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

Hyunju Park, Keun Jae Ahn, Jihee Lee Kang, Youn Hee Choi

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


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.

Original languageEnglish
Pages (from-to)184-189
Number of pages6
JournalBMB Reports
Issue number3
StatePublished - 2015

Bibliographical note

Publisher Copyright:
© 2015 by the The Korean Society for Biochemistry and Molecular Biology.


  • Astrocytes
  • Caveolin-1
  • Reactive oxygen species
  • SHP-2
  • Src


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