Protein-protein interaction between caveolin-1 and SHP-2 is dependent on the N-SH2 domain of SHP-2
- 주제(키워드) Astrocytes , Caveolin-1 , Reactive oxygen species , SHP-2 , Src
- 등재 SCIE, KCI등재, SCOPUS
- 발행기관 The Biochemical Society of the Republic of Korea
- 발행년도 2015
- 총서유형 Journal
- URI http://www.dcollection.net/handler/ewha/000000115502
- 본문언어 영어
- Published As http://dx.doi.org/10.5483/BMBRep.2015.48.3.249
초록/요약
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<inf>2</inf>O<inf>2</inf>-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. © 2015 by the The Korean Society for Biochemistry and Molecular Biology.
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