ArticleEukaryotic cell2006
Mapping of an internal protease cleavage site in the Ssy5p component of the amino acid sensor of Saccharomyces cerevisiae and functional characterization of the resulting pro- and protease domains by gain-of-function genetics.
Article in Eukaryotic cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 27 citations in OpenAlex.
- Structural bases of signal generation and transduction by the SPS amino acid sensor of Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2026Article
- TheInternational journal of molecular sciences · 2023Article
- Spatial and temporal regulation of the endoproteolytic activity of the SPS-sensor-controlled Ssy5 signaling protease.Molecular biology of the cell · 2019Article
- 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
- Nutrient sensing and TOR signaling in yeast and mammals.The EMBO journal · 2017Review
- Proteolytic activation of both components of the cation stress-responsive Slt pathway in Aspergillus nidulans.Molecular biology of the cell · 2016Article
- Rts1-protein phosphatase 2A antagonizes Ptr3-mediated activation of the signaling protease Ssy5 by casein kinase I.Molecular biology of the cell · 2013Article
- Article
- Regulation of amino acid, nucleotide, and phosphate metabolism in Saccharomyces cerevisiae.Genetics · 2012Article
- A phosphodegron controls nutrient-induced proteasomal activation of the signaling protease Ssy5.Molecular biology of the cell · 2011Article
- Amino acid signaling in yeast: activation of Ssy5 protease is associated with its phosphorylation-induced ubiquitylation.The Journal of biological chemistry · 2011Article
- Differential regulation of transcription factors Stp1 and Stp2 in the Ssy1-Ptr3-Ssy5 amino acid sensing pathway.The Journal of biological chemistry · 2011Article
- The prodomain of Ssy5 protease controls receptor-activated proteolysis of transcription factor Stp1.Molecular and cellular biology · 2010Article
- Amino acid transceptors: gate keepers of nutrient exchange and regulators of nutrient signaling.American journal of physiology. Endocrinology and metabolism · 2009Review
- Regulation of peptide import through phosphorylation of Ubr1, the ubiquitin ligase of the N-end rule pathway.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Activation of the SPS amino acid-sensing pathway in Saccharomyces cerevisiae correlates with the phosphorylation state of a sensor component, Ptr3.Molecular and cellular biology · 2008Article
- Regulation of transcription factor latency by receptor-activated proteolysis.Genes & development · 2006Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ssy5p is a 77-kDa protein believed to be a component of the SPS amino acid sensor complex in the plasma membrane of Saccharomyces cerevisiae. Ssy5p has been suggested to be a chymotrypsin-like serine protease that activates the transcription factor Stp1p upon exposure of the yeast to extracellular amino acid. Here we overexpressed and partially purified Ssy5p to improve our understanding of its structure and function. Antibodies against Ssy5p expressed in Escherichia coli were isolated and used to detect Ssy5p processing in S. cerevisiae cells. Partial purification and N-terminal sequencing of processed Ssy5p revealed in vivo cleavage of Ssy5p between amino acids 381 and 382. We also isolated constitutively signaling SSY5 mutants and quantified target promoter activation and Stp1p processing. One mutant contained an amino acid substitution in the prodomain, whereas three others harbored amino acid substitutions in the protease domain. Dose-response analysis indicated that all four mutants exhibited increased basal levels of Stp1p processing. Interestingly, whereas the three constitutive mutants mapping to the protease domain of Ssy5p exhibited the decreased 50% effective concentration (EC(50)) characteristic of constitutive mutations previously found in Ssy1p, Ptr3p, and Ssy5p, the EC(50) of the mutation that maps to the prodomain of Ssy5p remained essentially unchanged. In a model of Ssy5p derived from its similarities with alpha-lytic protease from Lysobacter enzymogenes, the sites corresponding to the mutations in the protease domain are clustered in a region facing the prodomain, suggesting that this region interacts with the prodomain and participates in the conformational dynamics of sensing.
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