ArticleThe Journal of biological chemistry2016
Catalytically Active Proteasomes Function Predominantly in the Cytosol.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
19 citing papers in PubMed.
- Proteasome localization and activity in pig brain andFrontiers in cellular neuroscience · 2024Article
- AKIR-1 regulates proteasome subcellular function iniScience · 2023Article
- SIRT1 activation synergizes with FXR agonism in hepatoprotectionActa pharmaceutica Sinica. B · 2023Article
- IntracellularFrontiers in immunology · 2023Article
- Comprehensive Analysis of Proteasomal Complexes in Mouse Brain Regions Detects ENO2 as a Potential Partner of the Proteasome in the Striatum.Cellular and molecular neurobiology · 2022Article
- The role of ubiquitination in spinal and bulbar muscular atrophy.Frontiers in molecular neuroscience · 2022Review
- Tumor-targeting cell-penetrating peptide, p28, for glioblastoma imaging and therapy.Frontiers in oncology · 2022Article
- MDM2-Driven Ubiquitination Rapidly Removes p53 from Its Cognate Promoters.Biomolecules · 2021Article
- Ubiquitin Ligase Redundancy and Nuclear-Cytoplasmic Localization in Yeast Protein Quality Control.Biomolecules · 2021Review
- Proteasome Complexes and Their Heterogeneity in Colorectal, Breast and Pancreatic Cancers.Journal of Cancer · 2021Article
- The E3 ubiquitin ligase SCF(Fbxo7) mediates proteasomal degradation of UXT isoform 2 (UXT-V2) to inhibit the NF-κB signaling pathway.Biochimica et biophysica acta. General subjects · 2021Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Sledgehammer to Scalpel: Broad Challenges to the Heart and Other Tissues Yield Specific Cellular Responses via Transcriptional Regulation of the ER-Stress Master Regulator ATF6α.International journal of molecular sciences · 2020Review
- Ubiquitin-dependent protein degradation at the endoplasmic reticulum and nuclear envelope.Seminars in cell & developmental biology · 2019Review
- Nuclear Transport of Yeast Proteasomes.Frontiers in molecular biosciences · 2019Review
- Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation.Frontiers in molecular biosciences · 2019Review
- Proteasomes tether to two distinct sites at the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Programmed cell death 4 mechanism of action: The model to be updated?Cell cycle (Georgetown, Tex.) · 2017Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The ubiquitin/proteasome pathway is a well characterized system for degrading intracellular proteins, although many aspects remain poorly understood. There is, for instance, a conspicuous lack of understanding of the site(s) where nuclear proteins are degraded because the subcellular distribution of peptidase activity has not been investigated systematically. Although nuclear proteins could be degraded by importing proteasomes into the nucleus, it is also evident that some nuclear proteins are degraded only after export to cytosolic proteasomes. Proteasomes and substrates are mobile, and consequently, the sites of degradation might not be static. We sought to identify the location of proteasomes to provide more conclusive evidence on the sites of protein degradation. We report that catalytically active proteasomes exist almost exclusively in the cytosol. The resulting lack of nuclear peptidase activity suggests that little, if any, degradation occurs in the nucleus. These and other studies suggest that the export of proteolytic substrates could define an important regulatory step in the degradation of nuclear proteins by cytosolic proteasomes.
Indexed as
Identifiers
What Socratic holds
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 Socratic graph.