ArticleMolecular cell2014
Dss1 is a 26S proteasome ubiquitin receptor.
Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
What it found
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Who cites it
61 citing papers in PubMed, 95 citations in OpenAlex.
- The Arabidopsis Mutant of the Small Intrinsically Disordered Protein DSS1(V) Exhibits Increased Sensitivity to Drought Stress.Plant direct · 2026Article
- Structural basis of K11/K48-branched ubiquitin chain recognition by the human 26S proteasome.Nature communications · 2025Article
- DSS1 inhibits autophagy to activate epithelial-mesenchymal transition in a pro-metastatic niche of renal cell carcinoma.Nature communications · 2025Article
- DSS1 is required for proper Integrator-PP2A function.Nature communications · 2025Article
- The deubiquitinase Rpn11 functions as an allosteric ubiquitin sensor to promote substrate engagement by the 26S proteasome.Cell reports · 2025Article
- Comparative physiological and cytological analysis, and omics approach provide clues to the coloring mechanism of the pumpkin yellow stems.BMC plant biology · 2025Article
- SP1 promotes triple-negative breast cancer progression by targeting USP5.Cancer cell international · 2025Article
- Locating Polyubiquitin Receptors on the 19S Regulatory Proteasome ofJournal of the American Society for Mass Spectrometry · 2025Article
- Assessing Transcriptomic Responses to Oxidative Stress: Contrasting Wild-Type Arabidopsis Seedlings withInternational journal of molecular sciences · 2024Article
- Analysis of the indispensable RAD51 cofactor BRCA2 inLife science alliance · 2024Article
- Phosphorylation of Schizosaccharomyces pombe Dss1 mediates direct binding to the ubiquitin-ligase Dma1 in vitro.Protein science : a publication of the Protein Society · 2023Article
- Lysine deserts prevent adventitious ubiquitylation of ubiquitin-proteasome components.Cellular and molecular life sciences : CMLS · 2023Article
- Deciphering the Alphabet of Disorder-Glu and Asp Act Differently on Local but Not Global Properties.Biomolecules · 2022Article
- Structural assembly of the nucleic-acid-binding Thp3-Csn12-Sem1 complex functioning in mRNA splicing.Nucleic acids research · 2022Article
- A context-dependent and disordered ubiquitin-binding motif.Cellular and molecular life sciences : CMLS · 2022Article
- BRCA2-DSS1 interaction is dispensable for RAD51 recruitment at replication-induced and meiotic DNA double strand breaks.Nature communications · 2022Article
- Proteasomal subunit depletions differentially affect germline integrity inFrontiers in cell and developmental biology · 2022Article
- Starvation-induced proteasome assemblies in the nucleus link amino acid supply to apoptosis.Nature communications · 2021Article
- The disordered PCI-binding human proteins CSNAP and DSS1 have diverged in structure and function.Protein science : a publication of the Protein Society · 2021Article
- Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies.The FEBS journal · 2021Review
1 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
Abstract
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome. The proteasome subunits Rpn10 and Rpn13 are known to bind ubiquitin, but genetic and biochemical data suggest the existence of at least one other substrate receptor. Here, we show that the phylogenetically conserved proteasome subunit Dss1 (Sem1) binds ubiquitin chains linked by K63 and K48. Atomic resolution data show that Dss1 is disordered and binds ubiquitin by binding sites characterized by acidic and hydrophobic residues. The complementary binding region in ubiquitin is composed of a hydrophobic patch formed by I13, I44, and L69 flanked by two basic regions. Mutations in the ubiquitin-binding site of Dss1 cause growth defects and accumulation of ubiquitylated proteins.
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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.