IndraLab

Statements

PI3K binds PI3K_p85 and KCNH2. 3 / 3
| 3
sparser
"Furthermore, by sequestering the channel in the closed conformation, Cla inhibited the formation of a macromolecular complex between hERG1 and the p85 subunit of PI3K. This strongly reduced Akt phosphorylation, and stimulated the p53-dependent cell apoptosis, as witnessed by late caspase activation."
32123164
sparser
"These data indicate that Cla affects the PI3K/Akt pathway by impairing the functional interaction between hERG1 and the p85 subunit of PI3K, and that these effects are different from those exerted by hERG1 blockers."
32123164
sparser
"Furthermore, by sequestering the channel in the closed conformation, Cla inhibited the formation of a macromolecular complex between hERG1 and the p85 subunit of PI3K. This strongly reduced Akt phosphorylation, and stimulated the p53-dependent cell apoptosis, as witnessed by late caspase activation."
32123164