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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Protein-protein interaction between caveolin-1 and SHP-2 is dependent on the N-SH2 domain of SHP-2

  • Park, Hyunju (Department of Physiology, Tissue Injury Defense Research Center, Ewha Womans University School of Medicine) ;
  • Ahn, Keun Jae (Department of Science Education, Jeju National University) ;
  • Kang, Jihee Lee (Department of Physiology, Tissue Injury Defense Research Center, Ewha Womans University School of Medicine) ;
  • Choi, Youn-Hee (Department of Physiology, Tissue Injury Defense Research Center, Ewha Womans University School of Medicine)
  • Received : 2014.11.21
  • Accepted : 2015.02.04
  • Published : 2015.03.31
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Abstract

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 $H_2O_2$-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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References

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