The motor protein myosin-X transports VE-cadherin along filopodia to allow the formation of early endothelial cell-cell contacts.

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 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.

journal_name

Mol Cell Biol

authors

Almagro S,Durmort C,Chervin-Pétinot A,Heyraud S,Dubois M,Lambert O,Maillefaud C,Hewat E,Schaal JP,Huber P,Gulino-Debrac D

doi

10.1128/MCB.01226-09

subject

Has Abstract

pub_date

2010-04-01 00:00:00

pages

1703-17

issue

7

eissn

0270-7306

issn

1098-5549

pii

MCB.01226-09

journal_volume

30

pub_type

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