Membrane-targeting is critical for the phosphorylation of Vav2 by activated EGF receptor

Péter Tamás, Zita Solti, László Buday

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Vav2 is a member of the Vav family that serves as guanine nucleotide exchange factors (GEFs) for the Rho family of Ras-related GTPases. Unlike Vav1, whose expression is restricted to cells of hematopoietic origin, Vav2 is broadly expressed. Recently, Vav2 has been identified as a substrate for the EGF receptor. Here, we show that in EGF-treated COS7 cells Vav2 is phosphorylated on tyrosine residues and associates with the EGF receptor. In addition, introducing point mutations into the SH2 domain of green fluorescens protein (GFP)-Vav2 fusion protein leads to the loss of Vav2 tyrosine phosphorylation in response to EGF. To investigate further the mechanism of Vav2 phosphorylation, N-terminal (NT) domain of Vav2 was transiently expressed in COS7 cells as GFP fusion protein. Whereas the NT domain of Vav2 is a preferred substrate for the activated EGF receptor in vitro, we could not detect tyrosine phosphorylation of the GFP-NT construct in EGF-treated cells. However, when the SH2 domain of Vav2 was fused to its NT domain, NT domain proved to be a substrate for the EGF receptor in vivo. These data suggest that membrane-targeting of Vav2 through its SH2 domain is an important event in the phosphorylation and activation of Vav2 in response to EGF.

Original languageEnglish
Pages (from-to)475-481
Number of pages7
JournalCellular Signalling
Volume13
Issue number7
DOIs
Publication statusPublished - Jun 27 2001

Keywords

  • EGF
  • GFP
  • SH2 domain
  • Vav2

ASJC Scopus subject areas

  • Cell Biology

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