Physical and functional interactions between protein tyrosine phosphatase alpha, PI 3-kinase, and PKCdelta

Biochem Biophys Res Commun. 2001 Nov 2;288(3):564-72. doi: 10.1006/bbrc.2001.5811.

Abstract

The somatostatin analogue, TT-232 inhibits cell proliferation and induces apoptosis in a variety of tumor cells both in vivo and in vitro. While the early transient activation of Erk/MAPK was found to be important for the induction of cell cycle arrest, the signaling pathway leading to the activation of Erk/MAPK had not been fully established. Here we present evidence that activation of the Erk/MAPK pathway by TT-232 involves PI 3-kinase, PKCdelta and the protein tyrosine phosphatase alpha (PTPalpha). We show a physical interaction of PI 3-kinase and PKCdelta with PTPalpha and show that the tyrosine phosphatase plays a role in the activation of MAPK. In this process, PTPalpha Ser-180 and Ser-204 phosphorylation is critical for the induction of phosphatase activity, which is required for dephosphorylation of pp60(c-src). Taken together, we demonstrate the physical and functional association between PI 3-kinase, PKCdelta and PTPalpha in a signaling complex that mediates the antitumor activity of the somatostatin analogue TT-232.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antineoplastic Agents / pharmacology
  • COS Cells
  • Cells, Cultured
  • Enzyme Activation
  • GTP-Binding Proteins / physiology
  • Genes, src / physiology
  • Heterogeneous-Nuclear Ribonucleoprotein Group F-H*
  • Humans
  • Isoenzymes / metabolism*
  • Mitogen-Activated Protein Kinases / metabolism
  • Peptides, Cyclic / pharmacology
  • Phosphatidylinositol 3-Kinases / metabolism*
  • Phosphorylation
  • Protein Kinase C / metabolism*
  • Protein Kinase C-delta
  • Protein Tyrosine Phosphatases / metabolism*
  • RNA-Binding Proteins
  • Serine / metabolism
  • Signal Transduction / drug effects
  • Somatostatin
  • Virulence Factors, Bordetella / pharmacology

Substances

  • Antineoplastic Agents
  • HNRNPH2 protein, human
  • Heterogeneous-Nuclear Ribonucleoprotein Group F-H
  • Isoenzymes
  • Peptides, Cyclic
  • RNA-Binding Proteins
  • Virulence Factors, Bordetella
  • Serine
  • TT2-32
  • Somatostatin
  • Phosphatidylinositol 3-Kinases
  • PRKCD protein, human
  • Protein Kinase C
  • Protein Kinase C-delta
  • Mitogen-Activated Protein Kinases
  • Protein Tyrosine Phosphatases
  • GTP-Binding Proteins