PUBLICATION
Characterization of PDZ-binding kinase, a mitotic kinase
- Authors
- Gaudet, S., Branton, D., and Lue, R.A.
- ID
- ZDB-PUB-020513-4
- Date
- 2000
- Source
- Proceedings of the National Academy of Sciences of the United States of America 97(10): 5167-5172 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Adaptor Proteins, Signal Transducing
- Adult
- Amino Acid Sequence
- Animals
- Binding Sites
- Brain/enzymology
- Cell Cycle
- Cell Line
- Drosophila/enzymology
- Female
- Guanylate Kinases
- HeLa Cells
- Humans
- Membrane Proteins
- Mice
- Mitogen-Activated Protein Kinase Kinases
- 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
- PubMed
- 10779557 Full text @ Proc. Natl. Acad. Sci. USA
Citation
Gaudet, S., Branton, D., and Lue, R.A. (2000) Characterization of PDZ-binding kinase, a mitotic kinase. Proceedings of the National Academy of Sciences of the United States of America. 97(10):5167-5172.
Abstract
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping