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

ABSTRACT: 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.

INSTRUMENT(S):

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Michael Stumpe

LAB HEAD: Joern Dengjel

PROVIDER: PXD069824 | Pride | 2026-01-30

REPOSITORIES: Pride

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			Action	DRS
	20191216_ZH_LD_PPPome_Ctrl_1.raw	Raw
	20191216_ZH_LD_PPPome_Ctrl_2.raw	Raw
	20191216_ZH_LD_PPPome_Ctrl_3.raw	Raw
	20191216_ZH_LD_PPPome_w_Rapa_1.raw	Raw
	20191216_ZH_LD_PPPome_w_Rapa_2.raw	Raw

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