Signal transduction and cellular functions of the TEL/ARG oncoprotein

Leukemia. 2005 Apr;19(4):603-10. doi: 10.1038/sj.leu.2403668.

Abstract

The TEL/ARG oncogene is formed by t(1;12)(q25;p13) reciprocal translocation and is associated with human leukemia. We have previously demonstrated that the expression of TEL/ARG in Ba/F3 cells results in prolonged viability and hyper-responsiveness to IL-3. To determine the molecular mechanisms, a series of mutants of TEL/ARG were generated, and each cDNA was expressed in Ba/F3 or CHO cells. The PNT domain in TEL and K317 in ARG were essential for both signaling and biological effects. The SH3 domain in ARG was required for hyper-responsiveness to IL-3, but not for prolonged viability. The opposite was true for the SH2 domain in ARG. Mutation of Y314 in TEL, a putative GRB2-binding site, led to reduced viability, and loss of hyper-responsiveness to IL-3. All biological functions were profoundly impaired with deletion of the C-terminus in ARG, despite maintaining high levels of its kinase activity. When expressed in CHO cells, wild-type TEL/ARG induced the formation of fillopodia, in a fashion dependent on the C-terminal portion and intact kinase activity. Thus, these results suggest several critical domains within TEL/ARG necessary for function, and indicate that the signaling pathways necessary for viability, growth factor hyper-responsiveness and cytoskeletal reorganization are likely to be separate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / metabolism
  • Adaptor Proteins, Signal Transducing / metabolism
  • Animals
  • Anti-Bacterial Agents / pharmacology
  • CHO Cells
  • Cell Movement / physiology
  • Cricetinae
  • Doxycycline / pharmacology
  • GRB2 Adaptor Protein
  • Gene Expression Regulation, Leukemic / drug effects
  • Hematopoietic Stem Cells / cytology
  • Hematopoietic Stem Cells / physiology
  • Humans
  • Integrin beta1 / genetics
  • Interleukin-3 / pharmacology
  • Leukemia / metabolism*
  • Leukemia / pathology
  • Mutagenesis
  • Oncogene Proteins, Fusion / genetics*
  • Oncogene Proteins, Fusion / metabolism*
  • Protein-Tyrosine Kinases / metabolism
  • Recombinant Fusion Proteins / genetics*
  • Recombinant Fusion Proteins / metabolism*
  • Signal Transduction / physiology*
  • src Homology Domains / physiology

Substances

  • Adaptor Proteins, Signal Transducing
  • Anti-Bacterial Agents
  • GRB2 Adaptor Protein
  • GRB2 protein, human
  • Integrin beta1
  • Interleukin-3
  • Oncogene Proteins, Fusion
  • Recombinant Fusion Proteins
  • TEL-ARG fusion protein, human
  • Protein-Tyrosine Kinases
  • Doxycycline