ArticleJournal of cell science2014
A nuclear ubiquitin-proteasome pathway targets the inner nuclear membrane protein Asi2 for degradation.
Article in Journal of cell science, 2014. 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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Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- Ubiquitin Ligase Redundancy and Nuclear-Cytoplasmic Localization in Yeast Protein Quality Control.Biomolecules · 2021Review
- Nuclear envelope budding is a response to cellular stress.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- 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
- Protein quality control in the endoplasmic reticulum.Current opinion in cell biology · 2020Review
- Ubiquitin-proteasome-mediated cyclin C degradation promotes cell survival following nitrogen starvation.Molecular biology of the cell · 2020Article
- Quality Control of Protein Complex Assembly by a Transmembrane Recognition Factor.Molecular cell · 2020Article
- Endoplasmic reticulum stress differentially inhibits endoplasmic reticulum and inner nuclear membrane protein quality control degradation pathways.The Journal of biological chemistry · 2019Article
- Regulation of inner nuclear membrane associated protein degradation.Nucleus (Austin, Tex.) · 2019Review
- Patrolling the nucleus: inner nuclear membrane-associated degradation.Current genetics · 2019Review
- Distribution of Proteins at the Inner Nuclear Membrane Is Regulated by the Asi1 E3 Ligase inGenetics · 2019Article
- In vitro expression and functional characterization of NPA motifs in aquaporins of Nosema bombycis.Parasitology research · 2018Article
- 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
- E4-Ubiquitin ligase Ufd2 stabilizes Yap8 and modulates arsenic stress responses independent of the U-box motif.Biology open · 2015Article
- Atypical ubiquitylation in yeast targets lysine-less Asi2 for proteasomal degradation.The Journal of biological chemistry · 2015Article
- Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The nuclear envelope consists of inner and outer nuclear membranes. Whereas the outer membrane is an extension of the endoplasmic reticulum, the inner nuclear membrane (INM) represents a unique membranous environment containing specific proteins. The mechanisms of integral INM protein degradation are unknown. Here, we investigated the turnover of Asi2, an integral INM protein in Saccharomyces cerevisiae. We report that Asi2 is degraded by the proteasome independently of the vacuole and that it exhibited a half-life of ∼45 min. Asi2 exhibits enhanced stability in mutants lacking the E2 ubiquitin conjugating enzymes Ubc6 or Ubc7, or the E3 ubiquitin ligase Doa10. Consistent with these data, Asi2 is post-translationally modified by poly-ubiquitylation in a Ubc7- and Doa10-dependent manner. Importantly Asi2 degradation is significantly reduced in a sts1-2 mutant that fails to accumulate proteasomes in the nucleus, indicating that Asi2 is degraded in the nucleus. Our results reveal a molecular pathway that affects the stability of integral proteins of the inner nuclear membrane and indicate that Asi2 is subject to protein quality control in the nucleus.
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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.