ArticlePloS one2013
Concerted action of the ubiquitin-fusion degradation protein 1 (Ufd1) and Sumo-targeted ubiquitin ligases (STUbLs) in the DNA-damage response.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- Solo or in Concert: SUMOylation in Pathogenic Fungi.The plant pathology journal · 2025Review
- The fission yeast SUMO-targeted ubiquitin ligase Slx8 functionally associates with clustered centromeres and the silent mating-type region at the nuclear periphery.Biology open · 2024Article
- Cdc48 and its co-factor Ufd1 extract CENP-A from centromeric chromatin and can induce chromosome elimination in the fission yeast Schizosaccharomyces pombe.Biology open · 2024Article
- SUMOylation regulates Lem2 function in centromere clustering and silencing.Journal of cell science · 2023Article
- SUMO enhances unfolding of SUMO-polyubiquitin-modified substrates by the Ufd1/Npl4/Cdc48 complex.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Intricate SUMO-based control of the homologous recombination machinery.Genes & development · 2019Review
- Dynamics of RIF1 SUMOylation is regulated by PIAS4 in the maintenance of Genomic Stability.Scientific reports · 2017Article
- The role of ubiquitin-dependent segregase p97 (VCP or Cdc48) in chromatin dynamics after DNA double strand breaks.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- SUMO-targeted ubiquitin ligase activity can either suppress or promote genome instability, depending on the nature of the DNA lesion.PLoS genetics · 2017Article
- Ubiquitin-dependent and independent roles of SUMO in proteostasis.American journal of physiology. Cell physiology · 2016Review
- Cooperativity of the SUMO and Ubiquitin Pathways in Genome Stability.Biomolecules · 2016Review
- Ring of Change: CDC48/p97 Drives Protein Dynamics at Chromatin.Frontiers in genetics · 2016Review
- Targeting of SUMO substrates to a Cdc48-Ufd1-Npl4 segregase and STUbL pathway in fission yeast.Nature communications · 2015Article
- High Confidence Fission Yeast SUMO Conjugates Identified by Tandem Denaturing Affinity Purification.Scientific reports · 2015Article
- Pli1(PIAS1) SUMO ligase protected by the nuclear pore-associated SUMO protease Ulp1SENP1/2.The Journal of biological chemistry · 2015Article
- Single site suppressors of a fission yeast temperature-sensitive mutant in cdc48 identified by whole genome sequencing.PloS one · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotes many players in the DNA-damage response (DDR) catalyze protein sumoylation or ubiquitylation. Emphasis has been placed on how these modifications orchestrate the sequential recruitment of repair factors to sites of DNA damage or stalled replication forks. Here, we shed light on a pathway in which sumoylated factors are eliminated through the coupled action of Sumo-targeted ubiquitin ligases (STUbLs) and the ubiquitin-fusion degradation protein 1 (Ufd1). Ufd1 is a subunit of the Cdc48-Ufd1-Npl4 complex implicated in the sorting of ubiquitylated substrates for degradation by the proteasome. We find that in fission yeast, Ufd1 interacts physically and functionally with the Sumo-targeted ubiquitin ligase (STUbL) Rfp1, homologous to human RNF4, and with the Sumo E3 ligase Pli1, homologous to human PIAS1. Deleting a C-terminal domain of Ufd1 that mediates the interaction of Ufd1 with Rfp1, Pli1, and Sumo (ufd1ΔCt(213-342) ) lead to an accumulation of high-molecular-weight Sumo conjugates and caused severe genomic instabilities. The spectrum of sensitivity of ufd1ΔCt(213-342) cells to genotoxins, the epistatic relationships of ufd1ΔCt(213-342) with mutations in DNA repair factors, and the localization of the repair factor Rad22 in ufd1ΔCt(213-342) cells point to ufd1ΔCt(213-342) cells accumulating aberrant structures during replication that require homologous recombination (HR) for their repair. We present evidence that HR is however often not successful in ufd1ΔCt(213-342) cells and we identify Rad22 as one of the high-molecular-weight conjugates accumulating in the ufd1ΔCt(213-342) mutant consistent with Rad22 being a STUbL/Ufd1 substrate. Suggesting a direct role of Ufd1 in the processing of Sumo-conjugates, Ufd1 formed nuclear foci colocalizing with Sumo during the DDR, and Sumo-conjugates accumulated in foci in the ufd1ΔCt(213-342) mutant. Broader functional relationships between Ufd1 and STUbLs conceivably affect numerous cellular processes beyond the DDR.
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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.