Redox control of the ubiquitin-proteasome system: from molecular mechanisms to functional significance

Franziska Kriegenburg; Esben G Poulsen; Annett Koch; Elke Krüger; Rasmus Hartmann-Petersen

doi:10.1089/ars.2010.3590

Redox control of the ubiquitin-proteasome system: from molecular mechanisms to functional significance

Franziska Kriegenburg, Esben G Poulsen, Annett Koch, Elke Krüger, Rasmus Hartmann-Petersen

Biomolecular Sciences

50 Citationer (Scopus)

Abstract

In their natural environments, cells are regularly exposed to oxidizing conditions that may lead to protein misfolding. If such misfolded proteins are allowed to linger, they may form insoluble aggregates and pose a serious threat to the cell. Accumulation of misfolded, oxidatively damaged proteins is characteristic of many diseases and during aging. To counter the adverse effects of oxidative stress, cells can initiate an antioxidative response in an attempt to repair the damage, or rapidly channel the damaged proteins for degradation by the ubiquitin-proteasome system (UPS). Recent studies have shown that elements of the oxidative stress response and the UPS are linked on many levels. To manage the extra burden of misfolded proteins, the UPS is induced by oxidative stress, and special proteasome subtypes protect cells against oxidative damage. In addition, the proteasome is directly associated with a thioredoxin and other cofactors that may adjust the particle's response during an oxidative challenge. Here, we give an overview of the UPS and a detailed description of the degradation of oxidized proteins and of the crosstalk between oxidative stress and protein degradation in health and disease.

Originalsprog	Engelsk
Tidsskrift	Antioxidants & Redox Signaling
Vol/bind	15
Udgave nummer	8
Sider (fra-til)	2265-99
Antal sider	35
ISSN	1523-0864
DOI	https://doi.org/10.1089/ars.2010.3590
Status	Udgivet - 15 okt. 2011

Adgang til dokumentet

10.1089/ars.2010.3590

Citationsformater

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title = "Redox control of the ubiquitin-proteasome system: from molecular mechanisms to functional significance",

abstract = "In their natural environments, cells are regularly exposed to oxidizing conditions that may lead to protein misfolding. If such misfolded proteins are allowed to linger, they may form insoluble aggregates and pose a serious threat to the cell. Accumulation of misfolded, oxidatively damaged proteins is characteristic of many diseases and during aging. To counter the adverse effects of oxidative stress, cells can initiate an antioxidative response in an attempt to repair the damage, or rapidly channel the damaged proteins for degradation by the ubiquitin-proteasome system (UPS). Recent studies have shown that elements of the oxidative stress response and the UPS are linked on many levels. To manage the extra burden of misfolded proteins, the UPS is induced by oxidative stress, and special proteasome subtypes protect cells against oxidative damage. In addition, the proteasome is directly associated with a thioredoxin and other cofactors that may adjust the particle's response during an oxidative challenge. Here, we give an overview of the UPS and a detailed description of the degradation of oxidized proteins and of the crosstalk between oxidative stress and protein degradation in health and disease.",

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T1 - Redox control of the ubiquitin-proteasome system

T2 - from molecular mechanisms to functional significance

AU - Kriegenburg, Franziska

AU - Poulsen, Esben G

AU - Koch, Annett

AU - Krüger, Elke

AU - Hartmann-Petersen, Rasmus

PY - 2011/10/15

Y1 - 2011/10/15

N2 - In their natural environments, cells are regularly exposed to oxidizing conditions that may lead to protein misfolding. If such misfolded proteins are allowed to linger, they may form insoluble aggregates and pose a serious threat to the cell. Accumulation of misfolded, oxidatively damaged proteins is characteristic of many diseases and during aging. To counter the adverse effects of oxidative stress, cells can initiate an antioxidative response in an attempt to repair the damage, or rapidly channel the damaged proteins for degradation by the ubiquitin-proteasome system (UPS). Recent studies have shown that elements of the oxidative stress response and the UPS are linked on many levels. To manage the extra burden of misfolded proteins, the UPS is induced by oxidative stress, and special proteasome subtypes protect cells against oxidative damage. In addition, the proteasome is directly associated with a thioredoxin and other cofactors that may adjust the particle's response during an oxidative challenge. Here, we give an overview of the UPS and a detailed description of the degradation of oxidized proteins and of the crosstalk between oxidative stress and protein degradation in health and disease.

AB - In their natural environments, cells are regularly exposed to oxidizing conditions that may lead to protein misfolding. If such misfolded proteins are allowed to linger, they may form insoluble aggregates and pose a serious threat to the cell. Accumulation of misfolded, oxidatively damaged proteins is characteristic of many diseases and during aging. To counter the adverse effects of oxidative stress, cells can initiate an antioxidative response in an attempt to repair the damage, or rapidly channel the damaged proteins for degradation by the ubiquitin-proteasome system (UPS). Recent studies have shown that elements of the oxidative stress response and the UPS are linked on many levels. To manage the extra burden of misfolded proteins, the UPS is induced by oxidative stress, and special proteasome subtypes protect cells against oxidative damage. In addition, the proteasome is directly associated with a thioredoxin and other cofactors that may adjust the particle's response during an oxidative challenge. Here, we give an overview of the UPS and a detailed description of the degradation of oxidized proteins and of the crosstalk between oxidative stress and protein degradation in health and disease.

KW - Animals

KW - Humans

KW - Oxidation-Reduction

KW - Oxidative Stress

KW - Proteasome Endopeptidase Complex

KW - Proteins

KW - Ubiquitin

U2 - 10.1089/ars.2010.3590

DO - 10.1089/ars.2010.3590

M3 - Journal article

C2 - 21314436

SN - 1523-0864

VL - 15

SP - 2265

EP - 2299

JO - Antioxidants & Redox Signaling

JF - Antioxidants & Redox Signaling

IS - 8

ER -