ArticleThe Journal of cell biology2006
Asi1 is an inner nuclear membrane protein that restricts promoter access of two latent transcription factors.
Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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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.
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Who cites it
30 citing papers in PubMed, 47 citations in OpenAlex.
- Lipid bilayer thinning near a ubiquitin ligase selects ER membrane proteins for degradation.bioRxiv : the preprint server for biology · 2025Article
- Dynamic quality control machinery that operates across compartmental borders mediates the degradation of mammalian nuclear membrane proteins.Cell reports · 2022Article
- Quality control mechanisms that protect nuclear envelope identity and function.The Journal of cell biology · 2022Review
- Amino Acid Sensing and Assimilation by the Fungal PathogenPathogens (Basel, Switzerland) · 2021Review
- Inner-nuclear-membrane-associated degradation employs Dfm1-independent retrotranslocation and alleviates misfolded transmembrane-protein toxicity.Molecular biology of the cell · 2021Article
- Nuclear Ubiquitin-Proteasome Pathways in Proteostasis Maintenance.Biomolecules · 2021Review
- Regulation of inner nuclear membrane associated protein degradation.Nucleus (Austin, Tex.) · 2019Review
- Patrolling the nucleus: inner nuclear membrane-associated degradation.Current genetics · 2019Review
- Ubiquitin-dependent protein degradation at the endoplasmic reticulum and nuclear envelope.Seminars in cell & developmental biology · 2019Review
- Distribution of Proteins at the Inner Nuclear Membrane Is Regulated by the Asi1 E3 Ligase inGenetics · 2019Article
- 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
- Repair or destruction-an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasis.FEBS letters · 2017Review
- Analysis of membrane proteins localizing to the inner nuclear envelope in living cells.The Journal of cell biology · 2016Article
- Spatial control of lipid droplet proteins by the ERAD ubiquitin ligase Doa10.The EMBO journal · 2016Article
- Degradation-mediated protein quality control at the inner nuclear membrane.Nucleus (Austin, Tex.) · 2016Review
- Border Safety: Quality Control at the Nuclear Envelope.Trends in cell biology · 2016Review
- Atypical ubiquitylation in yeast targets lysine-less Asi2 for proteasomal degradation.The Journal of biological chemistry · 2015Article
- Article
- 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Stp1 and Stp2 are homologous transcription factors in yeast that are synthesized as latent cytoplasmic precursors with NH2-terminal regulatory domains. In response to extracellular amino acids, the plasma membrane-localized Ssy1-Ptr3-Ssy5 (SPS) sensor endoproteolytically processes Stp1 and Stp2, an event that releases the regulatory domains. The processed forms of Stp1 and Stp2 efficiently target to the nucleus and bind promoters of amino acid permease genes. In this study, we report that Asi1 is an integral component of the inner nuclear membrane that maintains the latent characteristics of unprocessed Stp1 and Stp2. In cells lacking Asi1, full-length forms of Stp1 and Stp2 constitutively induce SPS sensor-regulated genes. The regulatory domains of Stp1 and Stp2 contain a conserved motif that confers Asi1-mediated control when fused to an unrelated DNA-binding protein. Our results indicate that latent precursor forms of Stp1 and Stp2 inefficiently enter the nucleus; however, once there, Asi1 restricts them from binding SPS sensor-regulated promoters. These findings reveal an unanticipated role of inner nuclear membrane proteins in controlling gene expression.
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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.