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PMID:11035045
| Citation |
Torres, J and Pulido, R (2001) The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation. J. Biol. Chem. 276:993-8 |
|---|---|
| Abstract |
The tumor suppressor phosphatase PTEN regulates cell migration, growth, and survival by dephosphorylating phosphatidylinositol second messengers and signaling phosphoproteins. PTEN possesses a C-terminal noncatalytic regulatory domain that contains multiple putative phosphorylation sites, which could play an important role in the control of its biological activity. The protein kinase CK2 phosphorylated, in a constitutive manner, a cluster of Ser/Thr residues located at the PTEN C terminus. PTEN-phosphorylated defective mutants showed decreased stability in comparison with wild type PTEN and were more rapidly degraded by the proteasome. Inhibition of PTEN phosphorylation by the CK2 inhibitor 5,6-dichloro-1-beta-d-ribofuranosyl-benzimidazole also diminished the PTEN protein content. Our results support the notion that proper phosphorylation of PTEN by CK2 is important for PTEN protein stability to proteasome-mediated degradation. |
| Links |
PubMed Online version:10.1074/jbc.M009134200 |
| Keywords |
Amino Acid Sequence; Breast Neoplasms; Casein Kinase II; Cloning, Molecular; Consensus Sequence; Cysteine Endopeptidases/metabolism; Enzyme Stability; Female; Genes, Tumor Suppressor; Humans; Kinetics; Multienzyme Complexes/metabolism; Mutagenesis; PTEN Phosphohydrolase; Phosphoproteins/chemistry; Phosphoproteins/metabolism; Phosphoric Monoester Hydrolases/chemistry; Phosphoric Monoester Hydrolases/genetics; Phosphoric Monoester Hydrolases/metabolism; Phosphorylation; Proteasome Endopeptidase Complex; Protein-Serine-Threonine Kinases/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Deletion; Transfection; Tumor Suppressor Proteins |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004674: protein serine/threonine kinase activity |
ECO:0000315: |
F |
Figure three shows CK2 phosphorylates the C terminus of PTEN. |
complete | ||||
|
enables |
GO:0004674: protein serine/threonine kinase activity |
ECO:0000315: mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
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