c-Cbl is a suppressor of the neu oncogene

J Biol Chem. 2000 Nov 10;275(45):35532-9. doi: 10.1074/jbc.M002661200.

Abstract

A rodent oncogenic mutant of the Neu receptor tyrosine kinase is a useful experimental model because overexpression of the respective receptor, namely HER2/ErbB-2, in human malignancies is associated with relatively aggressive diseases. Here we show that the oncogenic form of Neu is constitutively associated with the product of the c-cbl proto-oncogene and is part of a large complex that includes the phosphoinositide 3-kinase and Shc. Ectopic expression of c-Cbl, a ubiquitin-protein isopeptide ligase specific to activated tyrosine kinases, causes rapid removal of Neu from the cell surface and severely reduces signaling downstream of oncogenic Neu. c-Cbl-induced down-regulation of Neu involves covalent attachment of ubiquitin molecules and requires the carboxyl-terminal domain of Neu. The negative effect of c-Cbl is antagonized by v-Cbl, a virus-encoded oncogenic truncated form of c-Cbl. In an in vivo model, infection of a Neu-transformed neuroblastoma with a c-Cbl-encoding retrovirus caused enhanced down-regulation of Neu and correlated with tumor retardation. Our results implicate c-Cbl in negative regulation of Neu and offer a potential target for treatment of HER2/ErbB-2-positive human malignancies.

Publication types

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

MeSH terms

  • 3T3 Cells
  • Adaptor Proteins, Signal Transducing*
  • Adaptor Proteins, Vesicular Transport*
  • Animals
  • Antibodies, Monoclonal / metabolism
  • Biotinylation
  • CHO Cells
  • Cell Line
  • Cricetinae
  • DNA, Complementary / metabolism
  • DNA-Binding Proteins / metabolism
  • Down-Regulation
  • Electrophoresis, Polyacrylamide Gel
  • Fibroblasts / metabolism
  • Humans
  • Immunoblotting
  • Ligases / metabolism
  • Male
  • Mice
  • Mice, Nude
  • Neoplasm Transplantation
  • Neuroblastoma / metabolism
  • Nuclear Proteins / metabolism
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphorylation
  • Precipitin Tests
  • Protein Structure, Tertiary
  • Proteins / metabolism
  • Proto-Oncogene Mas
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins / physiology*
  • Proto-Oncogene Proteins c-cbl
  • Rats
  • Receptor, ErbB-2 / genetics
  • Receptor, ErbB-2 / metabolism*
  • Retroviridae / genetics
  • Serum Response Factor
  • Shc Signaling Adaptor Proteins
  • Signal Transduction
  • Src Homology 2 Domain-Containing, Transforming Protein 1
  • Time Factors
  • Transfection
  • Ubiquitin-Protein Ligases

Substances

  • Adaptor Proteins, Signal Transducing
  • Adaptor Proteins, Vesicular Transport
  • Antibodies, Monoclonal
  • DNA, Complementary
  • DNA-Binding Proteins
  • MAS1 protein, human
  • Nuclear Proteins
  • Proteins
  • Proto-Oncogene Mas
  • Proto-Oncogene Proteins
  • SHC1 protein, human
  • Serum Response Factor
  • Shc Signaling Adaptor Proteins
  • Shc1 protein, mouse
  • Shc1 protein, rat
  • Src Homology 2 Domain-Containing, Transforming Protein 1
  • Proto-Oncogene Proteins c-cbl
  • Ubiquitin-Protein Ligases
  • Receptor, ErbB-2
  • Ligases
  • CBL protein, human
  • Cbl protein, mouse