- Western Blot
Human, mouse and rat
The T387 antibody was generated using EEGTMKRRDEp-TMQPA as the antigen.
150-200 mL at 1.5-3 mg/mL
Oxidative stress can induce apoptosis through activation of MstI, subsequent phosphorylation of FOXO and nuclear translocation. MstI is a common component of apoptosis initiated by various stresses. MstI kinase activation requires autophosphorylation and proteolytic degradation by caspases. Dr. Ye's group has demonstrated that MstI is a physiological substrate of Akt. Akt phosphorylation of MstI diminishes its apoptotic cleavage by caspases and prevents its kinase activity on FOXO3. MstI directly binds to Akt, which is regulated Akt kinase activity. Akt phosphorylates MstI on the Thr387 residue and protects MstI from apoptotic cleavage in vitro and in apoptotic cells. Furthermore, Akt phosphorylation of MstI strongly inhibits its kinase activity on FOXO3. The findings support that Akt blocks MstI-triggered FOXO3 nuclear translocation by phosphorylating MstI, promoting cell survival.
Publication: Jang et.al., (2007). J. Biol. Chem. 282(42):30836-44.