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Redox regulation of the proteasome via S-glutathionylation()

The proteasome is a multimeric and multicatalytic intracellular protease responsible for the degradation of proteins involved in cell cycle control, various signaling processes, antigen presentation, and control of protein synthesis. The central catalytic complex of the proteasome is called the 20S...

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Autores principales: Demasi, Marilene, Netto, Luis E.S., Silva, Gustavo M., Hand, Adrian, de Oliveira, Cristiano L.P., Bicev, Renata N., Gozzo, Fabio, Barros, Mario H., Leme, Janaina M.M., Ohara, Erina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3881202/
https://www.ncbi.nlm.nih.gov/pubmed/24396728
http://dx.doi.org/10.1016/j.redox.2013.12.003
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author Demasi, Marilene
Netto, Luis E.S.
Silva, Gustavo M.
Hand, Adrian
de Oliveira, Cristiano L.P.
Bicev, Renata N.
Gozzo, Fabio
Barros, Mario H.
Leme, Janaina M.M.
Ohara, Erina
author_facet Demasi, Marilene
Netto, Luis E.S.
Silva, Gustavo M.
Hand, Adrian
de Oliveira, Cristiano L.P.
Bicev, Renata N.
Gozzo, Fabio
Barros, Mario H.
Leme, Janaina M.M.
Ohara, Erina
author_sort Demasi, Marilene
collection PubMed
description The proteasome is a multimeric and multicatalytic intracellular protease responsible for the degradation of proteins involved in cell cycle control, various signaling processes, antigen presentation, and control of protein synthesis. The central catalytic complex of the proteasome is called the 20S core particle. The majority of these are flanked on one or both sides by regulatory units. Most common among these units is the 19S regulatory unit. When coupled to the 19S unit, the complex is termed the asymmetric or symmetric 26S proteasome depending on whether one or both sides are coupled to the 19S unit, respectively. The 26S proteasome recognizes poly-ubiquitinylated substrates targeted for proteolysis. Targeted proteins interact with the 19S unit where they are deubiquitinylated, unfolded, and translocated to the 20S catalytic chamber for degradation. The 26S proteasome is responsible for the degradation of major proteins involved in the regulation of the cellular cycle, antigen presentation and control of protein synthesis. Alternatively, the proteasome is also active when dissociated from regulatory units. This free pool of 20S proteasome is described in yeast to mammalian cells. The free 20S proteasome degrades proteins by a process independent of poly-ubiquitinylation and ATP consumption. Oxidatively modified proteins and other substrates are degraded in this manner. The 20S proteasome comprises two central heptamers (β-rings) where the catalytic sites are located and two external heptamers (α-rings) that are responsible for proteasomal gating. Because the 20S proteasome lacks regulatory units, it is unclear what mechanisms regulate the gating of α-rings between open and closed forms. In the present review, we discuss 20S proteasomal gating modulation through a redox mechanism, namely, S-glutathionylation of cysteine residues located in the α-rings, and the consequence of this post-translational modification on 20S proteasomal function.
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spelling pubmed-38812022014-01-06 Redox regulation of the proteasome via S-glutathionylation() Demasi, Marilene Netto, Luis E.S. Silva, Gustavo M. Hand, Adrian de Oliveira, Cristiano L.P. Bicev, Renata N. Gozzo, Fabio Barros, Mario H. Leme, Janaina M.M. Ohara, Erina Redox Biol Review Article The proteasome is a multimeric and multicatalytic intracellular protease responsible for the degradation of proteins involved in cell cycle control, various signaling processes, antigen presentation, and control of protein synthesis. The central catalytic complex of the proteasome is called the 20S core particle. The majority of these are flanked on one or both sides by regulatory units. Most common among these units is the 19S regulatory unit. When coupled to the 19S unit, the complex is termed the asymmetric or symmetric 26S proteasome depending on whether one or both sides are coupled to the 19S unit, respectively. The 26S proteasome recognizes poly-ubiquitinylated substrates targeted for proteolysis. Targeted proteins interact with the 19S unit where they are deubiquitinylated, unfolded, and translocated to the 20S catalytic chamber for degradation. The 26S proteasome is responsible for the degradation of major proteins involved in the regulation of the cellular cycle, antigen presentation and control of protein synthesis. Alternatively, the proteasome is also active when dissociated from regulatory units. This free pool of 20S proteasome is described in yeast to mammalian cells. The free 20S proteasome degrades proteins by a process independent of poly-ubiquitinylation and ATP consumption. Oxidatively modified proteins and other substrates are degraded in this manner. The 20S proteasome comprises two central heptamers (β-rings) where the catalytic sites are located and two external heptamers (α-rings) that are responsible for proteasomal gating. Because the 20S proteasome lacks regulatory units, it is unclear what mechanisms regulate the gating of α-rings between open and closed forms. In the present review, we discuss 20S proteasomal gating modulation through a redox mechanism, namely, S-glutathionylation of cysteine residues located in the α-rings, and the consequence of this post-translational modification on 20S proteasomal function. Elsevier 2013-12-14 /pmc/articles/PMC3881202/ /pubmed/24396728 http://dx.doi.org/10.1016/j.redox.2013.12.003 Text en © 2013 The Authors http://creativecommons.org/licenses/by-nc-nd/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-No Derivative Works License, which permits non-commercial use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Review Article
Demasi, Marilene
Netto, Luis E.S.
Silva, Gustavo M.
Hand, Adrian
de Oliveira, Cristiano L.P.
Bicev, Renata N.
Gozzo, Fabio
Barros, Mario H.
Leme, Janaina M.M.
Ohara, Erina
Redox regulation of the proteasome via S-glutathionylation()
title Redox regulation of the proteasome via S-glutathionylation()
title_full Redox regulation of the proteasome via S-glutathionylation()
title_fullStr Redox regulation of the proteasome via S-glutathionylation()
title_full_unstemmed Redox regulation of the proteasome via S-glutathionylation()
title_short Redox regulation of the proteasome via S-glutathionylation()
title_sort redox regulation of the proteasome via s-glutathionylation()
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3881202/
https://www.ncbi.nlm.nih.gov/pubmed/24396728
http://dx.doi.org/10.1016/j.redox.2013.12.003
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