ArticleMolecular and cellular biology2011
Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 55 papers, 1 of them a synthesis that pooled it.
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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
55 citing papers in PubMed, 1 synthesis or guideline pooled it, 87 citations in OpenAlex.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- TOR-NOT4 signalling couples translation to co-translational quality control in plants.Nature communications · 2026Article
- Puf3 contributes to changes in mRNA solubility, translation elongation dynamics at rare arginine codons and loss of protein homeostasis in cells lacking Not4.RNA (New York, N.Y.) · 2026Article
- Quantitative proteome analysis of LAP1-deficient human fibroblasts: A pilot approach for predicting the signaling pathways deregulated in LAP1-associated diseases.Biochemistry and biophysics reports · 2024Article
- Roles of the CCR4-Not complex in translation and dynamics of co-translation events.Wiley interdisciplinary reviews. RNA · 2023Review
- Cooperative regulation of coupled oncoprotein synthesis and stability in triple-negative breast cancer by EGFR and CDK12/13.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Retrotransposon LINE-1 bodies in the cytoplasm of piRNA-deficient mouse spermatocytes: Ribonucleoproteins overcoming the integrated stress response.PLoS genetics · 2023Article
- Not1 and Not4 inversely determine mRNA solubility that sets the dynamics of co-translational events.Genome biology · 2023Article
- Transcription feedback dynamics in the wake of cytoplasmic mRNA degradation shutdown.Nucleic acids research · 2022Article
- Assembly checkpoint of the proteasome regulatory particle is activated by coordinated actions of proteasomal ATPase chaperones.Cell reports · 2022Article
- Ccr4-Not as a mediator of environmental signaling: a jack of all trades and master of all.Current genetics · 2021Review
- The C-terminal region of yeast ubiquitin-protein ligase Not4 mediates its cellular localization and stress response.FEMS microbiology letters · 2021Article
- The Arabidopsis NOT4A E3 ligase promotes PGR3 expression and regulates chloroplast translation.Nature communications · 2021Article
- Review
- The Ccr4-Not complex regulates TORC1 signaling and mitochondrial metabolism by promoting vacuole V-ATPase activity.PLoS genetics · 2020Article
- Ecm29-mediated proteasomal distribution modulates excitatory GABA responses in the developing brain.The Journal of cell biology · 2020Article
- Cellular Responses to Proteasome Inhibition: Molecular Mechanisms and Beyond.International journal of molecular sciences · 2019Review
- Ccr4-Not maintains genomic integrity by controlling the ubiquitylation and degradation of arrested RNAPII.Genes & development · 2019Article
- Assembly en route.Nature structural & molecular biology · 2019Article
- Co-translational assembly of proteasome subunits in NOT1-containing assemblysomes.Nature structural & molecular biology · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study we determine that the Not4 E3 ligase is important for proteasome integrity. Consequently, deletion of Not4 leads to an accumulation of polyubiquitinated proteins and reduced levels of free ubiquitin. In the absence of Not4, the proteasome regulatory particle (RP) and core particle (CP) form salt-resistant complexes, and all other forms of RPs are unstable. Not4 can associate with RP species present in purified proteasome holoenzyme but not with purified RP. Additionally, Not4 interacts with Ecm29, a protein that stabilizes the proteasome. Interestingly, Ecm29 is identified in RP species that are inactive and not detectable in cells lacking Not4. In the absence of Not4, Ecm29 interacts less well with the proteasome and becomes ubiquitinated and degraded. Our results characterize Ecm29 as a proteasome chaperone whose appropriate interaction with the proteasome requires Not4.
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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.