Tyrosyl phosphorylation and growth factor receptor association of the human corkscrew homologue, SH-PTP2

J Biol Chem. 1993 Jun 25;268(18):13434-8.

Abstract

The pivotal role of tyrosine kinases in signal transduction is well established, but the role of tyrosine phosphatases remains obscure. The discovery of src homology 2 domain-containing protein tyrosine phosphatases suggested roles for these molecules in growth factor signaling pathways, since src homology 2 domains direct association of downstream signaling molecules with activated growth factor receptors and other phosphotyrosyl proteins. We have found that SH-PTP2, a putative homologue of Drosophila corkscrew, associates in vivo with the ligand-activated epidermal growth factor and platelet-derived growth factor receptors. The N-terminal src homology 2 domain of SH-PTP2 directly associates with activated receptors. SH-PTP2 itself is a phosphoprotein, and it becomes tyrosyl phosphorylated upon growth factor activation. These findings suggest several possible models for SH-PTP2 signaling.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3T3 Cells
  • Animals
  • CHO Cells
  • Cells, Cultured
  • Cricetinae
  • ErbB Receptors / metabolism*
  • Humans
  • Mice
  • Mice, Inbred BALB C
  • Phosphorylation
  • Protein Tyrosine Phosphatases / metabolism*
  • Receptors, Platelet-Derived Growth Factor / metabolism*
  • Tyrosine / metabolism*

Substances

  • Tyrosine
  • ErbB Receptors
  • Receptors, Platelet-Derived Growth Factor
  • Protein Tyrosine Phosphatases