Characterization of PDZ-binding kinase, a mitotic kinase.

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.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Adult, Amino Acid Sequence, Animals, Binding Sites, Brain, Cell Cycle, Cell Line, Discs Large Homolog 1 Protein, Drosophila, Female, Guanylate Kinases, HeLa Cells, Humans, Membrane Proteins, Mice, Mitogen-Activated Protein Kinase Kinases, Molecular Sequence Data, Placenta, Pregnancy, Protein Serine-Threonine Kinases, Proteins, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Spodoptera, Transfection, Zebrafish
Proc Natl Acad Sci U S A
Date: May. 09, 2000
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