Our data suggest that in cancer cells, AKT and mTORC1 cooperate to maintain phosphorylation of PRAS40, which in turn, relieves PRAS40-inhibitory constraint on mTORC1 activity; the activated mTORC1 supports cap-dependent translation by phosphorylation of 4E-BP1 and promotes cell growth and motility. This evidence concerns the gene EIF4EBP1 and cancer.