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.

Keywords

Cytotoxic T cellCloning (programming)BiologyMolecular biologyCell biologyProtein kinase ACell cultureCancer researchChemistryKinaseBiochemistryIn vitroGenetics

MeSH Terms

Amino Acid SequenceAnimalsBase SequenceBlottingNorthernChromosome MappingCloningMolecularDNA PrimersDNAComplementaryHumansImmunohistochemistryIn Situ HybridizationFluorescenceInterleukin-2Intracellular Signaling Peptides and ProteinsLymphocyte ActivationMaleMolecular Sequence DataPhosphorylationPhylogenyPolymerase Chain ReactionProtein KinasesProtein Serine-Threonine KinasesSequence HomologyAmino AcidT-LymphocytesCytotoxicTestisTranscriptionGeneticTumor CellsCulturedTumor Suppressor Protein p53

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Publication Info

Year
2001
Type
article
Volume
276
Issue
47
Pages
44003-44011
Citations
80
Access
Closed

Citation Metrics

80
OpenAlex
5
Influential
61
CrossRef

Cite This

Yasuhito Abe, Suguru Matsumoto, Shumei Wei et al. (2001). Cloning and Characterization of a p53-related Protein Kinase Expressed in Interleukin-2-activated Cytotoxic T-cells, Epithelial Tumor Cell Lines, and the Testes. Journal of Biological Chemistry , 276 (47) , 44003-44011. https://doi.org/10.1074/jbc.m105669200

Identifiers

DOI
10.1074/jbc.m105669200
PMID
11546806

Data Quality

Data completeness: 86%