ArticleMolecular and cellular biology2004
Amino acid signaling in yeast: casein kinase I and the Ssy5 endoprotease are key determinants of endoproteolytic activation of the membrane-bound Stp1 transcription factor.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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47 citing papers in PubMed, 75 citations in OpenAlex.
- Structural bases of signal generation and transduction by the SPS amino acid sensor of Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2026Article
- Organic matter degradation by oceanic fungi differs between polar and non-polar waters.Nature communications · 2025Article
- A dual reporter system for intracellular and extracellular amino acid sensing in budding yeast.Molecular biology of the cell · 2025Article
- TheInternational journal of molecular sciences · 2023Article
- Contribution of proteases to the hallmarks of aging and to age-related neurodegeneration.Aging cell · 2022Review
- Regulation of Amino Acid Transport in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2019Review
- Origins of peptidases.Biochimie · 2019Article
- Spatial and temporal regulation of the endoproteolytic activity of the SPS-sensor-controlled Ssy5 signaling protease.Molecular biology of the cell · 2019Article
- Regulation of Sensing, Transportation, and Catabolism of Nitrogen Sources in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2018Review
- Ssy5 is a signaling serine protease that exhibits atypical biogenesis and marked S1 specificity.The Journal of biological chemistry · 2018Article
- Fungal lifestyle reflected in serine protease repertoire.Scientific reports · 2017Article
- Casein Kinase I Isoform Hrr25 Is a Negative Regulator of Haa1 in the Weak Acid Stress Response Pathway in Saccharomyces cerevisiae.Applied and environmental microbiology · 2017Article
- Identification of Genes inG3 (Bethesda, Md.) · 2017Article
- Nutrient sensing and TOR signaling in yeast and mammals.The EMBO journal · 2017Review
- The SPS amino acid sensor mediates nutrient acquisition and immune evasion in Candida albicans.Cellular microbiology · 2016Article
- An Arginine Deprivation Response Pathway Is Induced in Leishmania during Macrophage Invasion.PLoS pathogens · 2016Article
- A second component of the SltA-dependent cation tolerance pathway in Aspergillus nidulans.Fungal genetics and biology : FG & B · 2015Article
- Review
- Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae.FEMS microbiology reviews · 2014Review
- Rts1-protein phosphatase 2A antagonizes Ptr3-mediated activation of the signaling protease Ssy5 by casein kinase I.Molecular biology of the cell · 2013Article
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Saccharomyces cerevisiae cells possess a plasma membrane sensor able to detect the presence of extracellular amino acids and then to activate a signaling pathway leading to transcriptional induction of multiple genes, e.g., AGP1, encoding an amino acid permease. This sensing function requires the permease-like Ssy1 and associated Ptr3 and Ssy5 proteins, all essential to activation, by endoproteolytic processing, of the membrane-bound Stp1 transcription factor. The SCF(Grr1) ubiquitin-ligase complex is also essential to AGP1 induction, but its exact role in the amino acid signaling pathway remains unclear. Here we show that Stp1 undergoes casein kinase I-dependent phosphorylation. In the yck mutant lacking this kinase, Stp1 is not cleaved and AGP1 is not induced in response to amino acids. Furthermore, we provide evidence that Ssy5 is the endoprotease responsible for Stp1 processing. Ssy5 is significantly similar to serine proteases, its self-processing is a prerequisite for Stp1 cleavage, and its overexpression causes inducer-independent Stp1 cleavage and high-level AGP1 transcription. We further show that Stp1 processing also requires the SCF(Grr1) complex but is insensitive to proteasome inhibition. However, Stp1 processing does not require SCF(Grr1), Ssy1, or Ptr3 when Ssy5 is overproduced. Finally, we describe the properties of a particular ptr3 mutant that suggest that Ptr3 acts with Ssy1 in amino acid detection and signal initiation. We propose that Ssy1 and Ptr3 form the core components of the amino acid sensor. Upon detection of external amino acids, Ssy1-Ptr3 likely allows-in a manner dependent on SCF(Grr1)-the Ssy5 endoprotease to gain access to and to cleave Stp1, this requiring prior phosphorylation of Stp1 by casein kinase I.
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