ReviewCurrent genetics2018
The paradox of proteasome granules.
Review in Current genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 25 citations in OpenAlex.
- Celery root-plant derived vesicles: comprehensive isolation, characterization and proteomic analysis.Molecular biology reports · 2025Article
- Protein quality control machinery: regulators of condensate architecture and functionality.Trends in biochemical sciences · 2025Review
- Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1.Scientific reports · 2024Article
- To Kill or to Be Killed: How Does the Battle between the UPS and Autophagy Maintain the Intracellular Homeostasis in Eukaryotes?International journal of molecular sciences · 2023Review
- Proteasome granule formation is regulated through mitochondrial respiration and kinase signaling.Journal of cell science · 2022Article
- Phase-Separated Subcellular Compartmentation and Related Human Diseases.International journal of molecular sciences · 2022Review
- Understanding circadian regulation of mammalian cell function, protein homeostasis, and metabolism.Current opinion in systems biology · 2021Review
- Structural Insights into Substrate Recognition and Processing by the 20S Proteasome.Biomolecules · 2021Review
- Tagging the proteasome active site β5 causes tag specific phenotypes in yeast.Scientific reports · 2020Article
- Asymmetric cell division and replicative aging: a new perspective from the spindle poles.Current genetics · 2020Review
- Microautophagy regulates proteasome homeostasis.Current genetics · 2020Review
- Sky1: at the intersection of prion-like proteins and stress granule regulation.Current genetics · 2020Review
- How does protein degradation regulate TOM machinery-dependent mitochondrial import?Current genetics · 2020Review
- Direct visualization of degradation microcompartments at the ER membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Patrolling the nucleus: inner nuclear membrane-associated degradation.Current genetics · 2019Review
- More than just a phase: the search for membraneless organelles in the bacterial cytoplasm.Current genetics · 2019Review
- Spatial Organization of Proteasome Aggregates in the Regulation of Proteasome Homeostasis.Frontiers in molecular biosciences · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Profound knowledge is available for the structure, function and regulation of proteasomes, the key proteases for ubiquitin-dependent protein degradation in dividing cells. Far less understood are proteasome structure and function in quiescence, the resting phase of our body's cells, as in yeast cells grown to stationary phase. In quiescent yeast proteasomes exit the nucleus and accumulate in cytoplasmic protein droplets, called proteasome storage granules (PSG). PSG-like structures also exist in non-dividing mammalian cells suggesting that the mechanism underlying PSG organization is conserved from yeast to human. The PSG has physiological significance as it protects yeast cells against stress and confers fitness during aging. The molecular architecture of PSG remains an enigma, since PSG freely move as spherical units without being surrounded by membranes through the cytoplasm. They rapidly resolve with the resumption of cell proliferation and proteasomes reenter the nucleus. Our systems biology and biochemical data revealed that PSG are mainly composed of proteasomes and free ubiquitin. Often intrinsically disordered proteins undergo liquid phase separations, allowing soluble proteins to condense into protein droplets in an aqueous solution. The question is which proteins and factors nucleate PSG formation, since proteasomes composed of folded subunits are able to degrade intrinsically disordered proteins.
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What OpenQuestion 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 OpenQuestion graph.