PTEN is a protein tyrosine phosphatase that acts as a tumor suppressor, as a lipid phosphatase that dephosphorylates the D3 position of phosphatidylinositol 3,4,5-trisphosphate and as an antagonist of the PI3k/AKT signaling pathway (1-3). PTEN structural domains includes an N-terminal phosphatase domain, a lipid binding C2 domain and a 50-amino acid C-terminal tail that contains a PDZ biding sequence. Phosphorylation of the tail suppresses the activity of PTEN by controlling its recruitment into the PTEN-associated complex (4). PTEN is phosphorylated in vitro on Threonine 366 and Serine 370 by glycogen synthase kindase 3 (GSK3) and casein kinase 2 (CK2) respectively. Prior phosphorylation of PTEN at Serine 370 by CK2 strongly increased its phosphorylation at Threonine 366 by GSK3, suggesting that the two may synergize. Generally, phosphorylation in the C-terminal tail of PTEN is thought to enhance stability and to decrease membrane localization and activity. However, phosphorylation at Threonine 366 is linked to destabilization of PTEN (5).
Senescence and Autophagy
* Shipping is in business days
* OriGene provides validated application data and protocol, with money back guarantee.