Journal
FEBS LETTERS
Volume 577, Issue 3, Pages 327-332Publisher
WILEY
DOI: 10.1016/j.febslet.2004.10.011
Keywords
catalase; SHP2; integrin; hydrogen peroxide; tet-off HeLa; A549; TNF alpha
Funding
- NIEHS NIH HHS [R03ES11474] Funding Source: Medline
- NIGMS NIH HHS [S06GM08239, S06 GM008239] Funding Source: Medline
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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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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