Optimization of the cellular import of functionally active SH2-domain-interacting phosphopeptides

Á Kertész, G. Váradi, G. K. Tóth, R. Fajka-Boja, É Monostori, G. Sármay

Research output: Contribution to journalArticle

3 Citations (Scopus)


Phosphopeptides interacting with src homology 2 (SH2) domains can activate essential signaling enzymes in vitro. When delivered to cells, they may disrupt protein-protein interactions, thereby influencing intracellular signaling. We showed earlier that phosphopeptides corresponding to the inhibitory motif of Fcγ receptor IIb and a motif of the Grb2-associated binder 1 adaptor protein activate SH2-containing tyrosine phosphatase 2 in vitro. To study the ex vivo effects of these peptides, we have now compared different methods for peptide delivery: (i) permeabilization of the target cells and (ii) the use of cell-permeable vectors, which are potentially able to transport biologically active compounds into B cells. We found octanoyl-Arg8 to be an optimal carrier for the delivery of phosphopeptides to the cells. With this strategy, the function of cell-permeable SHP-2-binding phosphopeptides was analyzed. These peptides modulated the protein phosphorylation in B cells in a dose- and time-dependent manner.

Original languageEnglish
Pages (from-to)2682-2693
Number of pages12
JournalCellular and Molecular Life Sciences
Issue number22
Publication statusPublished - Nov 1 2006


  • Cell-permeable peptide
  • Phosphopeptide
  • SH2 domain
  • Signaling
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology

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