{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Juettner VV"],"funding":["NHLBI NIH HHS","National Institutes of Health"],"pagination":["1725-1742"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6504901"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["218(5)"],"pubmed_abstract":["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 ju"],"journal":["The Journal of cell biology"],"pubmed_title":["VE-PTP stabilizes VE-cadherin junctions and the endothelial barrier via a phosphatase-independent mechanism."],"pmcid":["PMC6504901"],"funding_grant_id":["P01 HL60678","P01 HL060678","R01HL45638","T32 HL07829","R01 HL045638","R01 HL103922","T32 HL007829"],"pubmed_authors":["Khan Y","Komarova Y","Vu VH","Le J","Kruse K","Dan A","Leckband D","Malik AB","Juettner VV"],"additional_accession":[]},"is_claimable":false,"name":"VE-PTP stabilizes VE-cadherin junctions and the endothelial barrier via a phosphatase-independent mechanism.","description":"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 ju","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 May","modification":"2025-04-26T06:41:06.141Z","creation":"2019-11-12T08:04:29Z"},"accession":"S-EPMC6504901","cross_references":{"pubmed":["30948425"],"doi":["10.1083/jcb.201807210"]}}