Mitochondrial Protein Quality Control Systems in Aging and Disease

2010 ◽  
pp. 108-125 ◽  
Author(s):  
Karin Luce ◽  
Andrea C. Weil ◽  
Heinz D. Osiewacz
Keyword(s):  
Quality Control ◽  
Control Systems ◽  
Protein Quality ◽  
Mitochondrial Protein ◽  
Protein Quality Control

Protein quality control at the mitochondrion

2016 ◽  
Vol 60 (2) ◽  
pp. 213-225 ◽  
Author(s):  
Wolfgang Voos ◽  
Witold Jaworek ◽  
Anne Wilkening ◽  
Michael Bruderek
Keyword(s):  
Quality Control ◽  
Structural Integrity ◽  
Protein Quality ◽  
Mitochondrial Protein ◽  
Protein Quality Control ◽  
Eukaryotic Cell ◽  
Control Mechanisms ◽  
Biochemical Processes ◽  
Unfolded Protein ◽  
Protein Response

Mitochondria are essential constituents of a eukaryotic cell by supplying ATP and contributing to many mayor metabolic processes. As endosymbiotic organelles, they represent a cellular subcompartment exhibiting many autonomous functions, most importantly containing a complete endogenous machinery responsible for protein expression, folding and degradation. This article summarizes the biochemical processes and the enzymatic components that are responsible for maintaining mitochondrial protein homoeostasis. As mitochondria lack a large part of the required genetic information, most proteins are synthesized in the cytosol and imported into the organelle. After reaching their destination, polypeptides must fold and assemble into active proteins. Under pathological conditions, mitochondrial proteins become misfolded or damaged and need to be repaired with the help of molecular chaperones or eventually removed by specific proteases. Failure of these protein quality control mechanisms results in loss of mitochondrial function and structural integrity. Recently, novel mechanisms have been identified that support mitochondrial quality on the organellar level. A mitochondrial unfolded protein response allows the adaptation of chaperone and protease activities. Terminally damaged mitochondria may be removed by a variation of autophagy, termed mitophagy. An understanding of the role of protein quality control in mitochondria is highly relevant for many human pathologies, in particular neurodegenerative diseases.

Mitochondrial protein quality control: Implications in ageing

2008 ◽  
Vol 3 (6) ◽  
pp. 757-764 ◽  
Author(s):  
Bertrand Friguet ◽  
Anne-Laure Bulteau ◽  
Isabelle Petropoulos
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Mitochondrial Protein ◽  
Protein Quality Control

scholarly journals Mitochondrial Protein Quality Control: The Mechanisms Guarding Mitochondrial Health

2015 ◽  
Vol 22 (12) ◽  
pp. 977-994 ◽  
Author(s):  
Iryna Bohovych ◽  
Sherine S.L. Chan ◽  
Oleh Khalimonchuk
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Mitochondrial Protein ◽  
Protein Quality Control

scholarly journals Chaperone-mediated autophagy: dedicated saviour and unfortunate victim in the neurodegeneration arena

2013 ◽  
Vol 41 (6) ◽  
pp. 1483-1488 ◽  
Author(s):  
Jaime L. Schneider ◽  
Ana Maria Cuervo
Keyword(s):  
Quality Control ◽  
Neurodegenerative Diseases ◽  
Disease Progression ◽  
Control Systems ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Dual Role ◽  
Selective Degradation ◽  
Main Components ◽  
Chaperone Mediated Autophagy

The importance of cellular quality-control systems in the maintenance of neuronal homoeostasis and in the defence against neurodegeneration is well recognized. Chaperones and proteolytic systems, the main components of these cellular surveillance mechanisms, are key in the fight against the proteotoxicity that is often associated with severe neurodegenerative diseases. However, in recent years, a new theme has emerged which suggests that components of protein quality-control pathways are often targets of the toxic effects of pathogenic proteins and that their failure to function properly contributes to pathogenesis and disease progression. In the present mini-review, we describe this dual role as ‘saviour’ and ‘victim’ in the context of neurodegeneration for chaperone-mediated autophagy, a cellular pathway involved in the selective degradation of cytosolic proteins in lysosomes.

scholarly journals ER-associated degradation: Protein quality control and beyond

2014 ◽  
Vol 204 (6) ◽  
pp. 869-879 ◽  
Author(s):  
Annamaria Ruggiano ◽  
Ombretta Foresti ◽  
Pedro Carvalho
Keyword(s):  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Protein Degradation ◽  
Control Systems ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Secretory Proteins ◽  
Toxic Species ◽  
Cellular Factors

Even with the assistance of many cellular factors, a significant fraction of newly synthesized proteins ends up misfolded. Cells evolved protein quality control systems to ensure that these potentially toxic species are detected and eliminated. The best characterized of these pathways, the ER-associated protein degradation (ERAD), monitors the folding of membrane and secretory proteins whose biogenesis takes place in the endoplasmic reticulum (ER). There is also increasing evidence that ERAD controls other ER-related functions through regulated degradation of certain folded ER proteins, further highlighting the role of ERAD in cellular homeostasis.

scholarly journals Age-associated declines in mitochondrial biogenesis and protein quality control factors are minimized by exercise training

2012 ◽  
Vol 303 (2) ◽  
pp. R127-R134 ◽  
Author(s):  
Erika Koltai ◽  
Nikolett Hart ◽  
Albert W. Taylor ◽  
Sataro Goto ◽  
Jenny K. Ngo ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Quality Control ◽  
Exercise Training ◽  
Mitochondrial Biogenesis ◽  
Protein Quality ◽  
Mitochondrial Protein ◽  
Protein Quality Control ◽  
Treadmill Running ◽  
Common Finding ◽  
Moderate Intensity

A decline in mitochondrial biogenesis and mitochondrial protein quality control in skeletal muscle is a common finding in aging, but exercise training has been suggested as a possible cure. In this report, we tested the hypothesis that moderate-intensity exercise training could prevent the age-associated deterioration in mitochondrial biogenesis in the gastrocnemius muscle of Wistar rats. Exercise training, consisting of treadmill running at 60% of the initial V̇o2max, reversed or attenuated significant age-associated (detrimental) declines in mitochondrial mass (succinate dehydrogenase, citrate synthase, cytochrome- c oxidase-4, mtDNA), SIRT1 activity, AMPK, pAMPK, and peroxisome proliferator-activated receptor gamma coactivator 1-α, UCP3, and the Lon protease. Exercise training also decreased the gap between young and old animals in other measured parameters, including nuclear respiratory factor 1, mitochondrial transcription factor A, fission-1, mitofusin-1, and polynucleotide phosphorylase levels. We conclude that exercise training can help minimize detrimental skeletal muscle aging deficits by improving mitochondrial protein quality control and biogenesis.

The role of protein quality control in mitochondrial protein homeostasis under oxidative stress

PROTEOMICS ◽  
2010 ◽  
Vol 10 (7) ◽  
pp. 1426-1443 ◽  
Author(s):  
Tom Bender ◽  
Claudia Leidhold ◽  
Thomas Ruppert ◽  
Sebastian Franken ◽  
Wolfgang Voos
Keyword(s):  
Oxidative Stress ◽  
Quality Control ◽  
Protein Quality ◽  
Mitochondrial Protein ◽  
Protein Quality Control ◽  
Protein Homeostasis
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