ArticleMolecular and cellular biology2000
Evidence for separable functions of Srp1p, the yeast homolog of importin alpha (Karyopherin alpha): role for Srp1p and Sts1p in protein degradation.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Spatial mechanisms of quality control during chaperone-mediated assembly of the proteasome.Nature communications · 2025Article
- Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1.Scientific reports · 2024Article
- Localized Proteasomal Degradation: From the Nucleus to Cell Periphery.Biomolecules · 2022Review
- Nuclear-capture of endosomes depletes nuclear G-actin to promote SRF/MRTF activation and cancer cell invasion.Nature communications · 2021Article
- 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
- Nuclear Transport of Yeast Proteasomes.Frontiers in molecular biosciences · 2019Review
- Importin α: functions as a nuclear transport factor and beyond.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2018Review
- 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
- Nuclear Import of Yeast Proteasomes.Cells · 2015Review
- Neurospora importin α is required for normal heterochromatic formation and DNA methylation.PLoS genetics · 2015Article
- Cell cycle-independent phospho-regulation of Fkh2 during hyphal growth regulates Candida albicans pathogenesis.PLoS pathogens · 2015Article
- Yeast importin-α (Srp1) performs distinct roles in the import of nuclear proteins and in targeting proteasomes to the nucleus.The Journal of biological chemistry · 2014Article
- Nuclear transport of yeast proteasomes.Biomolecules · 2014Review
- Nuclear import factor Srp1 and its associated protein Sts1 couple ribosome-bound nascent polypeptides to proteasomes for cotranslational degradation.The Journal of biological chemistry · 2014Article
- Identification of Novel Stress Granule Components That Are Involved in Nuclear Transport.PloS one · 2013Article
- Aggregation of human S100A8 and S100A9 amyloidogenic proteins perturbs proteostasis in a yeast model.PloS one · 2013Article
- Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates.Molecular biology of the cell · 2012Article
- Nuclear retention of importin α coordinates cell fate through changes in gene expression.The EMBO journal · 2012Article
- Time-course proteome analysis reveals the dynamic response of Cryptococcus gattii cells to fluconazole.PloS one · 2012Article
- Sts1 plays a key role in targeting proteasomes to the nucleus.The Journal of biological chemistry · 2011Article
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4 authors.
Funding
Abstract
Srp1p (importin alpha) functions as the nuclear localization signal (NLS) receptor in Saccharomyces cerevisiae. The srp1-31 mutant is defective in this nuclear localization function, whereas an srp1-49 mutant exhibits defects that are unrelated to this localization function, as was confirmed by intragenic complementation between the two mutants. RPN11 and STS1 (DBF8) were identified as high-dosage suppressors of the srp1-49 mutation but not of the srp1-31 mutation. We found that Sts1p interacts directly with Srp1p in vitro and also in vivo, as judged by coimmunoprecipitation and two-hybrid analyses. Mutants of Sts1p that cannot interact with Srp1p are incapable of suppressing srp1-49 defects, strongly suggesting that Sts1p functions in a complex with Srp1p. STS1 also interacted with the second suppressor, RPN11, a subunit of the 26S proteasome, in the two-hybrid system. Further, degradation of Ub-Pro-beta-galactosidase, a test substrate for the ubiquitin-proteasome system, was defective in srp1-49 but not in srp1-31. This defect in protein degradation was alleviated by overexpression of either RPN11 or STS1 in srp1-49. These results suggest a role for Srp1p in regulation of protein degradation separate from its well-established role as the NLS receptor.
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