ArticleThe Biochemical journal2006
Fission yeast Dss1 associates with the proteasome and is required for efficient ubiquitin-dependent proteolysis.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- Phosphorylation of Schizosaccharomyces pombe Dss1 mediates direct binding to the ubiquitin-ligase Dma1 in vitro.Protein science : a publication of the Protein Society · 2023Article
- Deciphering the Alphabet of Disorder-Glu and Asp Act Differently on Local but Not Global Properties.Biomolecules · 2022Article
- The disordered PCI-binding human proteins CSNAP and DSS1 have diverged in structure and function.Protein science : a publication of the Protein Society · 2021Article
- Novel Modular Rhodopsins from Green Algae Hold Great Potential for Cellular Optogenetic Modulation Across the Biological Model Systems.Life (Basel, Switzerland) · 2020Article
- Expanded Interactome of the Intrinsically Disordered Protein Dss1.Cell reports · 2018Article
- Sem1 links proteasome stability and specificity to multicellular development.PLoS genetics · 2018Article
- A systematic genomic screen implicates nucleocytoplasmic transport and membrane growth in nuclear size control.PLoS genetics · 2017Article
- Article
- Phosphorylation of ubiquitin at Ser65 affects its polymerization, targets, and proteome-wide turnover.EMBO reports · 2015Article
- Dss1 is a 26S proteasome ubiquitin receptor.Molecular cell · 2014Article
- Functional assays for analysis of variants of uncertain significance in BRCA2.Human mutation · 2014Review
- BRCA2: one small step for DNA repair, one giant protein purified.The Yale journal of biology and medicine · 2013Review
- Evidence that the Arabidopsis Ubiquitin C-terminal Hydrolases 1 and 2 associate with the 26S proteasome and the TREX-2 complex.Plant signaling & behavior · 2012Article
- Designed proteins to modulate cellular networks.ACS chemical biology · 2010Article
- Schizosaccharomyces pombe Dss1p is a DNA damage checkpoint protein that recruits Rad24p, Cdc25p, and Rae1p to DNA double-strand breaks.The Journal of biological chemistry · 2010Article
- Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery.The Journal of cell biology · 2009Article
- C. elegans dss-1 is functionally conserved and required for oogenesis and larval growth.BMC developmental biology · 2008Article
- The proteasome is involved in determining differential utilization of double-strand break repair pathways.Oncogene · 2007Article
- The roles of BRCA1 and BRCA2 and associated proteins in the maintenance of genomic stability.Oncogene · 2006Review
- Sem1: a versatile "molecular glue"?Nucleus (Austin, Tex.)Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human DSS1 associates with BRCA2, a tumour suppressor protein required for efficient recombinational DNA repair, but the biochemical function of DSS1 is not known. Orthologues of DSS1 are found in organisms such as budding yeast and fission yeast that do not have BRCA2-related proteins, indicating that DSS1 has a physiological role independent of BRCA2. The DSS1 orthologue in Saccharomyces cerevisiae has been shown to associate with the 26 S proteasome and, in the present paper, we report that in the distantly related fission yeast Schizosaccharomyces pombe, Dss1 associates with the 19 S RP (regulatory particle) of the 26 S proteasome. A role for S. pombe Dss1 in proteasome function is supported by three lines of evidence. First, overexpression of two components of the 19 S RP, namely Pad1/Rpn11 and Mts3/Rpn12, rescued the temperature-sensitive growth defect of the dss1 mutant. Secondly, the dss1 mutant showed phenotypes indicative of a defect in proteasome function: growth of the dss1 mutant was inhibited by low concentrations of L-canavanine, an amino acid analogue, and cells of the dss1 mutant accumulated high molecular mass poly-ubiquitylated proteins. Thirdly, synthetic growth defects were found when the dss1 mutation was combined with mutations in other proteasome subunit genes. These findings show that DSS1 has an evolutionarily conserved role as a regulator of proteasome function and suggest that DSS1 may provide a link between BRCA2 and ubiquitin-mediated proteolysis in human cells.
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Registered trials
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