ArticleJournal of cell science2015
N-terminal acetylation and replicative age affect proteasome localization and cell fitness during aging.
Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 42 citations in OpenAlex.
- Acetic acid induces proteasome storage granule formation and inhibits proteasomal proteolysis: Comparison with other induction conditions.The Journal of biological chemistry · 2026Article
- Sorbic acid triggers rapid formation of proteasome storage granules inMicrobial cell (Graz, Austria) · 2026Article
- Proteasome dynamics in response to metabolic changes.Frontiers in cell and developmental biology · 2025Review
- Proteasome condensate formation is driven by multivalent interactions with shuttle factors and ubiquitin chains.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Proteasome granule formation is regulated through mitochondrial respiration and kinase signaling.Journal of cell science · 2022Article
- Age-Related Unstructured Spike Patterns and Molecular Localization inFrontiers in physiology · 2022Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Tagging the proteasome active site β5 causes tag specific phenotypes in yeast.Scientific reports · 2020Article
- Application of Recombination -Induced Tag Exchange (RITE) to study histone dynamics in human cells.Epigenetics · 2020Article
- Microautophagy regulates proteasome homeostasis.Current genetics · 2020Review
- AMPK regulates ESCRT-dependent microautophagy of proteasomes concomitant with proteasome storage granule assembly during glucose starvation.PLoS genetics · 2019Article
- Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation.Frontiers in molecular biosciences · 2019Review
- Nuclear Transport of Yeast Proteasomes.Frontiers in molecular biosciences · 2019Review
- Spatial Organization of Proteasome Aggregates in the Regulation of Proteasome Homeostasis.Frontiers in molecular biosciences · 2019Review
- N-terminal Acetylation Levels Are Maintained During Acetyl-CoA Deficiency inMolecular & cellular proteomics : MCP · 2018Article
- Control of protein degradation by N-terminal acetylation and the N-end rule pathway.Experimental & molecular medicine · 2018Review
- Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation.eLife · 2018Article
- The paradox of proteasome granules.Current genetics · 2018Review
- Ubiquitin orchestrates proteasome dynamics between proliferation and quiescence in yeast.Molecular biology of the cell · 2017Article
- From Genes to Ecosystems in Microbiology: Modeling Approaches and the Importance of Individuality.Frontiers in microbiology · 2017Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Specific degradation of proteins is essential for virtually all cellular processes and is carried out predominantly by the proteasome. The proteasome is important for clearance of damaged cellular proteins. Damaged proteins accumulate over time and excess damaged proteins can aggregate and induce the death of old cells. In yeast, the localization of the proteasome changes dramatically during aging, possibly in response to altered proteasome activity requirements. We followed two key parameters of this process: the distribution of proteasomes in nuclear and cytosolic compartments, and the formation of cytoplasmic aggregate-like structures called proteasome storage granules (PSGs). Whereas replicative young cells efficiently relocalized proteasomes from the nucleus to the cytoplasm and formed PSGs, replicative old cells were less efficient in relocalizing the proteasome and had less PSGs. By using a microscopy-based genome-wide screen, we identified genetic factors involved in these processes. Both relocalization of the proteasome and PSG formation were affected by two of the three N-acetylation complexes. These N-acetylation complexes also had different effects on the longevity of cells, indicating that each N-acetylation complex has different roles in proteasome location and aging.
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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.