26S proteasome exhibits endoribonuclease activity controlled by extra-cellular stimuli

Куличкова, В. А.; Цимоха, А. С.; Fedorova, Olga; Moiseeva, Tatiana N.; Bottril, Andrew; Lezina, Larissa; Gauze, L N; Konstantinova, Irina D.; Mittenberg, A. G.; Barlev, Nickolai A.

doi:10.4161/cc.9.4.10829

Cited by 39 publications

(29 citation statements)

References 55 publications

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“…Transcriptional activity of GR and other nuclear receptors is regulated by the proteasome via proteolysis-dependent and independent mechanisms [52,53]. One of the proteins with the strongest translocation from cytosol to nucleus was PSMA1, component of the 26S core proteasome, exhibiting also endonuclease activity [54]. The others are components of the 11S or 19S regulatory particle, involved in antigen presentation.…”

Section: Discussionmentioning

confidence: 99%

Proteomic profiling of rapid non-genomic and concomitant genomic effects of acute restraint stress on rat thymocytes

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Revets

Hoffmann

et al. 2012

Journal of Proteomics

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Section: Discussionmentioning

confidence: 99%

Proteomic profiling of rapid non-genomic and concomitant genomic effects of acute restraint stress on rat thymocytes

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Revets

Hoffmann

et al. 2012

Journal of Proteomics

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“…RNase activity: The 20S CP (particularly the α5 subunit) exhibits RNase activity dependent upon divalent cations such as Ca 2＋ and Mg 2＋ , whereas the proteolytic activity does not require divalent cations (5). Interestingly, the α5-RNase activity is highly correlated with the extent of α6- and α7-subunit phosphorylation.…”

Section: Introductionmentioning

confidence: 99%

“…Interestingly, the α5-RNase activity is highly correlated with the extent of α6- and α7-subunit phosphorylation. Moreover, the α5-RNase activity increases markedly during erythroid differentiation and programmed cell death (5). Mittenberg et al recently reported that most α-subunits (except α3) exhibit in vitro RNase activity against p53 mRNA (6).…”

Section: Introductionmentioning

confidence: 99%

Precise assembly and regulation of 26S proteasome and correlation between proteasome dysfunction and neurodegenerative diseases

Im¹,

Chung²

2016

BMB Reports

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Neurodegenerative diseases (NDs) often involve the formation of abnormal and toxic protein aggregates, which are thought to be the primary factor in ND occurrence and progression. Aged neurons exhibit marked increases in aggregated protein levels, which can lead to increased cell death in specific brain regions. As no specific drugs/therapies for treating the symptoms or/and progression of NDs are available, obtaining a complete understanding of the mechanism underlying the formation of protein aggregates is needed for designing a novel and efficient removal strategy. Intracellular proteolysis generally involves either the lysosomal or ubiquitin-proteasome system. In this review, we focus on the structure and assembly of the proteasome, proteasome-mediated protein degradation, and the multiple dynamic regulatory mechanisms governing proteasome activity. We also discuss the plausibility of the correlation between changes in proteasome activity and the occurrence of NDs. [BMB Reports 2016; 49(9): 459-473]

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“…In addition to “canonical” proteolytic activities proteasomes also possess several “non-canonical” activities [18]. In this respect, it is important to note that several decades ago a number of reports described the proteasome (at least the 20S CP) as an RNA binding protein complex [19, 20].…”

Section: Introductionmentioning

confidence: 99%

“…Subsequent studies have identified the alpha5 subunit of CP as the one possessing RNAse activity. The latter can be regulated by various post-translational modifications in response to different environmental cues [18, 26]. Finally, the work from our group indicates that proteasomes may be involved in regulation of alternative splicing [27].…”

Section: Introductionmentioning

confidence: 99%

DNA damage modulates interactions between microRNAs and the 26S proteasome

et al. 2014

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26S proteasomes are known as major non-lysosomal cellular machines for coordinated and specific destruction of ubiquitinylated proteins. The proteolytic activities of proteasomes are controlled by various post-translational modifications in response to environmental cues, including DNA damage. Besides proteolysis, proteasomes also associate with RNA hydrolysis and splicing. Here, we extend the functional diversity of proteasomes by showing that they also dynamically associate with microRNAs (miRNAs) both in the nucleus and cytoplasm of cells. Moreover, DNA damage induced by an anti-cancer drug, doxorubicin, alters the repertoire of proteasome-associated miRNAs, enriching the population of miRNAs that target cell cycle checkpoint regulators and DNA repair proteins. Collectively, these data uncover yet another potential mode of action for proteasomes in the cell via their dynamic association with microRNAs.

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26S proteasome exhibits endoribonuclease activity controlled by extra-cellular stimuli

Cited by 39 publications

References 55 publications

Proteomic profiling of rapid non-genomic and concomitant genomic effects of acute restraint stress on rat thymocytes

Proteomic profiling of rapid non-genomic and concomitant genomic effects of acute restraint stress on rat thymocytes

Precise assembly and regulation of 26S proteasome and correlation between proteasome dysfunction and neurodegenerative diseases

DNA damage modulates interactions between microRNAs and the 26S proteasome

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