ArticleProceedings of the National Academy of Sciences of the United States of America2011
The Cdc48 ATPase modulates the interaction between two proteolytic factors Ufd2 and Rad23.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 52 citations in OpenAlex.
- Direct observation of ATP-driven ubiquitin chain handling by Cdc48.Nature communications · 2026Article
- UBL7 is indispensable for spermiogenesis through protecting critical factors from excessive degradation by proteasomes.Nature communications · 2025Article
- Deciphering UBE4B phosphorylation dynamics: a key mechanism in p53 accumulation and cancer cell response to DNA damage.Cell death discovery · 2025Article
- The derlin Dfm1 couples retrotranslocation of a folded protein domain to its proteasomal degradation.The Journal of cell biology · 2024Article
- DNA damage response revisited: the p53 family and its regulators provide endless cancer therapy opportunities.Experimental & molecular medicine · 2022Review
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Multi-Step Ubiquitin Decoding Mechanism for Proteasomal Degradation.Pharmaceuticals (Basel, Switzerland) · 2020Review
- AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms.Biomolecules · 2020Review
- Review
- The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome.Communications biology · 2019Article
- Transcriptome Profiling of the Elongating Internode of Cotton (Frontiers in plant science · 2019Article
- Whole-Genome Sequencing of Suppressor DNA Mixtures Identifies Pathways That Compensate for Chromosome Segregation Defects inG3 (Bethesda, Md.) · 2018Article
- 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
- Deviation of the typical AAA substrate-threading pore prevents fatal protein degradation in yeast Cdc48.Scientific reports · 2017Article
- Article
- UV-B Inhibits Leaf Growth through Changes in Growth Regulating Factors and Gibberellin Levels.Plant physiology · 2017Article
- Article
- Ufd2p synthesizes branched ubiquitin chains to promote the degradation of substrates modified with atypical chains.Nature communications · 2017Article
- Sumoylation, Phosphorylation, and Acetylation Fine-Tune the Turnover of Plant Immunity Components Mediated by Ubiquitination.Frontiers in plant science · 2017Review
- Single base substitution in OsCDC48 is responsible for premature senescence and death phenotype in rice.Journal of integrative plant biology · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Rad23 and cell division cycle protein 48 (Cdc48), two key regulators of postubiquitylation events, act on distinct and overlapping sets of substrates. The principle underlying their division of labor and cooperation in proteolysis remains elusive. Both Rad23 and Cdc48 bind a ubiquitin protein ligase ubiquitin fusion degradation-2 (Ufd2), and regulate the degradation of Ufd2 substrates. With its ability to bind ubiquitin chains directly and the proteasome via different domains, Rad23 serves as a bridge linking ubiquitylated substrates to the proteasome. The significance and specific role of the Ufd2-Cdc48 interaction are unclear. Here, we demonstrate that mutations in Ufd2 alter its interaction with Cdc48 and impair its function in substrate proteolysis but not in ubiquitylation. Furthermore, Cdc48 promotes the disassembly of the Ufd2-Rad23 complex in an manner that is dependent on ATP and Ufd2 binding, revealing a biochemical role for Cdc48. Rad23 was shown to bind separately to Ufd2 and to the proteasome subunit Rpn1, which define two distinct steps in proteolysis. The action of Cdc48 could free Rad23 from Ufd2 to allow its subsequent association with Rpn1, which in turn may facilitate the orderly transfer of the substrate from the ubiquitylation apparatus to the proteasome.
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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.