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    J Biol Chem. 2001 Nov 23;276(47):44003-11. Epub 2001 Sep 6.

    Cloning and characterization of a p53-related protein kinase expressed in interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and the testes.

    Abe Y, Matsumoto S, Wei S, Nezu K, Miyoshi A, Kito K, Ueda N, Shigemoto K, Hitsumoto Y, Nikawa J, Enomoto Y.

    First Department of Pathology and Hygiene, Ehime University School of Medicine, Shigenobu, Ehime 791-0295, Japan. yasuhito@m.ehime-u.ac.jp

    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.

    PMID: 11546806 [PubMed - indexed for MEDLINE]

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