Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/200946
Type: Artigo de periódico
Title: Redox Regulation Of The Proteasome Via S-glutathionylation.
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
Abstract: 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.
Subject: 20spt, 20s Proteasome Core Particle
26spt, 26s Proteasome
Gsh, Reduced Glutathione
Gssg, Oxidized Glutathione
Oxidized Proteins
Proteasomal Gating
Proteasome
Ros, Reactive Oxygen Species
Redox Regulation
S-glutathionylation
Saxs, Small Angle X-rays Scattering
Tem, Transmission Electron Microscopy
Rights: aberto
Identifier DOI: 10.1016/j.redox.2013.12.003
Address: http://www.ncbi.nlm.nih.gov/pubmed/24396728
Date Issue: 2014
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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