Fig. 6

DUSP19 dephosphorylates VEGFR3 via a direct receptor tyrosine kinase–protein phosphatase interaction. A Western blot analysis of the VEGFR3 immunoprecipitates showed that DUSP19 was present in the immunocomplex from QGP-1 cells with knockdown of vector control (shLuc) but not present in the immunocomplex from QGP-1 cells with DUSP19 knockdown (left panel). Western blot analysis of the DUSP19 immunoprecipitates showed that VEGFR3 was present in the immunocomplex from QGP-1 cells with knockdown of vector control (shLuc) but not present in the immunocomplex from QGP-1 cells with VEGFR3 knockdown (right panel). Immunoprecipitation with IgG was used as negative control. B VEGFR3 and DUSP19 were shown to be colocalized on the cell membrane of QGP-1 cells by immunofluorescence staining. C Confocal microscope images of XY and XZ sections. D The phospho-signal of the phospho-VEGFR3 peptide was reduced by the addition of recombinant DUSP19 (P = 0.021, Wilcoxon rank-sum test)