ArticleThe Journal of biological chemistry2014
Nuclear import factor Srp1 and its associated protein Sts1 couple ribosome-bound nascent polypeptides to proteasomes for cotranslational degradation.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1.Scientific reports · 2024Article
- Homeostatic regulation of ribosomal proteins by ubiquitin-independent cotranslational degradation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Genotypic, proteomic, and phenotypic approaches to decipher the response to caspofungin and calcineurin inhibitors in clinical isolates of echinocandin-resistant Candida glabrata.The Journal of antimicrobial chemotherapy · 2022Article
- Oxysterol-binding protein-like 2 contributes to the developmental progression of preadipocytes by binding to β-catenin.Cell death discovery · 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
- Transcriptomic analysis ofF1000Research · 2017Article
- Rapidly Translated Polypeptides Are Preferred Substrates for Cotranslational Protein Degradation.The Journal of biological chemistry · 2016Article
- Nuclear transport of yeast proteasomes.Biomolecules · 2014Review
- A nuclear ubiquitin-proteasome pathway targets the inner nuclear membrane protein Asi2 for degradation.Journal of cell science · 2014Article
- Translating DRiPs: MHC class I immunosurveillance of pathogens and tumors.Journal of leukocyte biology · 2014Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cotranslational protein degradation plays an important role in protein quality control and proteostasis. Although ubiquitylation has been suggested to signal cotranslational degradation of nascent polypeptides, cotranslational ubiquitylation occurs at a low level, suggesting the existence of an alternative route for delivery of nascent polypeptides to the proteasome. Here we report that the nuclear import factor Srp1 (also known as importin α or karyopherin α) is required for ubiquitin-independent cotranslational degradation of the transcription factor Rpn4. We further demonstrate that cotranslational protein degradation is generally impaired in the srp1-49 mutant. Srp1 binds nascent polypeptides emerging from the ribosome. The association of proteasomes with polysomes is weakened in srp1-49. The interaction between Srp1 and the proteasome is mediated by Sts1, a multicopy suppressor of srp1-49. The srp1-49 and sts1-2 mutants are hypersensitive to stressors that promote protein misfolding, underscoring the physiological function of Srp1 and Sts1 in degradation of misfolded nascent polypeptides. This study unveils a previously unknown role for Srp1 and Sts1 in cotranslational protein degradation and suggests a novel model whereby Srp1 and Sts1 cooperate to couple proteasomes to ribosome-bound nascent polypeptides.
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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.