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Cited by 1,432Barrier Structure and Function StudiesCell Adhesion Molecules ResearchIon Transport and Channel Regulation

The Tight Junction Protein ZO-1 Establishes a Link between the Transmembrane Protein Occludin and the Actin Cytoskeleton

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Fanning, Alan S., Jameson, Brian J., Jesaitis, Lynne A., Anderson, James Melvin·1998·Journal of Biological Chemistry
DOI 10.1074/jbc.273.45.29745
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Abstract

The tight junction protein ZO-1 belongs to a family of multidomain proteins known as the membrane-associated guanylate kinase homologs (MAGUKs). ZO-1 has been demonstrated to interact with the transmembrane protein occludin, a second tight junction-specific MAGUK, ZO-2, and F-actin, although the nature and functional significance of these interactions is poorly understood. To further elucidate the role of ZO-1 within the epithelial tight junction, we have introduced epitope-tagged fragments of ZO-1 into cultured MDCK cells and identified domains critical for the interaction with ZO-2, occludin, and F-actin. A combination of in vitro and in vivo binding assays indicate that both ZO-2 and occludin interact with specific domains within the N-terminal (MAGUK-like) half of ZO-1, whereas the unique proline-rich C-terminal half of ZO-1 cosediments with F-actin. Consistent with these observations, we found that a construct encoding the N-terminal half of ZO-1 is specifically associated with tight junctions, whereas the unique C-terminal half of ZO-1 is distributed over the entire lateral surface of the plasma membrane and other actin-rich structures. In addition, we have identified a 244-amino acid domain within the N-terminal half of ZO-1, which is required for the stable incorporation of ZO-1 into the junctional complex of polarized MDCK cells. These observations suggest that one functional role of ZO-1 is to organize components of the tight junction and link them to the cortical actin cytoskeleton.

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Crossref · 10.1074/jbc.273.45.29745

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  • ZO-1 interacts with the C-terminus of all claudins and occludin.

    “However, such a model does not explain why specifically claudin-1, but not claudin-4 or occludin, is lacking from the granular layer whereas ZO-1 interacts with the C-terminus of all claudins and occludin (Fanning et al, 1998;Itoh et al, 1999).”

    From E‐cadherin is essential for in vivo epidermal barrier function by regulating tight junctions (2005) · cites this paper as Fanning et al, 1998

    The Results (page not provided) report that ZO-1 binds a fusion protein containing the C-terminal region of occludin. The paper does not report interactions with claudins, so it does not support the claim about all claudins. (LLM, conf=0.90)

    Experimental — accuracy not yet measured

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Cites

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Research works printed but not linked: 24

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Cited by

Sorted by citations

Authors
Fanning, A. S., Jameson, B. J., Jesaitis, L. A., & Anderson, J. M.
Affiliations
  • Yale University (US)
  • University of California, Berkeley (US)
Corresponding author
Fanning, Alan S.
ORCID
Anderson, James Melvin
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-11
Volume
273
Issue
45
Pages
29745-29753
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.273.45.29745
OpenAlex
W2040645020
Cited by
1,432
References
2
Citations by year
2026: 40 · 2025: 49 · 2024: 53 · 2023: 45 · 2022: 74 · 2021: 68 · 2020: 66 · 2019: 51 · 2018: 49 · 2017: 56 · 2016: 51 · 2015: 47 · 2014: 58 · 2013: 45 · 2012: 54
FWCI
29.02
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5p01ca066263-05)
  • National Cancer Institute (CA66 263)
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK45134, R01DK045134, DK-34989, P30DK034989)
Topics
  • Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
Keywords
ZO-1, tight junctions, occludin, ZO-2, MAGUK proteins, actin cytoskeleton, F-actin binding, MDCK cells, protein-protein interaction, plasma membrane organization
MeSH terms
Actins, Animals, Base Sequence, Binding Sites, Cell Line, Cytoskeleton, Dogs, Membrane Proteins, Phosphoproteins, DNA Primers, Occludin, Zonula Occludens-1 Protein

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