Ligand-induced polyubiquitination of receptor tyrosine kinases

Biochem Biophys Res Commun. 1995 Aug 4;213(1):32-9. doi: 10.1006/bbrc.1995.2094.

Abstract

The platelet-derived growth factor beta-receptor undergoes polyubiquitination as a consequence of ligand binding. In the present study, we have examined the ligand-induced receptor ubiquitination also in the other receptor tyrosine kinase (structurally different) subfamilies by immunoblotting with anti-ubiquitin antiserum. In addition to the platelet-derived growth factor alpha- and beta-receptors, all the monomeric receptor tyrosine kinases examined, such as the receptors for epidermal growth factor (subfamily I), colony stimulating factor-1 (subfamily III), and fibroblast growth factor (subfamily IV), were found to be ubiquitinated after ligand stimulation. However, the insulin receptor (subfamily II), which is a tetrameric molecule, was not. These data suggest that the ligand-induced polyubiquitination of the receptor is a general phenomenon observed in most of the monomeric receptor tyrosine kinases.

MeSH terms

  • 3T3 Cells
  • Animals
  • Aorta
  • Becaplermin
  • CHO Cells
  • Cells, Cultured
  • Cricetinae
  • Endothelium, Vascular / metabolism*
  • ErbB Receptors / isolation & purification
  • ErbB Receptors / metabolism
  • Humans
  • Immunoblotting
  • Kinetics
  • Macromolecular Substances
  • Male
  • Mice
  • Platelet-Derived Growth Factor / pharmacology*
  • Proto-Oncogene Proteins c-sis
  • Receptor Protein-Tyrosine Kinases / drug effects
  • Receptor Protein-Tyrosine Kinases / metabolism*
  • Receptor, Insulin / isolation & purification
  • Receptor, Insulin / metabolism
  • Receptor, Macrophage Colony-Stimulating Factor / isolation & purification
  • Receptor, Macrophage Colony-Stimulating Factor / metabolism
  • Receptors, Fibroblast Growth Factor / isolation & purification
  • Receptors, Fibroblast Growth Factor / metabolism
  • Receptors, Platelet-Derived Growth Factor / isolation & purification
  • Receptors, Platelet-Derived Growth Factor / metabolism*
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / pharmacology
  • Skin / metabolism
  • Swine
  • Transfection
  • Ubiquitins / metabolism*

Substances

  • Macromolecular Substances
  • Platelet-Derived Growth Factor
  • Proto-Oncogene Proteins c-sis
  • Receptors, Fibroblast Growth Factor
  • Recombinant Proteins
  • Ubiquitins
  • Becaplermin
  • ErbB Receptors
  • Receptor Protein-Tyrosine Kinases
  • Receptor, Insulin
  • Receptor, Macrophage Colony-Stimulating Factor
  • Receptors, Platelet-Derived Growth Factor