Chaperone–protease networks in mitochondrial protein homeostasis

Voos, Wolfgang

doi:10.1016/j.bbamcr.2012.06.005

Cited by 186 publications

(173 citation statements)

References 155 publications

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“…Heat shock protein 60 has long been suggested to play an anti-apoptotic role in the cell (Shan et al, 2003) and control protein homestasis (Voos, 2013). A total of 3 spots were identified as HSP60 and all were increased in the low RFI line in the between RFI line comparison.…”

Section: Discussionmentioning

confidence: 99%

Liver and skeletal muscle mitochondria proteomes are altered in pigs divergently selected for residual feed intake1,2

Grubbs

Huff-Lonergan

Gabler

et al. 2014

Journal of Animal Science

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Animals selected for residual feed intake (RFI) can be used as a model to elucidate molecular explanations for differences in growth efficiency. The objective of this study was to determine the extent to which the protein profile and posttranslational modifications of mitochondria from skeletal muscle and liver relate to feed efficiency gains in pigs divergently selected for RFI. Mitochondria were isolated from the longissimus dorsi (LD) muscle and the liver from pigs (n = 9 each for the high and low RFI line; BW = 95.8 kg). Mitochondria protein profile differences were determined using two-dimensional difference in gel electrophoresis. Proteins were identified using electrospray ionization mass spectrometry. In the line comparison, the β subunit of ATP synthase, heat shock protein (HSP) 60, and HSP70, were identified as being increased in mitochondria from the liver of the low RFI line (23 to 50%; P < 0.1). These differences were not observed in the other comparisons. In the LD, proteins identified as being different between RFI phenotypes included HSP70 and subunit 1 of the cytochrome bc1 complex. These data indicate that genetic selection for RFI tends to result in a consistent change in mitochondrial protein profile. In contrast, classification by phenotype demonstrates that phenotypic differences in RFI are not specifically associated with alterations of the mitochondria protein profile. ABSTRACT: Animals selected for residual feed intake (RFI) can be used as a model to elucidate molecular explanations for differences in growth efficiency. The objective of this study was to determine the extent to which the protein profile and posttranslational modifications of mitochondria from skeletal muscle and liver relate to feed efficiency gains in pigs divergently selected for RFI. Mitochondria were isolated from the longissimus dorsi (LD) muscle and the liver from pigs (n = 9 each for the high and low RFI line; BW = 95.8 kg). Mitochondria protein profile differences were determined using twodimensional difference in gel electrophoresis. Proteins were identified using electrospray ionization mass spectrometry. In the line comparison, the β subunit of ATP synthase, heat shock protein (HSP) 60, and HSP70, were identified as being increased in mitochondria from the liver of the low RFI line (23 to 50%; P < 0.1). These differences were not observed in the other comparisons. In the LD, proteins identified as being different between RFI phenotypes included HSP70 and subunit 1 of the cytochrome bc1 complex. These data indicate that genetic selection for RFI tends to result in a consistent change in mitochondrial protein profile. In contrast, classification by phenotype demonstrates that phenotypic differences in RFI are not specifically associated with alterations of the mitochondria protein profile.

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Section: Discussionmentioning

confidence: 99%

Liver and skeletal muscle mitochondria proteomes are altered in pigs divergently selected for residual feed intake1,2

Grubbs

Huff-Lonergan

Gabler

et al. 2014

Journal of Animal Science

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“…The samples were held in a fixative without a detergent overnight at 4°C. The muscles were postfixed in 1% OsO 4 , en bloc stained with 1% uranyl acetate, dehydrated in an ethanol series, embedded in Embed 812 resin (Electron Microscopy Sciences, Hatfield, PA, USA) and cured at 60°C for 2 days. Sections were stained with uranyl acetate and lead citrate and examined with a JEM 1400 electron microscope (JEOL, Pleasanton, CA, USA) equipped with an AMT XR-111 digital camera (Advanced Microscopy Techniques, Wobrun, MA, USA).…”

Section: Discussionmentioning

confidence: 99%

“…4 The proteases are located in different submitochondrial compartments and carry out critical steps of mitochondrial biogenesis and turnover, including processing, assembly and degradation of mitochondrial proteins. Mitochondrial proteases of the AAA class (ATPases Associated with diverse cellular Activities) are the main regulators of proteostasis on the IMM, 5 which houses many important complexes including those of the ETC.…”

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confidence: 99%

Loss of Drosophila i-AAA protease, dYME1L, causes abnormal mitochondria and apoptotic degeneration

Liu

Daniels

et al. 2015

Cell Death Differ

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Mitochondrial AAA (ATPases Associated with diverse cellular Activities) proteases i-AAA (intermembrane space-AAA) and m-AAA (matrix-AAA) are closely related and have major roles in inner membrane protein homeostasis. Mutations of m-AAA proteases are associated with neuromuscular disorders in humans. However, the role of i-AAA in metazoans is poorly understood. We generated a deletion affecting Drosophila i-AAA, dYME1L (dYME1L del ). Mutant flies exhibited premature aging, progressive locomotor deficiency and neurodegeneration that resemble some key features of m-AAA diseases. dYME1L del flies displayed elevated mitochondrial unfolded protein stress and irregular cristae. Aged dYME1L del flies had reduced complex I (NADH/ubiquinone oxidoreductase) activity, increased level of reactive oxygen species (ROS), severely disorganized mitochondrial membranes and increased apoptosis. Furthermore, inhibiting apoptosis by targeting dOmi (Drosophila Htra2/Omi) or DIAP1, or reducing ROS accumulation suppressed retinal degeneration. Our results suggest that i-AAA is essential for removing unfolded proteins and maintaining mitochondrial membrane architecture. Loss of i-AAA leads to the accumulation of oxidative damage and progressive deterioration of membrane integrity, which might contribute to apoptosis upon the release of proapoptotic molecules such as dOmi. Containing ROS level could be a potential strategy to manage mitochondrial AAA protease deficiency.

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“…Quality control of mitochondrial proteins is described in detail elsewhere (e.g. [11,114]). The specific degradation of dysfunctional mitochondria ("mitophagy") is carried out by the lysosomal-autophagic machinery after the dysfunctional organelles have been marked for destruction.…”

Section: Mitochondrial Degradationmentioning

confidence: 99%

Regulation and Quantification of Cellular Mitochondrial Morphology and Content

Tronstad¹,

Nooteboom²,

Nilsson³

et al. 2014

CPD

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Running title: Regulation and quantification of mitochondrial morphology and content. Word count: 15,454 (total)Characters: 107,091 (including spaces); 92,067 (excluding spaces) Keywords: mitochondrial biogenesis, mitochondrial dynamics, mitochondrial degradation, living cells, TMRM, microscopy, segmentation, image analysis.Page 2 of 37 ABSTRACTMitochondria play a key role in signal transduction, redox homeostasis and cell survival, which extends far beyond their classical functioning in ATP production and energy metabolism. In living cells, mitochondrial content ("mitochondrial mass") depends on the cell-controlled balance between mitochondrial biogenesis and degradation. These processes are intricately linked to changes in net mitochondrial morphology and spatiotemporal positioning ("mitochondrial dynamics"), which are governed by mitochondrial fusion, fission and motility. It is becoming increasingly clear that mitochondrial mass and dynamics, as well as its ultrastructure and volume, are mechanistically linked to mitochondrial function and the cell. This means that proper quantification of mitochondrial morphology and content is of prime importance in understanding mitochondrial and cellular physiology in health and disease. This review first presents how cellular mitochondrial content is regulated at the level of mitochondrial biogenesis, degradation and dynamics. Next we discuss how mitochondrial dynamics and content can be analyzed with a special emphasis on quantitative live-cell microscopy strategies.

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Chaperone–protease networks in mitochondrial protein homeostasis

Cited by 186 publications

References 155 publications

Liver and skeletal muscle mitochondria proteomes are altered in pigs divergently selected for residual feed intake1,2

Liver and skeletal muscle mitochondria proteomes are altered in pigs divergently selected for residual feed intake1,2

Loss of Drosophila i-AAA protease, dYME1L, causes abnormal mitochondria and apoptotic degeneration

Regulation and Quantification of Cellular Mitochondrial Morphology and Content

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