Protein-protein interaction between caveolin-1 and SHP-2 is dependent on the N-SH2 domain of SHP-2
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Src homology 2-containing protein tyrosine phosphatase 2(SHP-2) is known to protect neurons from neurodegenerationduring ischemia/reperfusion injury. We recently reported thatROS-mediated oxidative stress promotes phosphorylation ofendogenous SHP-2 in astrocytes and complex formation betweencaveolin-1 and SHP-2 in response to oxidative stress. Toexamine the region of SHP-2 participating in complex formationwith caveolin-1, we generated three deletion mutantconstructs and six point mutation constructs of SHP-2. Compared with wild-type SHP-2, binding of the N-SH2 domaindeletion mutant of SHP-2 to p-caveolin-1 was reducedgreatly, using flow cytometric competitive binding assays andsurface plasmon resonance (SPR). Moreover, deletion of theN-SH2 domain of SHP-2 affected H2O2-mediated ERK phosphorylationand Src phosphorylation at Tyr 419 in primary astrocytes,suggesting that N-SH2 domain of SHP-2 is responsiblefor the binding of caveolin-1 and contributes to the regulationof Src phosphorylation and activation following ROS-inducedoxidative stress in brain astrocytes.
Abstract
Src homology 2-containing protein tyrosine phosphatase 2(SHP-2) is known to protect neurons from neurodegenerationduring ischemia/reperfusion injury. We recently reported thatROS-mediated oxidative stress promotes phosphorylation ofendogenous SHP-2 in astrocytes and complex formation betweencaveolin-1 and SHP-2 in response to oxidative stress. Toexamine the region of SHP-2 participating in complex formationwith caveolin-1, we generated three deletion mutantconstructs and six point mutation constructs of SHP-2. Compared with wild-type SHP-2, binding of the N-SH2 domaindeletion mutant of SHP-2 to p-caveolin-1 was reducedgreatly, using flow cytometric competitive binding assays andsurface plasmon resonance (SPR). Moreover, deletion of theN-SH2 domain of SHP-2 affected H2O2-mediated ERK phosphorylationand Src phosphorylation at Tyr 419 in primary astrocytes,suggesting that N-SH2 domain of SHP-2 is responsiblefor the binding of caveolin-1 and contributes to the regulationof Src phosphorylation and activation following ROS-inducedoxidative stress in brain astrocytes.
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