Matches in Nanopublications for { ?s ?p "We next examined the Akt T-loop Thr308 phosphorylation in wild-type and SIN1-/- cells. We found that although Ser473 phosphorylation was completely abolished in the SIN1-/- cells, Thr308 phosphorylation of Akt was not blocked (Figure 3A). These results indicate that SIN1 is not essential for Akt Thr308 phosphorylation and that the Ser473 phosphorylation is not a prerequisite for Thr308 phosphorylation. Akt, Singly Phosphorylated at Thr308, Remains Active and Functional in Response to Growth Factor Stimulation in SIN1-/- Cells Since Akt Thr308 phosphorylation was not dependent on Ser473 phosphorylation in SIN1-/- cells, we then asked whether this Thr308 singly phosphorylated Akt is still active and whether lack of Ser473 phosphorylation would have a global effect on the phosphorylation of Akt targets. Using an in vitro kinase assay, we found that Akt retained a substantial amount of enzymatic activity in SIN1-/- cells, although lower than that in wild-type cells (Figure 3B). Thus, singly phosphorylated (Thr308) Akt is an active but weaker enzyme." ?g. }
Showing items 1 to 2 of
2
with 100 items per page.
- _5 value "We next examined the Akt T-loop Thr308 phosphorylation in wild-type and SIN1-/- cells. We found that although Ser473 phosphorylation was completely abolished in the SIN1-/- cells, Thr308 phosphorylation of Akt was not blocked (Figure 3A). These results indicate that SIN1 is not essential for Akt Thr308 phosphorylation and that the Ser473 phosphorylation is not a prerequisite for Thr308 phosphorylation. Akt, Singly Phosphorylated at Thr308, Remains Active and Functional in Response to Growth Factor Stimulation in SIN1-/- Cells Since Akt Thr308 phosphorylation was not dependent on Ser473 phosphorylation in SIN1-/- cells, we then asked whether this Thr308 singly phosphorylated Akt is still active and whether lack of Ser473 phosphorylation would have a global effect on the phosphorylation of Akt targets. Using an in vitro kinase assay, we found that Akt retained a substantial amount of enzymatic activity in SIN1-/- cells, although lower than that in wild-type cells (Figure 3B). Thus, singly phosphorylated (Thr308) Akt is an active but weaker enzyme." provenance.
- _5 value "We next examined the Akt T-loop Thr308 phosphorylation in wild-type and SIN1-/- cells. We found that although Ser473 phosphorylation was completely abolished in the SIN1-/- cells, Thr308 phosphorylation of Akt was not blocked (Figure 3A). These results indicate that SIN1 is not essential for Akt Thr308 phosphorylation and that the Ser473 phosphorylation is not a prerequisite for Thr308 phosphorylation. Akt, Singly Phosphorylated at Thr308, Remains Active and Functional in Response to Growth Factor Stimulation in SIN1-/- Cells Since Akt Thr308 phosphorylation was not dependent on Ser473 phosphorylation in SIN1-/- cells, we then asked whether this Thr308 singly phosphorylated Akt is still active and whether lack of Ser473 phosphorylation would have a global effect on the phosphorylation of Akt targets. Using an in vitro kinase assay, we found that Akt retained a substantial amount of enzymatic activity in SIN1-/- cells, although lower than that in wild-type cells (Figure 3B). Thus, singly phosphorylated (Thr308) Akt is an active but weaker enzyme." provenance.