This study investigates the regulatory mechanisms of mRNA translation by mTOR Complex 1 (mTORC1) using high-resolution transcriptome-scale ribosome profiling in cells treated with the mTOR inhibitor Torin1. The results reveal that mTORC1-regulated mRNA translation is primarily controlled by 4E-BP family proteins and eIF4G1, rather than 5' UTR length or complexity. Specifically, mTORC1-dependent translation control is associated with 5' terminal oligopyrimidine (TOP) motifs or related TOP-like motifs. The study also shows that loss of 4E-BP1/2, which inhibits the interaction between eIF4E and eIF4G1, leads to selective suppression of TOP and TOP-like mRNA translation, highlighting the critical role of eIF4G1 in mTORC1-mediated translation regulation. These findings provide a unified model for understanding how mTORC1 differentially controls specific mRNAs.This study investigates the regulatory mechanisms of mRNA translation by mTOR Complex 1 (mTORC1) using high-resolution transcriptome-scale ribosome profiling in cells treated with the mTOR inhibitor Torin1. The results reveal that mTORC1-regulated mRNA translation is primarily controlled by 4E-BP family proteins and eIF4G1, rather than 5' UTR length or complexity. Specifically, mTORC1-dependent translation control is associated with 5' terminal oligopyrimidine (TOP) motifs or related TOP-like motifs. The study also shows that loss of 4E-BP1/2, which inhibits the interaction between eIF4E and eIF4G1, leads to selective suppression of TOP and TOP-like mRNA translation, highlighting the critical role of eIF4G1 in mTORC1-mediated translation regulation. These findings provide a unified model for understanding how mTORC1 differentially controls specific mRNAs.