Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 30, Issue 7, Pages 1703-1717Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.01226-09
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Funding
- Ligue Regionale de Savoie Contre le Cancer
- Agence Nationale de la Recherche (ANR)
- Association pour la Recherche sur le Cancer [4447, 3775]
- Commissariat a l'Energie Atomique (CEA)
- Agence Nationale de Recherche
- CEA
- Association de Recherche sur la Polyarthrite
- Agence Nationale de Recherche [ANR-06-PCV]
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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 VE-cadherin 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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