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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 RIS Download

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

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