title: Identification of protein kinase CK2 as a potent kinase of Epstein-Barr virus latent membrane protein 1.
abstract: The C-terminus of latent membrane protein 1 (LMP1) can be phosphorylated in vivo. However, the protein kinase responsible for LMP1 phosphorylation has not yet been identified. In this study, GST fusion proteins containing the C-terminus of LMP1 were generated and used as substrates to survey the kinases that phosphorylate LMP1. Among several purified protein kinases tested, only protein kinase CK2 (CK2) could specifically phosphorylate LMP1. Using the in-gel kinase assay in the absence and presence of a selective CK2 inhibitor, 4,5,6,7-tetrabromobenzotriazole, CK2 was determined to be the major kinase to phosphorylate LMP1 in lymphoma and epithelial cell lines. This is the first study to show that CK2 is a potent kinase to phosphorylate LMP1 in vitro.
authors.affiliation: Department of Medical Technology, Yuan-Pei Institute of Science and Technology, Hsinchu, Taiwan, ROC. lmchi@dns.ymit.edu.tw
authors.forename: Lang-Ming
authors.initials: LM
authors.lastname: Chi
authors.forename: Jau-Song
authors.initials: JS
authors.lastname: Yu
authors.forename: Yu-Sun
authors.initials: YS
authors.lastname: Chang
mesh_terms: D000595:Amino Acid Sequence; D047390:Casein Kinase II; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006801:Humans; D008969:Molecular Sequence Data; D010766:Phosphorylation / Q000187:drug effects; D017346:Protein Serine-Threonine Kinases / Q000032:analysis / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013379:Substrate Specificity; D014230:Triazoles / Q000494:pharmacology; D014407:Tumor Cells, Cultured; D014763:Viral Matrix Proteins / Q000378:metabolism*
chemical_list: C405354:4,5,6,7-tetrabromobenzotriazole; C037662:EBV-associated membrane antigen, Epstein-Barr virus; D004791:Enzyme Inhibitors; D014230:Triazoles; D014763:Viral Matrix Proteins; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases