Abstract
A human protein kinase, p53-related protein kinase (PRPK), was cloned from an interleukin-2-activated cytotoxic T-cell subtraction library. PRPK appears to be a homologue of a growth-related yeast serine/threonine protein kinase, YGR262c. However, a complementation assay using YGR262c-disrupted yeast indicated that PRPK is not functionally identical to the yeast enzyme. PRPK expression was observed in interleukin-2-activated cytotoxic T-cells, some human epithelial tumor cell lines, and the testes. The intrinsic transcriptional activity of p53 was up-regulated by a transient transfection of PRPK to COS-7 cells. PRPK was shown to bind to p53 and to phosphorylate p53 at Ser-15. These results indicate that PRPK may play an important role in the cell cycle and cell apoptosis through phosphorylation of p53.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Blotting, Northern
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Chromosome Mapping
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Cloning, Molecular
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DNA Primers
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DNA, Complementary
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Humans
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Immunohistochemistry
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In Situ Hybridization, Fluorescence
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Interleukin-2 / pharmacology*
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Intracellular Signaling Peptides and Proteins
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Lymphocyte Activation
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Male
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Molecular Sequence Data
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Phosphorylation
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Phylogeny
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Polymerase Chain Reaction
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Protein Kinases / chemistry
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Protein Kinases / genetics*
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Protein Kinases / metabolism
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Protein Serine-Threonine Kinases
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Sequence Homology, Amino Acid
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T-Lymphocytes, Cytotoxic / drug effects*
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T-Lymphocytes, Cytotoxic / metabolism
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Testis / cytology
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Testis / drug effects*
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Testis / metabolism
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Transcription, Genetic
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Tumor Cells, Cultured
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Tumor Suppressor Protein p53 / metabolism
Substances
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DNA Primers
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DNA, Complementary
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Interleukin-2
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Intracellular Signaling Peptides and Proteins
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Tumor Suppressor Protein p53
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Protein Kinases
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Protein Serine-Threonine Kinases
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TP53RK protein, human
Associated data
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GENBANK/AB017505
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GENBANK/AB028045