SHP2 binds catalase and acquires a hydrogen peroxide-resistant phosphatase activity via integrin-signaling

Abstract

Here, we examined whether catalase binds SHP2 and alters SHP2 susceptibility to H2O2. Our results indicated that serum and fibrinogen commonly evoked catalase binding to SHP2 in HeLa and A549 cells in a herbimycin-A and TNFalpha sensitive manner. Expression of active catalase nearly 15-fold over control levels in tet-off HeLa cells substantially increased the SHP2 binding, and the catalase-associated SHP2 displayed significantly high phosphatase activities with a H2O2-resistance compared to those with little catalase. Site-directed mutagenesis at 280 abolished the binding capability of catalase to SHP2-SH2 in vitro. These results suggest that catalase-280pYIQV binds SHP2 via integrin-signaling to increase a H2O2-resistant SHP2 activity.