ArticleCell reports2018
Expanded Interactome of the Intrinsically Disordered Protein Dss1.
Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- Assessing Transcriptomic Responses to Oxidative Stress: Contrasting Wild-Type Arabidopsis Seedlings withInternational journal of molecular sciences · 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
- Deciphering the Alphabet of Disorder-Glu and Asp Act Differently on Local but Not Global Properties.Biomolecules · 2022Article
- A context-dependent and disordered ubiquitin-binding motif.Cellular and molecular life sciences : CMLS · 2022Article
- OB-fold Families of Genome Guardians: A Universal Theme Constructed From the Small β-barrel Building Block.Frontiers in molecular biosciences · 2022Review
- The disordered PCI-binding human proteins CSNAP and DSS1 have diverged in structure and function.Protein science : a publication of the Protein Society · 2021Article
- Guardians of the Genome: BRCA2 and Its Partners.Genes · 2021Review
- Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins.Biomolecules · 2021Article
- Mass spectrometry-based protein‒protein interaction techniques and their applications in studies of DNA damage repair.Journal of Zhejiang University. Science. B · 2021Review
- DSS1 interacts with and stimulates RAD52 to promote the repair of DSBs.Nucleic acids research · 2020Article
- Distinct Functions of the Cap-Binding Complex in Stimulation of Nuclear mRNA Export.Molecular and cellular biology · 2019Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Dss1 (also known as Sem1) is a conserved, intrinsically disordered protein with a remarkably broad functional diversity. It is a proteasome subunit but also associates with the BRCA2, RPA, Csn12-Thp1, and TREX-2 complexes. Accordingly, Dss1 functions in protein degradation, DNA repair, transcription, and mRNA export. Here in Schizosaccharomyces pombe, we expand its interactome further to include eIF3, the COP9 signalosome, and the mitotic septins. Within its intrinsically disordered ensemble, Dss1 forms a transiently populated C-terminal helix that dynamically interacts with and shields a central binding region. The helix interfered with the interaction to ATP-citrate lyase but was required for septin binding, and in strains lacking Dss1, ATP-citrate lyase solubility was reduced and septin rings were more persistent. Thus, even weak, transient interactions within Dss1 may dynamically rewire its interactome.
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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.