The Motor Protein Myosin-X Transports VE-Cadherin along Filopodia To Allow the Formation of Early Endothelial Cell-Cell Contacts: MYOSIN-X TRANSPORT OF VE-CADHERIN ALONG FILOPODIA

Abstract : Vascular endothelium (VE), the monolayer of endothelial cells that lines the vascular tree, undergoes damage at the basis of some vascular diseases. Its integrity is maintained by VE-cadherin, an adhesive receptor localized at cell-cell junctions. Here, we show that VE-cadherin is also located at the tip and along filopodia in sparse or subconfluent endothelial cells. We observed that VE-cadherin navigates along intrafilopodial actin filaments. We found that the actin motor protein myosin-X is colocalized and moves synchronously with filopodial VE-cadherin. Immunoprecipitation and pulldown assays confirmed that myosin-X is directly associated with the VE-cadherin complex. Furthermore, expression of a dominant-negative mutant of myosin-X revealed that myosin-X is required for VE-cadherin export to cell edges and filopodia. These features indicate that myosin-X establishes a link between the actin cytoskeleton and VE-cadherin, thereby allowing VEcadherin transportation along intrafilopodial actin cables. In conclusion, we propose that VE-cadherin trafficking along filopodia using myosin-X motor protein is a prerequisite for cell-cell junction formation. This mechanism may have functional consequences for endothelium repair in pathological settings.
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Molecular and Cellular Biology, American Society for Microbiology, 2010, Apr. 2010, page 1703-1717. 〈10.1128/MCB.01226-09〉
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Sébastien Almagro, Claire Durmort, Adeline Chervin-Pétinot, Stéphanie Heyraud, Mathilde Dubois, et al.. The Motor Protein Myosin-X Transports VE-Cadherin along Filopodia To Allow the Formation of Early Endothelial Cell-Cell Contacts: MYOSIN-X TRANSPORT OF VE-CADHERIN ALONG FILOPODIA. Molecular and Cellular Biology, American Society for Microbiology, 2010, Apr. 2010, page 1703-1717. 〈10.1128/MCB.01226-09〉. 〈inserm-00462307〉

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