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. Author manuscript; available in PMC: 2020 Aug 15.
Published in final edited form as: Cell Chem Biol. 2019 May 23;26(8):1081–1094.e6. doi: 10.1016/j.chembiol.2019.04.007

Figure 7: The role of VE cadherin phosphorylation on Y731 following S1P treatment.

Figure 7:

(A) Phosphorylation of VE cadherin on Y731 following treatment with S1P. HPAE cells were serum starved for 1 hour and then treated with 1 μM S1P. Cell lysates were collected at the indicated time points, VE cadherin was immunoprecipitated, and samples were analyzed for phospho-Y731-VE cadherin and total VE cadherin. VE cadherin phosphorylation levels were normalized to time 0 to obtain relative phosphorylation values. The average relative phosphorylation was calculated from 3 independent experiments; error bars depict standard deviation. Significance was determined via a one-way ANOVA with a Dunnett’s multiple comparisons correction, *p < 0.05. (B) The role of VE cadherin phosphorylation in S1P-mediated endothelial barrier enhancement. HPAE cells expressing indicated VE cadherin-GFP construct wild-type (WT), Y658F, or Y731F mutant) were analyzed by TER. Cells were serum starved for 1 hour and then treated with S1P (1 μM) (0 min). Graph shows the average resistance from 3 independent experiments and the error bars show 90% confidence intervals. All exogenous proteins were expressed using adenoviral transduction. See also figures S6E–F.