ArticleEukaryotic cell2009
Distinct subsets of Sit4 holophosphatases are required for inhibition of Saccharomyces cerevisiae growth by rapamycin and zymocin.
Article in Eukaryotic cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- The nitrogen starvation-induced inhibitor Rts3 restrains Sit4/PP6 to gate quiescence downstream of TORC1.Nature communications · 2026Article
- Ser/Thr protein phosphatases in fungi: structure, regulation and function.Microbial cell (Graz, Austria) · 2019Review
- Roles of Elongator Dependent tRNA Modification Pathways in Neurodegeneration and Cancer.Genes · 2018Review
- Protein Phosphatase Sit4 Affects Lipid Droplet Synthesis and Soraphen A Resistance Independent of Its Role in Regulating Elongator Dependent tRNA Modification.Biomolecules · 2018Article
- Sit4-Associated Protein is Required for Pathogenicity of Leptosphaeria maculans on Brassica napus.Current microbiology · 2017Article
- Use of a Yeast tRNase Killer Toxin to Diagnose Kti12 Motifs Required for tRNA Modification by Elongator.Toxins · 2017Article
- Independent suppression of ribosomal +1 frameshifts by different tRNA anticodon loop modifications.RNA biology · 2017Article
- Wobble uridine modifications-a reason to live, a reason to die?!RNA biology · 2017Review
- Glutaredoxin GRXS17 Associates with the Cytosolic Iron-Sulfur Cluster Assembly Pathway.Plant physiology · 2016Article
- Loss of anticodon wobble uridine modifications affects tRNA(Lys) function and protein levels in Saccharomyces cerevisiae.PloS one · 2015Article
- The emerging role of complex modifications of tRNAMicrobial cell (Graz, Austria) · 2015Article
- Loss of wobble uridine modification in tRNA anticodons interferes with TOR pathway signaling.Microbial cell (Graz, Austria) · 2014Article
- A novel Sit4 phosphatase complex is involved in the response to ceramide stress in yeast.Oxidative medicine and cellular longevity · 2013Article
- Translational control of cell division by Elongator.Cell reports · 2012Article
- Cell-free reconstitution of vacuole membrane fragmentation reveals regulation of vacuole size and number by TORC1.Molecular biology of the cell · 2012Article
- Article
- A new fluorescence-based method identifies protein phosphatases regulating lipid droplet metabolism.PloS one · 2010Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein phosphatase Sit4 is required for growth inhibition of Saccharomyces cerevisiae by the antifungals rapamycin and zymocin. Here, we show that the rapamycin effector Tap42, which interacts with Sit4, is dispensable for zymocin action. Although Tap42 binding-deficient sit4 mutants are resistant to zymocin, these mutations also block interaction between Sit4 and the Sit4-associating proteins Sap185 and Sap190, previously shown to mediate zymocin toxicity. Among the four different SAP genes, we found that SAP190 deletions specifically induce rapamycin resistance but that this phenotype is reversed in the additional absence of SAP155. Similarly, the rapamycin resistance of an rrd1Delta mutant lacking the Sit4 interactor Rrd1 specifically requires the Sit4/Sap190 complex. Thus, Sit4/Sap190 and Sit4/Sap155 holophosphatases apparently play opposing roles following rapamycin treatment, although rapamycin inhibition is operational in the absence of all Sap family members or Sit4. We further identified a Sit4-interacting region on Sap185 in sap190Delta cells that mediates Sit4/Sap185 complex formation and is essential for dephosphorylation of Elp1, a subunit of the Elongator complex. This suggests that Sit4/Sap185 and Sit4/Sap190 holophosphatases promote Elongator functions, a notion supported by data showing that their inactivation eliminates Elongator-dependent processes, including tRNA suppression by SUP4 and tRNA cleavage by zymocin.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.