Cross-talk between redox regulation and the ubiquitin–proteasome system in mammalian cell differentiation

Demasi, Marilene; Simões, Vanessa; Bonatto, Diego

doi:10.1016/j.bbagen.2014.10.031

Cited by 14 publications

(8 citation statements)

References 175 publications

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“…In addition to its major role in antigen processing, the immunoproteasome seems to degrade oxidized proteins more efficiently than the standard 20S CP (70, 71). De novo synthesis of 20S proteasome and of immunoproteasome is crucially important for maintaining efficient proteostasis in oxidative stress conditions (49).…”

Section: Discussionmentioning

confidence: 99%

Mass Spectrometry-based Absolute Quantification of 20S Proteasome Status for Controlled Ex-vivo Expansion of Human Adipose-derived Mesenchymal Stromal/Stem Cells

Menneteau

Fabre

Garrigues

et al. 2019

Molecular & Cellular Proteomics

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20S proteasomes are very heterogeneous protein complexes involved in many cellular processes. In the present study, we combined an MRM-based assay with the production and purification of entire SILAC labelled proteasome to monitor absolute quantities of the different 20S proteasome subtypes in various human cells and tissues. This method applied to adipocyte-derived stem cells (ADSCs) amplified under various conditions highlights an increased expression of immunoproteasome when this type of cell is primed with IFNγ or amplified in a 20% O 2 environment.

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Section: Discussionmentioning

confidence: 99%

Mass Spectrometry-based Absolute Quantification of 20S Proteasome Status for Controlled Ex-vivo Expansion of Human Adipose-derived Mesenchymal Stromal/Stem Cells

Menneteau

Fabre

Garrigues

et al. 2019

Molecular & Cellular Proteomics

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“…In this review, we will focus exclusively on the chaperone arm of the proteostasis network, since regulation of the proteasomal system and its role during oxidative stress has been expertly reviewed in the very recent past (78, 79, 86). We will discuss several groups of redox-regulated chaperones; first the prototypical prokaryotic 33 kDa h eat s hock p rotein (Hsp33), then a number of multifunctional cellular components that gain chaperone activity under oxidative stress conditions: i) the eukaryotic ATPase Get3/TRC40; ii) the bacteria enamine/imine deaminase RidA; iii) the mammalian protein α2-macroglobulin; and iv) the prebiotic inorganic polymer polyphosphate (polyP).…”

Section: The Challenge Of Oxidative Stress: Maintaining Proteostasismentioning

confidence: 99%

Protein Quality Control under Oxidative Stress Conditions

Dahl

Gray

Jakob

2015

Journal of Molecular Biology

162

137

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Accumulation of reactive oxygen and chlorine species (RO/CS) is generally regarded to be a toxic and highly undesirable event, which serves as contributing factor in aging and many age-related diseases. However, it is also put to excellent use during host defense, when high levels of RO/CS are produced to kill invading microorganisms and regulate bacterial colonization. Biochemical and cell biological studies of how bacteria and other microorganisms deal with RO/CS have now provided important new insights into the physiological consequences of oxidative stress, the major targets that need protection, and the cellular strategies employed by organisms to mitigate the damage. This review examines the redox-regulated mechanisms by which cells maintain a functional proteome during oxidative stress. We will discuss the well-characterized redox-regulated chaperone Hsp33, and review recent discoveries demonstrating that oxidative stress-specific activation of chaperone function is a much more widespread phenomenon than previously anticipated. New members of this group include the cytosolic ATPase Get3 in yeast, the E. coli protein RidA, and the mammalian protein α2-macroglobin. We will conclude our review with recent evidence showing that inorganic polyphosphate (polyP), whose accumulation significantly increases bacterial oxidative stress resistance, works by a protein-like chaperone mechanism. Understanding the relationship between oxidative and proteotoxic stresses will improve our understanding of both host-microbe interactions and of how mammalian cells combat the damaging side effects of uncontrolled RO/CS production, a hallmark of inflammation.

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“…29 The role of UPS and regulation of redox processes have emerged as essential factors to control the fate of cells upon differentiation. 30 This is coherent with the role of reactive oxygen species (ROS) affecting the conjugation of those ubiquitin family members that contribute to an appropriate response to chemotherapy. 31 The analysis of ubiquitylated proteins associated to cellular events continues to be a difficult task partly due to the highly dynamic and reversible formation of ubiquitin chains.…”

Section: Discussionmentioning

confidence: 82%

Analysis of defective protein ubiquitylation associated to adriamycin resistant cells

Lang¹,

Aillet²,

Xolalpa³

et al. 2017

Cell Cycle

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DNA damage activated by Adriamycin (ADR) promotes ubiquitin-proteasome system-mediated proteolysis by stimulating both the activity of ubiquitylating enzymes and the proteasome. In ADR-resistant breast cancer MCF7 (MCF7) cells, protein ubiquitylation is significantly reduced compared to the parental MCF7 cells. Here, we used tandem ubiquitin-binding entities (TUBEs) to analyze the ubiquitylation pattern observed in MCF7 or MCF7 cells. While in MCF7, the level of total ubiquitylation increased up to six-fold in response to ADR, in MCF7 cells only a two-fold response was found. To further explore these differences, we looked for cellular factors presenting ubiquitylation defects in MCF7 cells. Among them, we found the tumor suppressor p53 and its ubiquitin ligase, Mdm2. We also observed a drastic decrease of proteins known to integrate the TUBE-associated ubiquitin proteome after ADR treatment of MCF7 cells, like histone H2AX, HMGB1 or β-tubulin. Only the proteasome inhibitor MG132, but not the autophagy inhibitor chloroquine partially recovers the levels of total protein ubiquitylation in MCF7 cells. p53 ubiquitylation is markedly increased in MCF7 cells after proteasome inhibition or a short treatment with the isopeptidase inhibitor PR619, suggesting an active role of these enzymes in the regulation of this tumor suppressor. Notably, MG132 alone increases apoptosis of MCF7 and multidrug resistant ovarian cancer A2780DR1 and A2780DR2 cells. Altogether, our results highlight the use of ubiquitylation defects to predict resistance to ADR and underline the potential of proteasome inhibitors to treat these chemoresistant cells.

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Cross-talk between redox regulation and the ubiquitin–proteasome system in mammalian cell differentiation

Cited by 14 publications

References 175 publications

Mass Spectrometry-based Absolute Quantification of 20S Proteasome Status for Controlled Ex-vivo Expansion of Human Adipose-derived Mesenchymal Stromal/Stem Cells

Mass Spectrometry-based Absolute Quantification of 20S Proteasome Status for Controlled Ex-vivo Expansion of Human Adipose-derived Mesenchymal Stromal/Stem Cells

Protein Quality Control under Oxidative Stress Conditions

Analysis of defective protein ubiquitylation associated to adriamycin resistant cells

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