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

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

Open access
Itoh, Masahiko, Nagafuchi, Akira, Moroi, Seiji, Tsukita, Shoichiro·1997·The Journal of Cell Biology
DOI 10.1083/jcb.138.1.181PMC PMC2139940
Open this paper in CoChat — free accountOpen PDF

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1083/jcb.138.1.181

Cites

71 of 71 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Related

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
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review