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

Author

Listed:
  • 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
    Present address: Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.)

  • 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
    Academic Medical Center, University of Amsterdam)

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.

Suggested Citation

  • 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, 2016. "The F-BAR protein pacsin2 inhibits asymmetric VE-cadherin internalization from tensile adherens junctions," Nature Communications, Nature, vol. 7(1), pages 1-18, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12210
    DOI: 10.1038/ncomms12210
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