ArticleThe Journal of biological chemistry2013
A conserved protein with AN1 zinc finger and ubiquitin-like domains modulates Cdc48 (p97) function in the ubiquitin-proteasome pathway.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Stimulating proteasomal degradation in human proteinopathies.The FEBS journal · 2026Review
- Activators of the 26S proteasome when protein degradation increases.Experimental & molecular medicine · 2025Review
- Comparative Proteome-Wide Abundance Profiling of Yeast Strains Deleted for Cdc48 Adaptors.Proteomes · 2024Article
- Role of Proteostasis Regulation in the Turnover of Stress Granules.International journal of molecular sciences · 2022Review
- Yeast PI31 inhibits the proteasome by a direct multisite mechanism.Nature structural & molecular biology · 2022Article
- Low complexity RGG-motif sequence is required for Processing body (P-body) disassembly.Nature communications · 2022Article
- AN1-type zinc finger protein 3 (ZFAND3) is a transcriptional regulator that drives Glioblastoma invasion.Nature communications · 2020Article
- Histone sumoylation promotes Set3 histone-deacetylase complex-mediated transcriptional regulation.Nucleic acids research · 2020Article
- The Proteasome and Its Network: Engineering for Adaptability.Cold Spring Harbor perspectives in biology · 2020Review
- The Ulp2 SUMO protease promotes transcription elongation through regulation of histone sumoylation.The EMBO journal · 2019Article
- An Allosteric Interaction Network Promotes Conformation State-Dependent Eviction of the Nas6 Assembly Chaperone from Nascent 26S Proteasomes.Cell reports · 2019Article
- ZFAND5/ZNF216 is an activator of the 26S proteasome that stimulates overall protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Phospholipase Lpl1 links lipid droplet function with quality control protein degradation.Molecular biology of the cell · 2017Article
- Tmc1 Is a Dynamically Regulated Effector of the Rpn4 Proteotoxic Stress Response.The Journal of biological chemistry · 2016Article
- Proteomic Analysis Identifies Ribosome Reduction as an Effective Proteotoxic Stress Response.The Journal of biological chemistry · 2015Article
- A protein interaction map of the LSU processome.Genes & development · 2015Article
- Cuz1/Ynl155w, a zinc-dependent ubiquitin-binding protein, protects cells from metalloid-induced proteotoxicity.The Journal of biological chemistry · 2014Article
- Article
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7 authors.
Funding
Abstract
Regulated protein degradation mediated by the ubiquitin-proteasome system (UPS) is critical to eukaryotic protein homeostasis. Often vital to degradation of protein substrates is their disassembly, unfolding, or extraction from membranes. These processes are catalyzed by the conserved AAA-ATPase Cdc48 (also known as p97). Here we characterize the Cuz1 protein (Cdc48-associated UBL/zinc finger protein-1), encoded by a previously uncharacterized arsenite-inducible gene in budding yeast. Cuz1, like its human ortholog ZFAND1, has both an AN1-type zinc finger (Zf_AN1) and a divergent ubiquitin-like domain (UBL). We show that Cuz1 modulates Cdc48 function in the UPS. The two proteins directly interact, and the Cuz1 UBL, but not Zf_AN1, is necessary for binding to the Cdc48 N-terminal domain. Cuz1 also associates, albeit more weakly, with the proteasome, and the UBL is dispensable for this interaction. Cuz1-proteasome interaction is strongly enhanced by exposure of cells to the environmental toxin arsenite, and in a proteasome mutant, loss of Cuz1 enhances arsenite sensitivity. Whereas loss of Cuz1 alone causes only minor UPS degradation defects, its combination with mutations in the Cdc48(Npl4-Ufd1) complex leads to much greater impairment. Cuz1 helps limit the accumulation of ubiquitin conjugates on both the proteasome and Cdc48, suggesting a possible role in the transfer of ubiquitylated substrates from Cdc48 to the proteasome or in their release from these complexes.
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