ArticleThe Journal of cell biology1989
A new 400-kD protein from isolated adherens junctions: its localization at the undercoat of adherens junctions and at microfilament bundles such as stress fibers and circumferential bundles.
Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Synaptopodin couples epithelial contractility to α-actinin-4-dependent junction maturation.The Journal of cell biology · 2015Article
- Ezrin promotes morphogenesis of apical microvilli and basal infoldings in retinal pigment epithelium.The Journal of cell biology · 1999Article
- Swelling-induced, CFTR-independent ATP release from a human epithelial cell line: lack of correlation with volume-sensitive cl(-) channels.The Journal of general physiology · 1999Article
- Afadin: A novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junction.The Journal of cell biology · 1997Article
- Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway.The Journal of cell biology · 1996Article
- Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions.The Journal of cell biology · 1994Article
- ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons.The Journal of cell biology · 1994Article
- Interactions of tensin with actin and identification of its three distinct actin-binding domains.The Journal of cell biology · 1994Article
- Focal adhesion as a signal transduction organelle.Cancer metastasis reviews · 1994Review
- Occludin: a novel integral membrane protein localizing at tight junctions.The Journal of cell biology · 1993Article
- 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.The Journal of cell biology · 1993Article
- Expression of chicken vinculin complements the adhesion-defective phenotype of a mutant mouse F9 embryonal carcinoma cell.The Journal of cell biology · 1993Article
- Restricted tissue distribution of a 37-kD possible adherens junction protein.The Journal of cell biology · 1992Article
- A 220-kD undercoat-constitutive protein: its specific localization at cadherin-based cell-cell adhesion sites.The Journal of cell biology · 1991Article
- Radixin is a novel member of the band 4.1 family.The Journal of cell biology · 1991Article
- Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated.The Journal of cell biology · 1991Article
- Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- Radixin, a barbed end-capping actin-modulating protein, is concentrated at the cleavage furrow during cytokinesis.The Journal of cell biology · 1991Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the previous study, we succeeded in isolating the cell-to-cell adherens junctions from rat liver (Tsukita, S., and S. Tsukita. 1989. J. Cell Biol. 108:31-41.). In this study, we have obtained mAbs specific to the 400-kD protein, which was identified as one of the major constituents of the undercoat of isolated adherens junctions. Immune blot analyses showed that this protein occurs in various types of tissues. Immunofluorescence microscopy and immune electron microscopy have revealed that this protein is distributed not only at the undercoat of adherens junctions but also along actin bundles associated with the junction in nonmuscle cells: stress fibers in cultured fibroblasts and circumferential bundles in epithelial cells. The partially purified protein molecule looks like a slender rod approximately 400 nm in length. By virtue of its molecular shape, we have named this protein 'tenuin' (from Latin 'tenuis', thin or slender).
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