!Name=CEN_Sch9_DDEEE_ALL !ExptSetNo=5224 !Description=The Target Of Rapamycin (TOR) protein is a Ser/Thr kinase that functions in two distinct multiprotein complexes: TORC1 and TORC2. These conserved complexes regulate many different aspects of cell growth in response to intra- and extracellular cues. Here we report the first bona fide substrate of yeast TORC1: the AGC-kinase Sch9. Six amino acids in the c-terminus of Sch9 are directly phosphorylated by TORC1. Phosphorylation of these residues is lost upon rapamycin-treatment as well as carbon- or nitrogen-starvation and transiently reduced following application of osmotic, oxidative or thermal stress. TORC1-dependent phosphorylation is required for Sch9 activity and replacement of residues phosphorylated by TORC1 with Asp/Glu renders Sch9 activity TORC1-independent. Sch9 is required for TORC1 to properly regulate ribosome biogenesis, translation initiation and entry into G0 phase, but not expression of Gln3-dependent genes. Our results suggest that Sch9 functions analogously to the mammalian TORC1 substrate S6K1 rather than the mTORC2 substrate PKB/akt. !Name=CEN_20MIN !Exptid=104503 !Name=CEN_30MIN !Exptid=104504 !Name=CEN_60MIN !Exptid=104724 !Name=CEN_90MIN !Exptid=104726 !Name=CEN_120MIN !Exptid=104728 !Name=CEN_180MIN !Exptid=104730 !Name=CEN_SCH9_20MIN !Exptid=104507 !Name=CEN_SCH9_30MIN !Exptid=104508 !Name=CEN_SCH9_60MIN !Exptid=104738 !Name=CEN_SCH9_90MIN !Exptid=104739 !Name=CEN_SCH9_120MIN !Exptid=104740 !Name=CEN_SCH9_180MIN !Exptid=104741 !Name=CEN_SCH9(DE)_20MIN !Exptid=104505 !Name=CEN_SCH9(DE)_30MIN !Exptid=104506 !Name=CEN_SCH9(DE)_90MIN !Exptid=104735 !Name=CEN_SCH9(DE)_120MIN !Exptid=104736 !Name=CEN_SCH9(DE)_180MIN !Exptid=104737