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Cited by 544Barrier Structure and Function StudiesCell Adhesion Molecules ResearchIon Transport and Channel Regulation

Architecture of tight junctions and principles of molecular composition

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Van Itallie, Christina M., Anderson, James M.·2014·Seminars in Cell & Developmental Biology
DOI 10.1016/j.semcdb.2014.08.011PMC PMC4254347
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Abstract

The tight junction creates an intercellular barrier limiting paracellular movement of solutes and material across epithelia. Currently many proteins have been identified as components of the tight junction and understanding their architectural organization and interactions is critical to understanding the biology of the barrier. In general the architecture can be conceptualized into compartments with the transmembrane barrier proteins (claudins, occludin, JAM-A, etc.), linked to peripheral scaffolding proteins (such as ZO-1, afadin, MAGI1, etc.) which are in turned linked to actin and microtubules through numerous linkers (cingulin, myosins, protein 4.1, etc.). Within this complex network are associated many signaling proteins that affect the barrier and broader cell functions. The PDZ domain is a commonly used motif to specifically link individual junction protein pairs. Here we review some of the key proteins defining the tight junction and general themes of their organization with the perspective that much will be learned about function by characterizing the detailed architecture and subcompartments within the junction.

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  • Tight junction proteins are connected to actin and vinculin-based cytoskeletal filaments via scaffolding proteins ZO-1, ZO-2, and ZO-3.

    “TJ proteins are connected to the actin and vinculin-based cytoskeletal filaments via scaffolding proteins of the membrane-associated guanylate kinase family ZO-1, -2, and -3 (595, 608) (FIGURE 2) .”

    From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [608]

    Sections 1.4.1 and 2 say that ZO-1, ZO-2, and ZO-3 bind tight-junction transmembrane proteins and actin, linking the junction to the cytoskeleton. Section 2 also identifies vinculin as a ZO-interacting actin-binding protein, but does not describe vinculin-based cytoskeletal filaments. Page numbers are not provided in our copy. (LLM, conf=0.88)

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Authors
Van Itallie, C. M., & Anderson, J. M.
Affiliations
National Institutes of Health (US)
ORCID
Anderson, James M.
Venue
Seminars in Cell & Developmental Biology
Publisher
Elsevier BV
Published
2014-12
Volume
36
Pages
157-165
ISSN
1084-9521 (ISSN-L)
DOI
10.1016/j.semcdb.2014.08.011
PMC
PMC4254347
OpenAlex
W2056700437
Cited by
544
References
2
Citations by year
2026: 29 · 2025: 33 · 2024: 44 · 2023: 45 · 2022: 41 · 2021: 51 · 2020: 61 · 2019: 61 · 2018: 37 · 2017: 58 · 2016: 38 · 2015: 42 · 2014: 3 · 2013: 1
FWCI
3.80
Type
journal article
Language
en
Open access
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Seminars in Cell and Developmental Biology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
Division of Intramural Research (CMV) and the Office of the Director (JMA), National Institutes of Health, USA
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
tight junctions, paracellular barrier, epithelial barrier function, claudins, occludin, JAM-A, ZO-1, afadin, MAGI1, cingulin, myosin, protein 4.1, actin, microtubules, PDZ domain, scaffold proteins, signaling proteins
MeSH terms
Biological Transport, Cytoskeletal Proteins, Humans, Membrane Proteins, Signal Transduction, Protein Structure, Tertiary, Tight Junctions, Junctional Adhesion Molecules

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