ArticleNature communications2026
The nitrogen starvation-induced inhibitor Rts3 restrains Sit4/PP6 to gate quiescence downstream of TORC1.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Cellular quiescence is a reversible state essential for survival under nutrient-limiting or growth-restrictive conditions, yet the mechanisms fine-tuning its depth and reversibility remain elusive. Here, we identify Saccharomyces cerevisiae Rts3 as a regulator of the quiescence trajectory downstream of TORC1. Using phosphatase inhibitor beads and mass spectrometry, we characterize Rts3 as a phosphatase interactor in rapamycin-treated cells and define it as an inhibitor of the PP6 phosphatase Sit4. Mechanistically, it employs an α-helix to dock directly into the Sit4-Sap185/190 catalytic cleft. Transcriptionally induced by Gln3/Gat1 during nitrogen starvation, Rts3 is rapidly degraded upon nutrient repletion via a TORC1-SCF
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