A restricted cytoplasmic region of IL-2 receptor beta chain is essential for growth signal transduction but not for ligand binding and internalization

Cell. 1989 Dec 1;59(5):837-45. doi: 10.1016/0092-8674(89)90607-7.


The functional, high affinity form of interleukin-2 receptor (IL-2R) is composed of two receptor components, the IL-2R alpha (p55) and IL-2R beta (p70-75) chains. Unlike the IL-2R alpha chain, the IL-2R beta chain contains a large cytoplasmic domain that shows no obvious tyrosine kinase motif. In the present study, we report the establishment of a system in which the cDNA-directed human IL-2R beta allows growth signal transduction in a mouse pro-B cell line. This system enabled us to identify a unique region within the cytoplasmic domain of the human IL-2R beta chain essential for ligand-mediated signal transduction. We also demonstrate that certain cytoplasmic deletion mutants in the IL-2R beta chain, although deficient in signal transduction, can still form high affinity IL-2R in conjunction with endogenous mouse IL-2R alpha chain; the mutants are still able to internalize the ligand as well.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies
  • B-Lymphocytes
  • Binding Sites
  • Cell Division
  • Cell Line
  • Cytoplasm / metabolism
  • DNA Replication*
  • Humans
  • Interleukin-2 / metabolism
  • Kinetics
  • Ligands
  • Macromolecular Substances
  • Mice
  • Molecular Sequence Data
  • Mutation
  • Plasmids
  • Receptors, Interleukin-2 / genetics*
  • Receptors, Interleukin-2 / metabolism
  • Receptors, Interleukin-2 / physiology
  • Signal Transduction*
  • Transfection


  • Antibodies
  • Interleukin-2
  • Ligands
  • Macromolecular Substances
  • Receptors, Interleukin-2