ArticleGenes & development2006
Regulation of transcription factor latency by receptor-activated proteolysis.
Article in Genes & development, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
38 citing papers in PubMed, 62 citations in OpenAlex.
- Structural bases of signal generation and transduction by the SPS amino acid sensor of Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2026Article
- 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
- The histone chaperone HIR maintains chromatin states to control nitrogen assimilation and fungal virulence.Cell reports · 2021Article
- Patrolling the nucleus: inner nuclear membrane-associated degradation.Current genetics · 2019Review
- Spatial and temporal regulation of the endoproteolytic activity of the SPS-sensor-controlled Ssy5 signaling protease.Molecular biology of the cell · 2019Article
- Nutrient and Stress Sensing in Pathogenic Yeasts.Frontiers in microbiology · 2019Review
- Ssy5 is a signaling serine protease that exhibits atypical biogenesis and marked S1 specificity.The Journal of biological chemistry · 2018Article
- Regulation of Sensing, Transportation, and Catabolism of Nitrogen Sources in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2018Review
- Nutrient Sensing at the Plasma Membrane of Fungal Cells.Microbiology spectrum · 2017Review
- Nutrient sensing and TOR signaling in yeast and mammals.The EMBO journal · 2017Review
- An agonist antibody that blocks autoimmunity by inducing anti-inflammatory macrophages.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Article
- Less is more: Nutrient limitation induces cross-talk of nutrient sensing pathways with NADFrontiers in biology · 2015Article
- Reduced Ssy1-Ptr3-Ssy5 (SPS) signaling extends replicative life span by enhancing NAD+ homeostasis in Saccharomyces cerevisiae.The Journal of biological chemistry · 2015Article
- Review
- Latency of transcription factor Stp1 depends on a modular regulatory motif that functions as cytoplasmic retention determinant and nuclear degron.Molecular biology of the cell · 2014Article
- Functional characterisation of Arabidopsis SPL7 conserved protein domains suggests novel regulatory mechanisms in the Cu deficiency response.BMC plant biology · 2014Article
- A nuclear ubiquitin-proteasome pathway targets the inner nuclear membrane protein Asi2 for degradation.Journal of cell science · 2014Article
- Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae.FEMS microbiology reviews · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transcription factor Stp1 is endoproteolytically processed in response to extracellular amino acids by the plasma membrane SPS (Ssy1-Ptr3-Ssy5)-sensor. Processed Stp1, lacking a cytoplasmic retention motif, enters the nucleus and induces amino acid transporter gene expression. The SPS-sensor component Ssy5 is a chymotrypsin-like protease with a Pro-domain and a catalytic domain. The Pro-domain, required for protease maturation, is autolytically cleaved from the catalytic domain but remains associated, forming an inactive protease complex that binds Stp1. Stp1 is processed only after amino acid-induced signals cause the dissociation of the inhibitory Pro-domain. Our findings demonstrate that gene expression can be controlled by regulating the enzymatic activity of an intracellular endoprotease.
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What OpenQuestion holds
Registered trials
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.