Related Experiment Video
Updated: Jan 31, 2026
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Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands
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Putting VE-cadherin into JAIL for junction remodeling
1Institute of Anatomy and Vascular Biology, Westfälische Wilhelms-Universität Münster, Münster Germany.
Journal of Cell Science
|January 5, 2019
Summary
Junction-associated intermittent lamellipodia (JAIL) drive VE-cadherin dynamics at endothelial cell junctions. These actin-driven protrusions enable subcellular regulation of cell adhesion, crucial for tissue repair and integrity.
Area of Science:
- Cell Biology
- Biophysics
- Molecular Biology
Background:
- Endothelial cell junction dynamics are vital for tissue integrity, repair, and regeneration.
- The VE-cadherin-catenin complex is central to endothelial cell adhesion.
- Actin cytoskeleton remodeling influences cell junction regulation.
Purpose of the Study:
- To identify the driving force behind VE-cadherin dynamics at endothelial cell junctions.
- To characterize the role of actin-driven protrusions in cell adhesion.
- To elucidate the autoregulatory mechanism of cell contact dynamics.
Main Methods:
- Microscopy to observe actin-driven protrusions.
- Analysis of VE-cadherin dynamics.
- Investigation of Arp2/3 complex involvement.
Main Results:
- Identified junction-associated intermittent lamellipodia (JAIL) as key drivers of VE-cadherin dynamics.
- Demonstrated that JAIL directly induce new VE-cadherin-mediated adhesion sites.
- Revealed a direct interdependence between local VE-cadherin concentration and JAIL formation, enabling autoregulation.
Conclusions:
- JAIL provide a mechanism for subcellular regulation of endothelial cell adhesion.
- This autoregulatory mechanism is critical for maintaining monolayer integrity during wound healing, angiogenesis, and inflammation.
- JAIL contribute significantly to the dynamic regulation of endothelial cell junctions.
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