ArticleThe EMBO journal1998
Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast.
Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 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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Who cites it
90 citing papers in PubMed, 214 citations in OpenAlex.
- Stress-Induced Reorganization of Proteasomes Through Diffusion and Cytoskeleton-Dependent Mechanisms.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Spatial mechanisms of quality control during chaperone-mediated assembly of the proteasome.Nature communications · 2025Article
- Proteasome dynamics in response to metabolic changes.Frontiers in cell and developmental biology · 2025Review
- AKIR-1 regulates proteasome subcellular function iniScience · 2023Article
- The ubiquitin-proteasome system and learning-dependent synaptic plasticity - A 10 year update.Neuroscience and biobehavioral reviews · 2023Review
- Yeast derlin Dfm1 employs a chaperone-like function to resolve misfolded membrane protein stress.PLoS biology · 2023Article
- Quality control mechanisms that protect nuclear envelope identity and function.The Journal of cell biology · 2022Review
- Unique Features of the Tissue Structure in the Naked Mole Rat (International journal of molecular sciences · 2022Article
- A phytoplasma effector acts as a ubiquitin-like mediator between floral MADS-box proteins and proteasome shuttle proteins.The Plant cell · 2022Article
- Nitric Oxide Signaling and Its Association with Ubiquitin-Mediated Proteasomal Degradation in Plants.International journal of molecular sciences · 2022Review
- Localized Proteasomal Degradation: From the Nucleus to Cell Periphery.Biomolecules · 2022Review
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Ubiquilin-2 differentially regulates polyglutamine disease proteins.Human molecular genetics · 2020Article
- Multi-Step Ubiquitin Decoding Mechanism for Proteasomal Degradation.Pharmaceuticals (Basel, Switzerland) · 2020Review
- ER-Resident Transcription Factor Nrf1 Regulates Proteasome Expression and Beyond.International journal of molecular sciences · 2020Review
- Golgi organization is regulated by proteasomal degradation.Nature communications · 2020Article
- Direct visualization of degradation microcompartments at the ER membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation.Frontiers in molecular biosciences · 2019Review
- Visualizing Proteasome Activity and Intracellular Localization Using Fluorescent Proteins and Activity-Based Probes.Frontiers in molecular biosciences · 2019Article
- Nuclear Transport of Yeast Proteasomes.Frontiers in molecular biosciences · 2019Review
30 more citing papers are in PubMed but not listed here.
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 at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
26S proteasomes are the key enzyme complexes responsible for selective turnover of short-lived and misfolded proteins. Based on the assumption that they are dispersed over the nucleoplasm and cytoplasm in all eukaryotic cells, we wanted to determine the subcellular distribution of 26S proteasomes in living yeast cells. For this purpose, we generated yeast strains that express functional green fluorescent protein (GFP) fusions of proteasomal subunits. An alpha subunit of the proteolytically active 20S core complex of the 26S proteasome, Pre6/YOL038w, as well as an ATPase-type subunit of the regulatory 19S cap complex, Cim5/YOL145w, were tagged with GFP. Both chimeras were shown to be incorporated completely into active 26S proteasomes. Microscopic analysis revealed that GFP-labelled 20S as well as 19S subunits are accumulated mainly in the nuclear envelope (NE)-endoplasmic reticulum (ER) network in yeast. These findings were supported by the co-localization and co-enrichment of 26S proteasomes with NE-ER marker proteins. A major location of proteasomal peptide cleavage activity was visualized in the NE-ER network, indicating that proteasomal degradation takes place mainly in this subcellular compartment in yeast.
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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.