Cloning and Characterization of a p53-related Protein Kinase Expressed in Interleukin-2-activated Cytotoxic T-cells, Epithelial Tumor Cell Lines, and the Testes

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 yeas...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-11, Vol.276 (47), p.44003-44011
Main Authors: Abe, Yasuhito, Matsumoto, Suguru, Wei, Shumei, Nezu, Kenji, Miyoshi, Akifumi, Kito, Katsumi, Ueda, Norifumi, Shigemoto, Kazuhiro, Hitsumoto, Yasuo, Nikawa, Jun-ichi, Enomoto, Yosuke
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Blotting, Northern
Chromosome Mapping
Cloning, Molecular
DNA Primers
DNA, Complementary
Humans
Immunohistochemistry
In Situ Hybridization, Fluorescence
Interleukin-2 - pharmacology
Intracellular Signaling Peptides and Proteins
Lymphocyte Activation
Male
Molecular Sequence Data
p53-related protein kinase
Phosphorylation
Phylogeny
Polymerase Chain Reaction
Protein Kinases - chemistry
Protein Kinases - genetics
Protein Kinases - metabolism
Protein-Serine-Threonine Kinases
PRPK protein
Sequence Homology, Amino Acid
T-Lymphocytes, Cytotoxic - drug effects
T-Lymphocytes, Cytotoxic - metabolism
Testis - cytology
Testis - drug effects
Testis - metabolism
Transcription, Genetic
Tumor Cells, Cultured
Tumor Suppressor Protein p53 - metabolism
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M105669200