Intracellular localization of the proteasome in response to stress conditions

Enenkel, Cordula; Kang, Ryu Won; Wilfling, Florian; Ernst, Oliver P.

doi:10.1016/j.jbc.2022.102083

Cited by 35 publications

(21 citation statements)

References 118 publications

(164 reference statements)

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“…At the same time, many proteasomes are located in the nucleus. Moreover, experiments with mouse embryonic fibroblasts have shown that the newly synthesized proteasomes were located particularly in the nucleus, while the three-day-old proteasomes were mainly found in the cytoplasm, which indicates inf low of the newly synthesized proteasomes from the nucleus to the cytoplasm [45]. Interestingly, proteins involved in realization of nuclear functions (cyclins, inhibitors of cyclin-dependent kinases, transcription factors NF-κB, IκB, p53) were among the first identified physiological proteasome substrates [46][47][48].…”

Section: Structure and Functions Of Proteasomesmentioning

confidence: 99%

“…In the context of known data on the intracellular traffic of proteasomes and their translocation into various cell compartments depending on the functional state of the cell [42][43][44][45], existence of the large number of proteins interacting with proteasomes and forming the proteasome interactome is quite understandable.…”

Section: Proteasome-associated Proteinsmentioning

confidence: 99%

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Proteasome Interactome and Its Role in the Mechanisms of Brain Plasticity

Buneeva

Kopylov²,

Медведев³

2023

Biochemistry Moscow

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Proteasomes are highly conserved multienzyme complexes responsible for proteolytic degradation of the short-lived, regulatory, misfolded, and damaged proteins. They play an important role in the processes of brain plasticity, and decrease in their function is accompanied by the development of neurodegenerative pathology. Studies performed in different laboratories both on cultured mammalian and human cells and on preparations of the rat and rabbit brain cortex revealed a large number of proteasome-associated proteins. Since the identified proteins belong to certain metabolic pathways, multiple enrichment of the proteasome fraction with these proteins indicates their important role in proteasome functioning. Extrapolation of the experimental data, obtained on various biological objects, to the human brain suggests that the proteasome-associated proteins account for at least 28% of the human brain proteome. The proteasome interactome of the brain contains a large number of proteins involved in the assembly of these supramolecular complexes, regulation of their functioning, and intracellular localization, which could be changed under different conditions (for example, during oxidative stress) or in different phases of the cell cycle. In the context of molecular functions of the Gene Ontology (GO) Pathways, the proteins of the proteasome interactome mediate cross-talk between components of more than 30 metabolic pathways annotated in terms of GO. The main result of these interactions is binding of adenine and guanine nucleotides, crucial for realization of the nucleotide-dependent functions of the 26S and 20S proteasomes. Since the development of neurodegenerative pathology is often associated with regioselective decrease in the functional activity of proteasomes, a positive therapeutic effect would be obviously provided by the factors increasing proteasomal activity. In any case, pharmacological regulation of the brain proteasomes seems to be realized through the changes in composition and/or activity of the proteins associated with proteasomes (deubiquitinase, PKA, CaMKIIα, etc.).

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Section: Structure and Functions Of Proteasomesmentioning

confidence: 99%

Section: Proteasome-associated Proteinsmentioning

confidence: 99%

Proteasome Interactome and Its Role in the Mechanisms of Brain Plasticity

Buneeva

Kopylov²,

Медведев³

2023

Biochemistry Moscow

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“…Depending on the type of neurodegeneration, these insoluble structures may aggregate in various subcellular compartments, including the nucleus [ 69 ], mitochondria [ 70 ], and cytoplasm [ 71 ], albeit the latter represents the predominant localization of these depositions. The observation that PA200 is mainly localized in the nucleus [ 1 , 72 ] suggests that the PA200/proteasomes are not primarily involved in the removal of cytosolic proteins. This also presupposes that the PA200 deficiencies in neurodegenerative diseases would only be marginally involved in the formation of the ubiquitin deposits.…”

Section: Dysregulation In Diseasementioning

confidence: 99%

The Proteasome Activator PA200/PSME4: An Emerging New Player in Health and Disease

2022

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Proteasomes comprise a family of proteasomal complexes essential for maintaining protein homeostasis. Accordingly, proteasomes represent promising therapeutic targets in multiple human diseases. Several proteasome inhibitors are approved for treating hematological cancers. However, their side effects impede their efficacy and broader therapeutic applications. Therefore, understanding the biology of the different proteasome complexes present in the cell is crucial for developing tailor-made inhibitors against specific proteasome complexes. Here, we will discuss the structure, biology, and function of the alternative Proteasome Activator 200 (PA200), also known as PSME4, and summarize the current evidence for its dysregulation in different human diseases. We hereby aim to stimulate research on this enigmatic proteasome regulator that has the potential to serve as a therapeutic target in cancer.

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“…Recent studies have suggested that conformational switching and deubiquitinating enzymes are involved in the regulation of 26S proteasome activity (de la Peña et al, 2018; Eisele et al, 2018; Kim & Goldberg, 2018; Kimura et al, 2012; Suresh et al, 2020). Furthermore, proteasome localization may be variable under certain conditions in yeast and mammalian cells (Enenkel et al, 2022; Fu et al, 2021; Gu et al, 2017; Kaganovich et al, 2008; Uriarte et al, 2021; Yasuda et al, 2020). However, details of the modification state and localization variation of the 26S proteasome under stress are largely unknown (Suresh et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

Severe ethanol stress inhibits yeast proteasome activity at moderate temperatures but not at low temperatures

et al. 2023

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Since yeast research under laboratory conditions is usually conducted at 25–30°C (moderate temperature range), most of the findings on yeast physiology are based on analyses in this temperature range. Due to inefficiencies in cultivation and analysis, insufficient information is available on yeast physiology in the low‐temperature range, although alcoholic beverage production is often conducted at relatively low temperatures (around 15°C). Recently, we reported that severe ethanol stress (10% v/v) inhibits proteasomal proteolysis in yeast cells under laboratory conditions at 28°C. In this study, proteasomal proteolysis at a low temperature (15°C) was evaluated using cycloheximide chase analysis of a short‐lived protein (Gic2‐3HA), an auxin‐inducible degron system (Paf1‐AID*‐6FLAG), and Spe1‐3HA, which is degraded ubiquitin‐independently by the proteasome. At 15°C, proteasomal proteolysis was not inhibited under severe ethanol stress, and sufficient proteasomal activity was maintained. These results provide novel insights into the effects of low temperature and ethanol on yeast physiology.

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Intracellular localization of the proteasome in response to stress conditions

Cited by 35 publications

References 118 publications

Proteasome Interactome and Its Role in the Mechanisms of Brain Plasticity

Proteasome Interactome and Its Role in the Mechanisms of Brain Plasticity

The Proteasome Activator PA200/PSME4: An Emerging New Player in Health and Disease

Severe ethanol stress inhibits yeast proteasome activity at moderate temperatures but not at low temperatures

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