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

被引：64

作者：

Abe, Y ^{[1
]}

Matsumoto, S

Wei, SM

Nezu, K

Miyoshi, A

Kito, K

Ueda, N

Shigemoto, K

Hitsumoto, Y

Nikawa, J

机构：

[1] Ehime Univ, Sch Med, Dept Pathol & Hyg 1, Shigenobu, Ehime 7910295, Japan

[2] Okayama Univ, Fac Sci, Dept Biol Chem, Div Clin Immunol, Okayama 7000005, Japan

[3] Kyushu Inst Technol, Fac Comp Sci & Syst Engn, Dept Biochem Engn & Sci, Kawazu, Fukuoka 8208502, Japan

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2001年 / 276卷 / 47期

关键词：

D O I：

10.1074/jbc.M105669200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：44003 / 44011

页数：9

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