The Tumor Suppressor PTEN Is Phosphorylated by the Protein Kinase CK2 at Its C Terminus: IMPLICATIONS FOR PTEN STABILITY TO PROTEASOME-MEDIATED DEGRADATION

Loading...
Thumbnail Image
Publication date
2001
Reading date
Journal Title
Journal ISSN
Volume Title
Publisher
Metrics
Export
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-β-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.
Description
Bibliographic reference
Torres Ibáñez, José Manuel Pulido Murillo, Rafael 2001 The Tumor Suppressor PTEN Is Phosphorylated by the Protein Kinase CK2 at Its C Terminus: IMPLICATIONS FOR PTEN STABILITY TO PROTEASOME-MEDIATED DEGRADATION Journal of Biological Chemistry 276 2 993 998