Regulation of platelet-derived growth factor-induced Ras signaling by poliovirus receptor Necl-5 and negative growth regulator Sprouty2

Genes Cells. 2007 Mar;12(3):345-57. doi: 10.1111/j.1365-2443.2007.01062.x.

Abstract

Necl-5, known as a poliovirus receptor and up-regulated in many cancer cells, enhances platelet-derived growth factor (PDGF)-induced activation of Ras-Raf-MEK-ERK signaling, but not PDGF-induced tyrosine phosphorylation of PDGF receptor, resulting in facilitation of cell proliferation. Here, we showed that Necl-5 interacted with Sprouty2, known to be a negative regulator of growth factor-induced signaling, and reduced the inhibitory effect of Sprouty2 on PDGF-induced Ras signaling. Necl-5 was reported to be down-regulated by its trans-interaction with nectin-3 upon cell-cell contact, initiating cooperative cell-cell adhesion with cadherin. This down-regulation of Necl-5 caused tyrosine phosphorylation of Sprouty2 by c-Src, which was activated by PDGF receptor in response to PDGF, and inhibited PDGF-induced Ras signaling. Thus, Necl-5 and Sprouty2 cooperatively regulate PDGF-induced Ras signaling. The roles of Necl-5 and Sprouty2 in contact inhibition for cell proliferation are also discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Antigens, Neoplasm / genetics
  • Antigens, Neoplasm / metabolism*
  • Becaplermin
  • CSK Tyrosine-Protein Kinase
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism*
  • Down-Regulation
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • MAP Kinase Signaling System
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mice
  • Models, Biological
  • NIH 3T3 Cells
  • Neoplasm Proteins / genetics
  • Neoplasm Proteins / metabolism*
  • Phosphorylation
  • Platelet-Derived Growth Factor / pharmacology*
  • Protein Serine-Threonine Kinases
  • Protein-Tyrosine Kinases / metabolism
  • Proto-Oncogene Proteins c-sis
  • Receptors, Platelet-Derived Growth Factor / metabolism
  • Receptors, Virus / genetics
  • Receptors, Virus / metabolism*
  • Recombinant Proteins / pharmacology
  • Signal Transduction / drug effects
  • ras Proteins / metabolism*
  • src-Family Kinases

Substances

  • Adaptor Proteins, Signal Transducing
  • Antigens, Neoplasm
  • Cell Adhesion Molecules
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Neoplasm Proteins
  • Platelet-Derived Growth Factor
  • Proto-Oncogene Proteins c-sis
  • Receptors, Virus
  • Recombinant Proteins
  • Taa1 protein, mouse
  • poliovirus receptor
  • Becaplermin
  • Protein-Tyrosine Kinases
  • Receptors, Platelet-Derived Growth Factor
  • CSK Tyrosine-Protein Kinase
  • src-Family Kinases
  • CSK protein, human
  • Protein Serine-Threonine Kinases
  • Spry2 protein, mouse
  • ras Proteins