title: Cloning and characterization of a p53-related protein kinase expressed in interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and the testes.
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.
authors.affiliation: First Department of Pathology and Hygiene, Ehime University School of Medicine, Shigenobu, Ehime 791-0295, Japan. yasuhito@m.ehime-u.ac.jp
authors.forename: Y
authors.initials: Y
authors.lastname: Abe
authors.forename: S
authors.initials: S
authors.lastname: Matsumoto
authors.forename: S
authors.initials: S
authors.lastname: Wei
authors.forename: K
authors.initials: K
authors.lastname: Nezu
authors.forename: A
authors.initials: A
authors.lastname: Miyoshi
authors.forename: K
authors.initials: K
authors.lastname: Kito
authors.forename: N
authors.initials: N
authors.lastname: Ueda
authors.forename: K
authors.initials: K
authors.lastname: Shigemoto
authors.forename: Y
authors.initials: Y
authors.lastname: Hitsumoto
authors.forename: J
authors.initials: J
authors.lastname: Nikawa
authors.forename: Y
authors.initials: Y
authors.lastname: Enomoto
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D017931:DNA Primers; D018076:DNA, Complementary; D006801:Humans; D007150:Immunohistochemistry; D017404:In Situ Hybridization, Fluorescence; D007376:Interleukin-2 / Q000494:pharmacology*; D047908:Intracellular Signaling Peptides and Proteins; D008213:Lymphocyte Activation; D008297:Male; D008969:Molecular Sequence Data; D010766:Phosphorylation; D010802:Phylogeny; D016133:Polymerase Chain Reaction; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases; D017386:Sequence Homology, Amino Acid; D013602:T-Lymphocytes, Cytotoxic / Q000187:drug effects* / Q000378:metabolism; D013737:Testis / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D014158:Transcription, Genetic; D014407:Tumor Cells, Cultured; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism
chemical_list: D017931:DNA Primers; D018076:DNA, Complementary; D007376:Interleukin-2; D047908:Intracellular Signaling Peptides and Proteins; D016159:Tumor Suppressor Protein p53; D011494:Protein Kinases; D017346:Protein Serine-Threonine Kinases; C441644:TP53RK protein, human