2016-07-15
The F-BAR protein pacsin2 inhibits asymmetric VE-cadherin internalization from tensile adherens junctions
Publication
Publication
Nature Communications , Volume 7
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.
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| doi.org/10.1038/ncomms12210, hdl.handle.net/1765/97642 | |
| Nature Communications | |
| Organisation | Department of Pediatrics |
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Dorland, Y.L. (Yvonne L.), Malinova, T.S. (Tsveta S.), Van Stalborch, A.-M.D. (Anne-Marieke D.), Grieve, A.G. (Adam G.), van Geemen, D., Jansen, N.S. (Nicolette S.), … Huveneers, H. (2016). The F-BAR protein pacsin2 inhibits asymmetric VE-cadherin internalization from tensile adherens junctions. Nature Communications, 7. doi:10.1038/ncomms12210 |
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