Activation-modulated association of 14-3-3 proteins with Cbl in T cells

J Biol Chem. 1996 Jun 14;271(24):14591-5. doi: 10.1074/jbc.271.24.14591.

Abstract

14-3-3 proteins have recently been implicated in the regulation of intracellular signaling pathways via their interaction with several oncogene and protooncogene products. We found recently that 14-3-3 associates with several tyrosine-phosphorylated proteins and phosphatidylinositol 3-kinase (PI3-K) in T cells. We report here the identification of the 120-kDa 14-3-3tau-binding phosphoprotein present in activated T cell lysates as Cbl, a protooncogene product of unknown function which was found recently to be a major protein-tyrosine kinase (PTK) substrate, and to interact with several signaling molecules including PI3-K, in T lymphocytes. The association between 14-3-3tau and Cbl was detected both in vitro and in intact T cells and, in contrast to Raf-1, was markedly increased following T cell activation. The use of truncated 14-3-3tau fusion proteins demonstrated that the 15 C-terminal residues are required for the association between 14-3-3 and three of its target proteins, namely, Cbl, Raf-1, and PI3-K. The findings that 14-3-3tau binds both PI3-K and Cbl, together with recent reports of an association between Cbl and PI3-K, suggest that 14-3-3 dimers play a critical role in signal transduction processes by promoting and coordinating protein-protein interactions of signaling proteins.

Publication types

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

MeSH terms

  • 14-3-3 Proteins
  • Base Sequence
  • Blotting, Western
  • Cell Line
  • Chromatography, Gel
  • DNA Primers
  • Escherichia coli
  • Humans
  • Leukemia
  • Lymphocyte Activation*
  • Molecular Sequence Data
  • Mutagenesis
  • Phosphatidylinositol 3-Kinases
  • Phosphotransferases (Alcohol Group Acceptor) / antagonists & inhibitors
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism
  • Polymerase Chain Reaction
  • Protein Binding
  • Protein Biosynthesis
  • Protein Serine-Threonine Kinases / metabolism
  • Protein-Tyrosine Kinases / metabolism
  • Proteins / isolation & purification
  • Proteins / metabolism*
  • Proto-Oncogene Proteins / biosynthesis
  • Proto-Oncogene Proteins / isolation & purification
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-cbl
  • Proto-Oncogene Proteins c-raf
  • Proto-Oncogenes
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / metabolism
  • Sequence Deletion
  • Signal Transduction
  • T-Lymphocytes / metabolism*
  • Tumor Cells, Cultured
  • Tyrosine 3-Monooxygenase*
  • Ubiquitin-Protein Ligases*

Substances

  • 14-3-3 Proteins
  • DNA Primers
  • Proteins
  • Proto-Oncogene Proteins
  • Recombinant Fusion Proteins
  • Tyrosine 3-Monooxygenase
  • Proto-Oncogene Proteins c-cbl
  • Ubiquitin-Protein Ligases
  • Phosphotransferases (Alcohol Group Acceptor)
  • Protein-Tyrosine Kinases
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-raf
  • CBL protein, human