ArticleMolecular cell2012
Signal-induced disassembly of the SCF ubiquitin ligase complex by Cdc48/p97.
Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed, 37 citations in OpenAlex.
- Distinct Stress Regulators in the CRL Family: Emerging Roles of F-Box Proteins: Cullin-RING Ligases and Stress-Sensing.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Evidence for a hydrogen sulfide-sensing E3 ligase in yeast.Genetics · 2024Article
- Cadmium binding by the F-box domain induces p97-mediated SCF complex disassembly to activate stress response programs.Nature communications · 2024Article
- Article
- Targeting of client proteins to the VCP/p97/Cdc48 unfolding machine.Frontiers in molecular biosciences · 2023Review
- Cdc48Ufd1/Npl4 segregase removes mislocalized centromeric histone H3 variant CENP-A from non-centromeric chromatin.Nucleic acids research · 2022Article
- Cdc48/Shp1 participates in dissociation of protein complexes to regulate their activity.Current genetics · 2021Review
- Sensing and Signaling of Methionine Metabolism.Metabolites · 2021Review
- Protein Homeostasis Networks and the Use of Yeast to Guide Interventions in Alzheimer's Disease.International journal of molecular sciences · 2020Review
- Cdc48 cofactor Shp1 regulates signal-induced SCFProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Proteomics Links Ubiquitin Chain Topology Change to Transcription Factor Activation.Molecular cell · 2019Article
- Glycosylation Promotes the Random Coil to Helix Transition in a Region of a Protist Skp1 Associated with F-Box Binding.Biochemistry · 2018Article
- Article
- OThe Journal of biological chemistry · 2017Article
- The pseudophosphatase STYX targets the F-box of FBXW7 and inhibits SCFFBXW7 function.The EMBO journal · 2017Article
- Plant Virus Infection and the Ubiquitin Proteasome Machinery: Arms Race along the Endoplasmic Reticulum.Viruses · 2016Review
- p97 Composition Changes Caused by Allosteric Inhibition Are Suppressed by an On-Target Mechanism that Increases the Enzyme's ATPase Activity.Cell chemical biology · 2016Article
- Article
- Skp1 Independent Function of Cdc53/Cul1 in F-box Protein Homeostasis.PLoS genetics · 2015Article
- SCF ubiquitin ligase-targeted therapies.Nature reviews. Drug discovery · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
A large group of E3 ubiquitin ligases is formed by the multisubunit SCF complex, whose core complex (Rbx1/Cul1-Cdc53/Skp1) binds one of many substrate recruiting F-box proteins to form an array of SCF ligases with diverse substrate specificities. It has long been thought that ubiquitylation by SCF ligases is regulated at the level of substrate binding. Here we describe an alternative mechanism of SCF regulation by active dissociation of the F-box subunit. We show that cadmium stress induces selective recruitment of the AAA(+) ATPase Cdc48/p97 to catalyze dissociation of the F-box subunit from the yeast SCF(Met30) ligase to block substrate ubiquitylation and trigger downstream events. Our results not only provide an additional layer of ubiquitin ligase regulation but also suggest that targeted, signal-dependent dissociation of multisubunit enzyme complexes is an important mechanism in control of enzyme function.
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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.