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Protein-protein interaction between caveolin-1 and SHP-2 is dependent on the N-SH2 domain of SHP-2

Title
Protein-protein interaction between caveolin-1 and SHP-2 is dependent on the N-SH2 domain of SHP-2
Authors
Park H.Ahn K.J.Kang J.L.Choi Y.-H.
Ewha Authors
이지희최윤희
SCOPUS Author ID
이지희scopus; 최윤희scopus
Issue Date
2015
Journal Title
BMB Reports
ISSN
1976-6696JCR Link
Citation
vol. 48, no. 3, pp. 184 - 189
Keywords
AstrocytesCaveolin-1Reactive oxygen speciesSHP-2Src
Publisher
The Biochemical Society of the Republic of Korea
Indexed
SCIE; SCOPUS; KCI WOS scopus
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<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.
DOI
10.5483/BMBRep.2015.48.3.249
Appears in Collections:
의학전문대학원 > 의학과 > Journal papers
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