[HTML][HTML] Control of Ser2448 phosphorylation in the mammalian target of rapamycin by insulin and skeletal muscle load
TH Reynolds, SC Bodine, JC Lawrence - Journal of Biological Chemistry, 2002 - ASBMB
We have investigated the effects of insulin, amino acids, and the degree of muscle loading
on the phosphorylation of Ser 2448, a site in the mammalian target of rapamycin (mTOR)
phosphorylated by protein kinase B (PKB) in vitro. Phosphorylation was assessed by
immunoblotting with a phosphospecific antibody (anti-Ser (P) 2448) and with mTAb1, an
activating antibody whose binding is inhibited by phosphorylation in the region of mTOR that
contains Ser 2448. Incubating rat diaphragm muscles with insulin increased Ser 2448 …
on the phosphorylation of Ser 2448, a site in the mammalian target of rapamycin (mTOR)
phosphorylated by protein kinase B (PKB) in vitro. Phosphorylation was assessed by
immunoblotting with a phosphospecific antibody (anti-Ser (P) 2448) and with mTAb1, an
activating antibody whose binding is inhibited by phosphorylation in the region of mTOR that
contains Ser 2448. Incubating rat diaphragm muscles with insulin increased Ser 2448 …