ArticlePLoS genetics2019
AMPK regulates ESCRT-dependent microautophagy of proteasomes concomitant with proteasome storage granule assembly during glucose starvation.
Article in PLoS genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
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Who cites it
24 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.
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- Microautophagy: current understanding of its molecular mechanisms and functions.Autophagy reports · 2026Review
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- Cellular homeostatic responses to lysosomal damage.Trends in cell biology · 2025Review
- Quiescent cells maintain active degradation-mediated protein quality control requiring proteasome, autophagy, and nucleus-vacuole junctions.The Journal of biological chemistry · 2025Article
- Proteasome dynamics in response to metabolic changes.Frontiers in cell and developmental biology · 2025Review
- Proteasome condensates repeatedly "contact and release" at the nuclear periphery during dissolution.microPublication biology · 2025Article
- Pep12 is important for proteasome microautophagy under low glucose conditions.microPublication biology · 2025Article
- The Potential of Edible and Medicinal Resource Polysaccharides for Prevention and Treatment of Neurodegenerative Diseases.Biomolecules · 2023Review
- The emerging mechanisms and functions of microautophagy.Nature reviews. Molecular cell biology · 2023Review
- Proteasome granule formation is regulated through mitochondrial respiration and kinase signaling.Journal of cell science · 2022Article
- Assembly checkpoint of the proteasome regulatory particle is activated by coordinated actions of proteasomal ATPase chaperones.Cell reports · 2022Article
- Selective microautophagy of proteasomes is initiated by ESCRT-0 and is promoted by proteasome ubiquitylation.Journal of cell science · 2022Article
- Atg39 selectively captures inner nuclear membrane into lumenal vesicles for delivery to the autophagosome.The Journal of cell biology · 2021Article
- Yeast Nst1 is a novel component of P-bodies and is a specific suppressor of proteasome base assembly defects.Molecular biology of the cell · 2021Article
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5 authors at 2 institutions in 2 countries.
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Abstract
The ubiquitin-proteasome system regulates numerous cellular processes and is central to protein homeostasis. In proliferating yeast and many mammalian cells, proteasomes are highly enriched in the nucleus. In carbon-starved yeast, proteasomes migrate to the cytoplasm and collect in proteasome storage granules (PSGs). PSGs dissolve and proteasomes return to the nucleus within minutes of glucose refeeding. The mechanisms by which cells regulate proteasome homeostasis under these conditions remain largely unknown. Here we show that AMP-activated protein kinase (AMPK) together with endosomal sorting complexes required for transport (ESCRTs) drive a glucose starvation-dependent microautophagy pathway that preferentially sorts aberrant proteasomes into the vacuole, thereby biasing accumulation of functional proteasomes in PSGs. The proteasome core particle (CP) and regulatory particle (RP) are regulated differently. Without AMPK, the insoluble protein deposit (IPOD) serves as an alternative site that specifically sequesters CP aggregates. Our findings reveal a novel AMPK-controlled ESCRT-mediated microautophagy mechanism in the regulation of proteasome trafficking and homeostasis under carbon starvation.
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