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SHP2 binds catalase and acquires a hydrogen peroxide‐resistant phosphatase activity via integrin‐signaling
Author(s) -
Yano Sumio,
Arroyo Nelly,
Yano Noriko
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.10.011
Subject(s) - catalase , hydrogen peroxide , chemistry , phosphatase , enzyme , hela , microbiology and biotechnology , binding site , biochemistry , in vitro , biology
Here, we examined whether catalase binds SHP2 and alters SHP2 susceptibility to H 2 O 2 . Our results indicated that serum and fibrinogen commonly evoked catalase binding to SHP2 in HeLa and A549 cells in a herbimycin‐A and TNFα 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 H 2 O 2 ‐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 H 2 O 2 ‐resistant SHP2 activity.