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Interleukin-2 stimulates association of protein kinase C with plasma membrane

Nature volume 315, pages 233–235 (1985)Cite this article

Abstract

Interleukin-2 (IL-2) is a regulatory peptide important for the growth and differentiation of antigen-specific T lymphocytes and large granular lymphocytes1,2. Interaction of IL-2 with its specific receptor results in the promotion of S-phase progression as well as, in certain circumstances, the production and release of γ-interferon (IFN-γ)3–5. Although the binding of IL-2 with high-affinity specific receptors has been well characterized6,7, the intracellular mechanisms by which this ligand–receptor interaction promotes growth and differentiation are unknown. Here, we present evidence that IL-2/receptor interaction produces a rapid and transient redistribution of protein kinase C (PK-C) from the cytosol to the plasma membrane. Phorbol myristate acetate (PMA) also induces PK-C transposition in an analogous manner, except that PMA-induced PK-C transposition to the plasma membrane is apparently protracted. As phorbol esters have been shown to mimic IL-2 in the regulation of cellular proliferation as well as IFN-γ production8–10, the activation of PK-C by either phorbol esters or IL-2/receptor interaction seems to have a crucial role in signal transduction elicited by these extracellular messengers.

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Authors and Affiliations

  1. Laboratory of Molecular Immunoregulation, National Cancer Institute-Frederick Cancer Research Facility, Frederick, Maryland, 21701, USA

    William L. Farrar

  2. Laboratory of Tumor Immunology and Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, 20205, USA

    Wayne B. Anderson

Authors
  1. William L. Farrar
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Farrar, W., Anderson, W. Interleukin-2 stimulates association of protein kinase C with plasma membrane. Nature 315, 233–235 (1985). https://doi.org/10.1038/315233a0

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