biostudies-literatureJuettner VVNHLBI NIH HHSNational Institutes of Health1725-1742https://www.ebi.ac.uk/biostudies/studies/S-EPMC6504901biostudies-literatureUnknown218(5)Vascular endothelial (VE) protein tyrosine phosphatase (PTP) is an endothelial-specific phosphatase that stabilizes VE-cadherin junctions. Although studies have focused on the role of VE-PTP in dephosphorylating VE-cadherin in the activated endothelium, little is known of VE-PTP's role in the quiescent endothelial monolayer. Here, we used the photoconvertible fluorescent protein VE-cadherin-Dendra2 to monitor VE-cadherin dynamics at adherens junctions (AJs) in confluent endothelial monolayers. We discovered that VE-PTP stabilizes VE-cadherin junctions by reducing the rate of VE-cadherin internalization independently of its phosphatase activity. VE-PTP serves as an adaptor protein that through binding and inhibiting the RhoGEF GEF-H1 modulates RhoA activity and tension across VE-cadherin juThe Journal of cell biologyVE-PTP stabilizes VE-cadherin junctions and the endothelial barrier via a phosphatase-independent mechanism.PMC6504901P01 HL60678P01 HL060678R01HL45638T32 HL07829R01 HL045638R01 HL103922T32 HL007829Khan YKomarova YVu VHLe JKruse KDan ALeckband DMalik ABJuettner VVfalseVE-PTP stabilizes VE-cadherin junctions and the endothelial barrier via a phosphatase-independent mechanism.Vascular endothelial (VE) protein tyrosine phosphatase (PTP) is an endothelial-specific phosphatase that stabilizes VE-cadherin junctions. Although studies have focused on the role of VE-PTP in dephosphorylating VE-cadherin in the activated endothelium, little is known of VE-PTP's role in the quiescent endothelial monolayer. Here, we used the photoconvertible fluorescent protein VE-cadherin-Dendra2 to monitor VE-cadherin dynamics at adherens junctions (AJs) in confluent endothelial monolayers. We discovered that VE-PTP stabilizes VE-cadherin junctions by reducing the rate of VE-cadherin internalization independently of its phosphatase activity. VE-PTP serves as an adaptor protein that through binding and inhibiting the RhoGEF GEF-H1 modulates RhoA activity and tension across VE-cadherin ju2019-01-01T00:00:00Z2019 May2025-04-26T06:41:06.141Z2019-11-12T08:04:29ZS-EPMC65049013094842510.1083/jcb.201807210