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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2002-2-1
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HRAS protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/NFATC Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/NFATC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PIM1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-pim-1,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins p21(ras),
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
168
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1524-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11823475-Animals,
pubmed-meshheading:11823475-COS Cells,
pubmed-meshheading:11823475-DNA-Binding Proteins,
pubmed-meshheading:11823475-Humans,
pubmed-meshheading:11823475-Interleukin-2,
pubmed-meshheading:11823475-Jurkat Cells,
pubmed-meshheading:11823475-Mutation,
pubmed-meshheading:11823475-NFATC Transcription Factors,
pubmed-meshheading:11823475-Nuclear Proteins,
pubmed-meshheading:11823475-Phosphorylation,
pubmed-meshheading:11823475-Phosphoserine,
pubmed-meshheading:11823475-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11823475-Proto-Oncogene Proteins,
pubmed-meshheading:11823475-Proto-Oncogene Proteins c-pim-1,
pubmed-meshheading:11823475-Proto-Oncogene Proteins p21(ras),
pubmed-meshheading:11823475-Signal Transduction,
pubmed-meshheading:11823475-T-Lymphocytes,
pubmed-meshheading:11823475-Transcription Factors,
pubmed-meshheading:11823475-Transcriptional Activation
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pubmed:year |
2002
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pubmed:articleTitle |
Cutting edge: Transcriptional activity of NFATc1 is enhanced by the Pim-1 kinase.
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pubmed:affiliation |
Turku Centre for Biotechnology, University of Turku/Abo Akademi University, and Turku Graduate School of Biomedical Sciences, Turku, Finland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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