Impaired endothelial barrier function results in a persistent increase in endothelial permeability and vascular leakage. Repair of a dysfunctional endothelial barrier requires controlled restoration of adherens junctions, comprised of Vascular-Endothelial (VE)-cadherin and associated β-, γ-, α- and p120-catenins. Little is known about the mechanisms by which the recovery of VE-cadherin-mediated cell-cell junctions is regulated. Here, using the inflammatory mediator thrombin, we demonstrate an important role for the tyrosine phosphatase SHP2 in mediating the recovery of the VE-cadherin-controlled endothelial barrier. Using SHP2 substrate-trapping mutants and an in vitro phosphatase activity assay, we validate β-catenin as a bona fide SHP2 substrate. SHP2 silencing and SHP2 inhibition both resulted in a delayed recovery of endothelial barrier function after thrombin stimulation. Moreover, upon thrombin challenge, we found a prolonged elevation in tyrosine phosphorylation levels of VE-cadherin-associated β-catenin in SHP2-depleted cells. No disassembly of the VE-cadherin complex was observed throughout the thrombin response. Using Fluorescence Recovery After Photobleaching (FRAP), we show that loss of SHP2 reduced the mobility of VE-cadherin at recovered cell-cell junctions.In conclusion, our data show that the SHP2 phosphatase plays an important role in the recovery of disrupted endothelial cell-cell junctions by dephosphorylating VE-cadherin-associated β-catenin and promoting the mobility of VE-cadherin at the plasma membrane.