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Cutting edge: Transcriptional activity of NFATc1 is enhanced by the Pim-1 kinase.

Pim-1 is an oncogenic serine/threonine kinase implicated in cytokine-induced signal transduction and in development of lymphoid malignancies. However, its precise function as well as physiological substrates have remained unknown. In this study we demonstrate that Pim-1 can physically interact with the NFATc1 transcription factor and phosphorylate it in vitro on several serine residues. In contrast to previously recognized NFATc kinases, wild-type Pim-1 enhances NFATc-dependent transactivation and IL-2 production in Jurkat T cells, while kinase-deficient Pim-1 mutants inhibit them in a dominant negative fashion. Our results reveal a novel, phosphorylation-dependent regulatory mechanism targeting NFATc1 through which Pim-1 acts as a downstream effector of Ras to facilitate IL-2-dependent proliferation and/or survival of lymphoid cells.

Pubmed ID: 11823475

Authors

  • Rainio EM
  • Sandholm J
  • Koskinen PJ

Journal

Journal of immunology (Baltimore, Md. : 1950)

Publication Data

February 15, 2002

Associated Grants

None

Mesh Terms

  • Animals
  • COS Cells
  • DNA-Binding Proteins
  • Humans
  • Interleukin-2
  • Jurkat Cells
  • Mutation
  • NFATC Transcription Factors
  • Nuclear Proteins
  • Phosphorylation
  • Phosphoserine
  • Protein-Serine-Threonine Kinases
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-pim-1
  • Proto-Oncogene Proteins p21(ras)
  • Signal Transduction
  • T-Lymphocytes
  • Transcription Factors
  • Transcriptional Activation