Proteomic analysis of the 20S proteasome (PSMA3)-interacting proteins reveals a functional link between the proteasome and mRNA metabolism

Fedorova, Olga; Moiseeva, Tatiana N.; Aa, Nikiforov; Цимоха, А. С.; Livinskaya, Veronika A.; Hodson, Mark; Bottrill, Andrew R.; Evteeva, I. N.; Ermolayeva, Julia B.; Kuznetzova, Irina M.; Turoverov, Konstantin K.; Eperon, Ian C.; Barlev, Nickolai A.

doi:10.1016/j.bbrc.2011.10.126

Cited by 45 publications

(31 citation statements)

References 22 publications

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“…These data are consistent with the data published earlier that proteasomes are highly enriched with Hsp90 proteins [49]. Our own observations that the alpha7 (PSMA3) subunit of the 20S complex interacts with Hsp90 are in line with this hypothesis [27]. Taking these facts together, it is likely that 26S proteasomes interact via Hsp90 with RISC complexes loaded with miRNAs and hence gain access to the pool of different miRNAs.…”

Section: Discussionsupporting

confidence: 92%

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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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Section: Discussionsupporting

confidence: 92%

“…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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“…Moreover, a proteomic approach revealed that the a 7 subunit interacts with proteins involved in the processing and splicing of RNA (Fedorova et al, 2011). The b ring also forms a central chamber where the peptidylglutamyl-like (cleaving after acidic residues), trypsin-like (cleaving after basic residues) and chymotrypsin-like (cleaving after hydrophobic residues) activities of the 20S proteasome are mediated by the b 1 , b 2 and b 5 subunits, respectively (Fig.…”

Section: Proteasomementioning

confidence: 99%

Role of the ubiquitin–proteasome system in brain ischemia: Friend or foe?

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Salazar

Curcio

et al. 2014

Progress in Neurobiology

110

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A B S T R A C TThe ubiquitin-proteasome system (UPS) is a catalytic machinery that targets numerous cellular proteins for degradation, thus being essential to control a wide range of basic cellular processes and cell survival. Degradation of intracellular proteins via the UPS is a tightly regulated process initiated by tagging a target protein with a specific ubiquitin chain. Neurons are particularly vulnerable to any change in protein composition, and therefore the UPS is a key regulator of neuronal physiology. Alterations in UPS activity may induce pathological responses, ultimately leading to neuronal cell death. Brain ischemia triggers a complex series of biochemical and molecular mechanisms, such as an inflammatory response, an exacerbated production of misfolded and oxidized proteins, due to oxidative stress, and the breakdown of cellular integrity mainly mediated by excitotoxic glutamatergic signaling. Brain ischemia also damages protein degradation pathways which, together with the overproduction of damaged proteins and consequent upregulation of ubiquitin-conjugated proteins, contribute to the accumulation of ubiquitincontaining proteinaceous deposits. Despite recent advances, the factors leading to deposition of such aggregates after cerebral ischemic injury remain poorly understood. This review discusses the current knowledge on the role of the UPS in brain function and the molecular mechanisms contributing to UPS dysfunction in brain ischemia with consequent accumulation of ubiquitin-containing proteins. Chemical inhibitors of the proteasome and small molecule inhibitors of deubiquitinating enzymes, which promote the degradation of proteins by the proteasome, were both shown to provide neuroprotection in brain ischemia, and this apparent contradiction is also discussed in this review. ß

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“…Multiple sclerosis patients were shown to generate antibodies to hnRNP A1 [26]. This splicing signal affecting splicing and post-transcriptional modifi- Allele and genotype presentation in MS patients and controls: Ars11543947; B -rs2348071; (1 -control; 2 -MS (multiple sclerosis); 3, 4 -RRMS and SPMS (relapsing remitting and secondary progressive MS course respectively)) cation of majority of expressed genes in mammals, was shown to interact directly with PSMA3 proteins [29] and may be potentially involved in regulation of the PSMA3 gene expression through the rs2348071 allelespecific targeting. In our previous studies, the rs2348071 heterozygotes were identified also as risk factor in Latvians for juvenile idiopathic arthritis [22], obesity in children with family history [30] and children bronchial asthma (own unpublished observation).…”

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confidence: 99%