ArticleThe Journal of biological chemistry2011
Sts1 plays a key role in targeting proteasomes to the nucleus.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 48 citations in OpenAlex.
- A multivalent adaptor mechanism drives the nuclear import of proteasomes.Nature communications · 2026Article
- Proteasome dynamics in response to metabolic changes.Frontiers in cell and developmental biology · 2025Review
- Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1.Scientific reports · 2024Article
- AKIR-1 regulates proteasome subcellular function iniScience · 2023Article
- Nuclear and cytoplasmic spatial protein quality control is coordinated by nuclear-vacuolar junctions and perinuclear ESCRT.Nature cell biology · 2023Article
- Localized Proteasomal Degradation: From the Nucleus to Cell Periphery.Biomolecules · 2022Review
- Emerging Connections between Nuclear Pore Complex Homeostasis and ALS.International journal of molecular sciences · 2022Review
- Nuclear destruction: A suicide mission by AKIRIN2 brings intact proteasomes into the nucleus.Molecular cell · 2022Article
- Inner-nuclear-membrane-associated degradation employs Dfm1-independent retrotranslocation and alleviates misfolded transmembrane-protein toxicity.Molecular biology of the cell · 2021Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- The Sts1 nuclear import adapter uses a non-canonical bipartite nuclear localization signal and is directly degraded by the proteasome.Journal of cell science · 2020Article
- Patrolling the nucleus: inner nuclear membrane-associated degradation.Current genetics · 2019Review
- Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation.Frontiers in molecular biosciences · 2019Review
- Nuclear Transport of Yeast Proteasomes.Frontiers in molecular biosciences · 2019Review
- Proteasomes tether to two distinct sites at the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Catalytically Active Proteasomes Function Predominantly in the Cytosol.The Journal of biological chemistry · 2016Article
- Endoplasmic Reticulum-associated Degradation of Pca1p, a Polytopic Protein, via Interaction with the Proteasome at the Membrane.The Journal of biological chemistry · 2016Article
- Deubiquitinase USP2a Sustains Interferons Antiviral Activity by Restricting Ubiquitination of Activated STAT1 in the Nucleus.PLoS pathogens · 2016Article
- Nuclear Import of Yeast Proteasomes.Cells · 2015Review
- Nucleocytoplasmic transport in the midzone membrane domain controls yeast mitotic spindle disassembly.The Journal of cell biology · 2015Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The evidence that nuclear proteins can be degraded by cytosolic proteasomes has received considerable experimental support. However, the presence of proteasome subunits in the nucleus also suggests that protein degradation could occur within this organelle. We determined that Sts1 can target proteasomes to the nucleus and facilitate the degradation of a nuclear protein. Specific sts1 mutants showed reduced nuclear proteasomes at the nonpermissive temperature. In contrast, high expression of Sts1 increased the levels of nuclear proteasomes. Sts1 targets proteasomes to the nucleus by interacting with Srp1, a nuclear import factor that binds nuclear localization signals. Deletion of the NLS in Sts1 prevented its interaction with Srp1 and caused proteasome mislocalization. In agreement with this observation, a mutation in Srp1 that weakened its interaction with Sts1 also reduced nuclear targeting of proteasomes. We reported that Sts1 could suppress growth and proteolytic defects of rad23Δ rpn10Δ. We show here that Sts1 suppresses a previously undetected proteasome localization defect in this mutant. Taken together, these findings explain the suppression of rad23Δ rpn10Δ by Sts1 and suggest that the degradation of nuclear substrates requires efficient proteasome localization.
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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.