The F-BAR protein pacsin2 inhibits asymmetric VE-cadherin internalization from tensile adherens junctions

Yvonne L. Dorland, Tsveta S. Malinova, Anne-Marieke D. van Stalborch, Adam G. Grieve, Daphne van Geemen, Nicolette S. Jansen, Bart-Jan de Kreuk, Kalim Nawaz, Jeroen Kole, Dirk Geerts, René J. P. Musters, Johan de Rooij, Peter L. Hordijk and Stephan Huveneers ()
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Yvonne L. Dorland: Sanquin Research and Landsteiner Laboratory, University of Amsterdam
Tsveta S. Malinova: Academic Medical Center, University of Amsterdam
Anne-Marieke D. van Stalborch: Sanquin Research and Landsteiner Laboratory, University of Amsterdam
Adam G. Grieve: Hubrecht Institute and University Medical Center Utrecht
Daphne van Geemen: Sanquin Research and Landsteiner Laboratory, University of Amsterdam
Nicolette S. Jansen: Sanquin Research and Landsteiner Laboratory, University of Amsterdam
Bart-Jan de Kreuk: University of California
Kalim Nawaz: Sanquin Research and Landsteiner Laboratory, University of Amsterdam
Jeroen Kole: VU University Medical Center
Dirk Geerts: Erasmus University Medical Center
René J. P. Musters: VU University Medical Center
Johan de Rooij: Center for Molecular Medicine, University Medical Center Utrecht
Peter L. Hordijk: VU University Medical Center
Stephan Huveneers: Sanquin Research and Landsteiner Laboratory, University of Amsterdam

Nature Communications, 2016, vol. 7, issue 1, 1-18

Abstract: Abstract Vascular homoeostasis, development and disease critically depend on the regulation of endothelial cell–cell junctions. Here we uncover a new role for the F-BAR protein pacsin2 in the control of VE-cadherin-based endothelial adhesion. Pacsin2 concentrates at focal adherens junctions (FAJs) that are experiencing unbalanced actomyosin-based pulling. FAJs move in response to differences in local cytoskeletal geometry and pacsin2 is recruited consistently to the trailing end of fast-moving FAJs via a mechanism that requires an intact F-BAR domain. Photoconversion, photobleaching, immunofluorescence and super-resolution microscopy reveal polarized dynamics, and organization of junctional proteins between the front of FAJs and their trailing ends. Interestingly, pacsin2 recruitment inhibits internalization of the VE-cadherin complex from FAJ trailing ends and is important for endothelial monolayer integrity. Together, these findings reveal a novel junction protective mechanism during polarized trafficking of VE-cadherin, which supports barrier maintenance within dynamic endothelial tissue.

Date: 2016
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DOI: 10.1038/ncomms12210

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