The TORC1-regulated quiescence trajectory is shaped by an Rts3-dependent feedback mechanism that limits Sit4/PP6 phosphatase activity

Four sets of MS-based proteomics experiments were performed: (1) Serine/Threonine protein phosphatases were profiled by microcystin-LR (MCLR)-based enrichment in different growth conditions; (2) TurboID-RTS3-based proximity labeling was performed to characterize the RTS3 protein neighborhood; (3) A global phosphoproteome was acquired to identify Rts3-regulated phosphosites, measuring both enriched phosphopetides and FT to determine protein abundances; (4) Expression proteomics of WT, sit4delta, rts3delta and sit4delta/rts3delta cells in different growth conditions to determine the role of Sit4 and Rts3 in regulating protein abundances.