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Gaudet, S, Branton, D and Lue, RA (2000) Characterization of PDZ-binding kinase, a mitotic kinase. Proc. Natl. Acad. Sci. U.S.A. 97:5167-72
hDlg, the human homologue of the Drosophila Discs-large (Dlg) tumor suppressor protein, is known to interact with the tumor suppressor protein APC and the human papillomavirus E6 transforming protein. In a two-hybrid screen, we identified a 322-aa serine/threonine kinase that binds to the PDZ2 domain of hDlg. The mRNA for this PDZ-binding kinase, or PBK, is most abundant in placenta and absent from adult brain tissue. The protein sequence of PBK has all the characteristic protein kinase subdomains and a C-terminal PDZ-binding T/SXV motif. In vitro, PBK binds specifically to PDZ2 of hDlg through its C-terminal T/SXV motif. PBK and hDlg are phosphorylated at mitosis in HeLa cells, and the mitotic phosphorylation of PBK is required for its kinase activity. In vitro, cdc2/cyclin B phosphorylates PBK. This evidence shows how PBK could link hDlg or other PDZ-containing proteins to signal transduction pathways regulating the cell cycle or cellular proliferation.
Adaptor Proteins, Signal Transducing; Adult; Amino Acid Sequence; Animals; Binding Sites; Brain/enzymology; Cell Cycle; Cell Line; Drosophila/enzymology; Female; Guanylate Kinase; HeLa Cells; Humans; Membrane Proteins; Mice; Molecular Sequence Data; Placenta/enzymology; Pregnancy; Protein-Serine-Threonine Kinases/chemistry; Protein-Serine-Threonine Kinases/genetics; Protein-Serine-Threonine Kinases/metabolism; Proteins/chemistry; Proteins/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Alignment; Sequence Homology, Amino Acid; Spodoptera; Transfection; Zebrafish
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