal of cell biology · 2021Article
- A microtubule-LUZP1 association around tight junction promotes epithelial cell apical constriction.The EMBO journal · 2021Article
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- The extracellular domain of angulin-1 and palmitoylation of its cytoplasmic region are required for angulin-1 assembly at tricellular contacts.The Journal of biological chemistry · 2020Article
- Claudins and JAM-A coordinately regulate tight junction formation and epithelial polarity.The Journal of cell biology · 2019Article
- Vinculin is critical for the robustness of the epithelial cell sheet paracellular barrier for ions.Life science alliance · 2019Article
- Homeostatic pruning and activity of epidermal nerves are dysregulated in barrier-impaired skin during chronic itch development.Scientific reports · 2019Article
- Pyk2-dependent phosphorylation of LSR enhances localization of LSR and tricellulin at tricellular tight junctions.PloS one · 2019Article
- Changes in cell junctions induced by inhibition of epidermal growth factor receptor in oral squamous cell carcinoma cells.Experimental and therapeutic medicine · 2017Article
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- Epidermal cell turnover across tight junctions based on Kelvin's tetrakaidecahedron cell shape.eLife · 2016Article
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32 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently we developed an isolation procedure for the cell-to-cell adherens junctions (AJ; cadherin-based junctions) from rat liver (Tsukita, Sh. and Sa. Tsukita. 1989. J. Cell Biol. 108:31-41). In this study, using the isolated AJ, we have obtained two mAbs specific to the 220-kD undercoat-constitutive protein. Immunofluorescence and immunoelectron microscopy with these mAbs showed that this 220-kD protein was highly concentrated at the undercoat of cell-to-cell AJ in various types of tissues and that this protein was located in the immediate vicinity of the plasma membrane in the undercoat of AJ. In the cells lacking typical cell-to-cell AJ, such as fibroblasts, the 220-kD protein was immunofluorescently shown to be coconcentrated with cadherin molecules at cell-cell adhesion sites. These localization analyses appeared to indicate the possible direct or indirect association of the 220-kD protein with cadherin molecules. Furthermore, it was revealed that the 220-kD protein and alpha-spectrin were coimmunoprecipitated with the above mAbs in both the isolated AJ and the brain. The affinity-purified 220-kD protein molecule looked like a spherical particle, and its binding site on the spectrin molecule was shown to be in the position approximately 10-20 nm from the midpoint of spectrin tetramer by low-angle rotary-shadowing electron microscopy. Taking all these results together with biochemical and immunological comparisons, we are persuaded to speculate that the 220-kD protein is a novel member of the ankyrin family. However, the possibility cannot be excluded that the 220-kD protein is an isoform of beta-spectrin. The possible roles of this 220-kD protein in the association of cadherin molecules with the spectrin-based membrane skeletons at the cadherin-based cell-cell adhesion sites are discussed.
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