ZO-1 controls endothelial adherens junctions, cell–cell tension, angiogenesis, and barrier formation
Open accessAbstract
Intercellular junctions are crucial for mechanotransduction, but whether tight junctions contribute to the regulation of cell–cell tension and adherens junctions is unknown. Here, we demonstrate that the tight junction protein ZO-1 regulates tension acting on VE-cadherin–based adherens junctions, cell migration, and barrier formation of primary endothelial cells, as well as angiogenesis in vitro and in vivo. ZO-1 depletion led to tight junction disruption, redistribution of active myosin II from junctions to stress fibers, reduced tension on VE-cadherin and loss of junctional mechanotransducers such as vinculin and PAK2, and induced vinculin dissociation from the α-catenin–VE-cadherin complex. Claudin-5 depletion only mimicked ZO-1 effects on barrier formation, whereas the effects on mechanotransducers were rescued by inhibition of ROCK and phenocopied by JAM-A, JACOP, or p114RhoGEF down-regulation. ZO-1 was required for junctional recruitment of JACOP, which, in turn, recruited p114RhoGEF. ZO-1 is thus a central regulator of VE-cadherin–dependent endothelial junctions that orchestrates the spatial actomyosin organization, tuning cell–cell tension, migration, angiogenesis, and barrier formation.
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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 [595]
The Introduction (page unavailable) says ZO-1 interacts with tight-junction proteins, binds F-actin, and has functional redundancy with ZO-2. The Discussion (page unavailable) links ZO-1 to the recruitment of vinculin, but the paper does not establish the claimed connection through all three ZO proteins or describe vinculin-based filaments. (LLM, conf=0.87)
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Size-selective loosening of the blood-brain barrier in claudin-5–deficient mice
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Mechanosensitive systems at the cadherin–F-actin interface
Huveneers, S., & de Rooij, J. (2013) · Journal of Cell Science · doi:10.1242/jcs.109447 · Cited by 222 · see citing works
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- Authors
- Tornavaca, O., Chia, M., Dufton, N., Almagro, L. O., Conway, D. E., Randi, A. M., Schwartz, M. A., Matter, K., & Balda, M. S.
- Affiliations
- University College London (GB)
- Hammersmith Hospital (GB)
- Virginia Commonwealth University (US)
- Yale University (US)
- Corresponding author
- Balda, Maria S.
- ORCID
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2015-03-09
- Volume
- 208
- Issue
- 6
- Pages
- 821-838
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC4362456
- OpenAlex
- W2139671059
- Cited by
- 585
- References
- 3
- Citations by year
- 2026: 42 · 2025: 56 · 2024: 70 · 2023: 51 · 2022: 63 · 2021: 72 · 2020: 66 · 2019: 45 · 2018: 43 · 2017: 45 · 2016: 24 · 2015: 8
- FWCI
- 21.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Spiral (Imperial College London) (submittedVersion, cc-by-nc-sa)
- Funders
- Wellcome Trust (099173/Z/12/Z)
- British Heart Foundation (RG/11/17/29256)
- Biotechnology and Biological Sciences Research Council (BB/J015032/1, BB/H002294/1, BB/L007584/1)
- National Heart, Lung, and Blood Institute (R01HL75092, R01HL075092)
- 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 › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- ZO-1, tight junctions, adherens junctions, mechanotransduction, VE-cadherin, endothelial cells, angiogenesis, myosin II, actomyosin, vinculin, PAK2, JAM-A, claudin-5, cell migration, stress fibers
- MeSH terms
- Cadherin 5, Actomyosin, Animals, Capillary Permeability, Cell Movement, Cells, Cultured, Cytoskeletal Proteins, Cytoskeleton, Humans, Mice, Inbred C57BL, Myosins, Receptors, Cell Surface, Antigens, CD, Cell Adhesion Molecules, Cadherins, Neovascularization, Physiologic, Tight Junctions, Protein Transport, Adherens Junctions, Mechanotransduction, Cellular, Endothelial Cells, Claudin-5, Zonula Occludens-1 Protein
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