Utilization of the beta and gamma chains of the IL-2 receptor by the novel cytokine IL-15

EMBO J. 1994 Jun 15;13(12):2822-30.

Abstract

We have recently cloned a novel cytokine, IL-15, with shared bioactivities but no sequence homology with IL-2. We found high affinity IL-15 binding to many cell types, including cells of non-lymphoid origin. Analysis of IL-15 interaction with subunits of the IL-2 receptor (IL-2R) revealed that the alpha subunit was not involved in IL-15 binding. We demonstrated directly in cells transfected with IL-2R subunits that both the beta and gamma chains are required for IL-15 binding and signaling. Hence, IL-15, like IL-2, IL-4 and IL-7, utilizes the common IL-2R gamma subunit found to be defective in X-linked severe combined immunodeficiency in humans. IL-15 is the only cytokine other than IL-2 that has also been shown to share the beta signaling subunit of IL-2R. The differential ability of some cells to bind and respond to IL-2 and IL-15 implies the existence of an additional IL-15-specific component.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Cell Line
  • Haplorhini
  • Humans
  • Interleukin-15
  • Interleukins / metabolism*
  • Protein Binding
  • Protein Conformation
  • Receptors, Interleukin-2 / metabolism*
  • Recombinant Proteins / metabolism
  • Structure-Activity Relationship

Substances

  • Interleukin-15
  • Interleukins
  • Receptors, Interleukin-2
  • Recombinant Proteins