Cited by 677Cell Adhesion Molecules ResearchSkin and Cellular Biology ResearchBarrier Structure and Function Studies

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Involvement of ZO-1 in Cadherin-based Cell Adhesion through Its Direct Binding to α Catenin and Actin Filaments

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Itoh, Masahiko, Nagafuchi, Akira, Moroi, Seiji, Tsukita, Shoichiro·1997·The Journal of Cell Biology

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Abstract

ZO-1, a 220-kD peripheral membrane protein consisting of an amino-terminal half discs large (dlg)-like domain and a carboxyl-terminal half domain, is concentrated at the cadherin-based cell adhesion sites in non-epithelial cells. We introduced cDNAs encoding the full-length ZO-1, its amino-terminal half (N-ZO-1), and carboxyl-terminal half (C-ZO-1) into mouse L fibroblasts expressing exogenous E-cadherin (EL cells). The full-length ZO-1 as well as N-ZO-1 were concentrated at cadherin-based cell–cell adhesion sites. In good agreement with these observations, N-ZO-1 was specifically coimmunoprecipitated from EL transfectants expressing N-ZO-1 (NZ-EL cells) with the E-cadherin/α, β catenin complex. In contrast, C-ZO-1 was localized along actin stress fibers. To examine the molecular basis of the behavior of these truncated ZO-1 molecules, N-ZO-1 and C-ZO-1 were produced in insect Sf9 cells by recombinant baculovirus infection, and their direct binding ability to the cadherin/catenin complex and the actin-based cytoskeleton, respectively, were examined in vitro. Recombinant N-ZO-1 bound directly to the glutathione-S-transferase fusion protein with α catenin, but not to that with β catenin or the cytoplasmic domain of E-cadherin. The dissociation constant between N-ZO-1 and α catenin was ∼0.5 nM. On the other hand, recombinant C-ZO-1 was specifically cosedimented with actin filaments in vitro with a dissociation constant of ∼10 nM. Finally, we compared the cadherin-based cell adhesion activity of NZ-EL cells with that of parent EL cells. Cell aggregation assay revealed no significant differences among these cells, but the cadherin-dependent intercellular motility, i.e., the cell movement in a confluent monolayer, was significantly suppressed in NZ-EL cells. We conclude that in nonepithelial cells, ZO-1 works as a cross-linker between cadherin/catenin complex and the actin-based cytoskeleton through direct interaction with α catenin and actin filaments at its amino- and carboxyl-terminal halves, respectively, and that ZO-1 is a functional component in the cadherin-based cell adhesion system.

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Authors: Itoh, M., Nagafuchi, A., Moroi, S., & Tsukita, S.
Affiliations: Kyoto University (JP)
*Department of Cell Biology, Faculty of Medicine, Kyoto University, Kyoto 606, Japan; and ‡Department of Urology, Faculty of Medicine, Kyoto University, Kyoto 606, Japan
Venue: The Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 1997-07-14
Volume: 138
Issue: 1
Pages: 181-192
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.138.1.181
PMC: PMC2139940
OpenAlex: W2102090879
Cited by: 677
References: 71
Citations by year: 2026: 10 · 2025: 13 · 2024: 15 · 2023: 14 · 2022: 20 · 2021: 18 · 2020: 21 · 2019: 17 · 2018: 21 · 2017: 21 · 2016: 13 · 2015: 9 · 2014: 15 · 2013: 30 · 2012: 22
FWCI: 14.93
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: The Journal of Cell Biology (publishedVersion)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
Keywords: ZO-1, E-cadherin, alpha-catenin, F-actin, cell-cell adhesion, stress fibers, cell aggregation, protein-protein interaction, L fibroblasts
MeSH terms: Actins, Animals, Cell Adhesion, Cell Line, Cytoskeletal Proteins, L Cells, Membrane Proteins, Phosphoproteins, Recombinant Fusion Proteins, Trans-Activators, Cadherins, Spodoptera, beta Catenin, alpha Catenin, Mice, Rats, Zonula Occludens-1 Protein

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Involvement of ZO-1 in Cadherin-based Cell Adhesion through Its Direct Binding to α Catenin and Actin Filaments

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