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KMID : 0624620150480030184
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BMB Reports
2015 Volume.48 No. 3 p.184 ~ p.189
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Protein-protein interaction between caveolin-1 and SHP-2 is dependent on the N-SH2 domain of SHP-2
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Park Hyun-Ju
Ahn Keun-Jae
Lee Kang Ji-Hee
Choi Youn-Hee
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Abstract
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Src homology 2-containing protein tyrosine phosphatase 2 (SHP-2) is known to protect neurons from neurodegeneration during ischemia/reperfusion injury. We recently reported that ROS-mediated oxidative stress promotes phosphorylation of endogenous SHP-2 in astrocytes and complex formation between caveolin-1 and SHP-2 in response to oxidative stress. To examine the region of SHP-2 participating in complex formation with caveolin-1, we generated three deletion mutant constructs and six point mutation constructs of SHP-2. Compared with wild-type SHP-2, binding of the N-SH2 domain deletion mutant of SHP-2 to p-caveolin-1 was reduced greatly, using flow cytometric competitive binding assays and surface plasmon resonance (SPR). Moreover, deletion of the N-SH2 domain of SHP-2 affected H2O2-mediated ERK phosphorylation and Src phosphorylation at Tyr 419 in primary astrocytes, suggesting that N-SH2 domain of SHP-2 is responsible for the binding of caveolin-1 and contributes to the regulation of Src phosphorylation and activation following ROS-induced oxidative stress in brain astrocytes.
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KEYWORD
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Astrocytes, Caveolin-1, Reactive oxygen species, SHP-2, Src
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