Mechanisms Orchestrating Mitochondrial Dynamics for Energy Homeostasis

Yu, Seungyoon B.; Pekkurnaz, Gülçin

doi:10.1016/j.jmb.2018.07.027

Cited by 131 publications

(99 citation statements)

References 179 publications

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“…For instance, mitochondria damaged by oxidative stress undergo fission and subsequently fragmentation (). It has been proposed that mitochondrial fission and fragmentation are parts of the process of mitophagy, removing aberrant mitochondria from cells (Yu and Pekkurnaz, ). A previous study demonstrated that adiponectin represses H 2 O 2 ‐induced mitophagy in C2C12 cells (Ren et al, ).…”

Section: Discussionmentioning

confidence: 99%

Inhibition of ubiquitin‐specific protease 2 causes accumulation of reactive oxygen species, mitochondria dysfunction, and intracellular ATP decrement in C2C12 myoblasts

et al. 2019

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Ubiquitin‐specific protease 2 (USP2) is considered to participate in the differentiation of myoblasts to myotubes, however, its functions in myoblasts under growth conditions remain elusive. In this study, we analyzed the physiological roles of USP2 in myoblasts using Usp2 knockout (KO) C2C12 cells as well as a USP2 specific inhibitor. In addition to the disruption of differentiation, clustered regularly interspaced short palindromic repeats/Cas9‐generated Usp2 KO cells exhibited inhibition of proliferation compared to parental C2C12 cells. Usp2 KO cells reduced the accumulation of intracellular adenosine triphosphate (ATP) content and oxygen consumption. Moreover, Usp2 KO cells had fragmented mitochondria, suggesting that mitochondrial respiration was inactive. The deficiency of Usp2 did not affect the enzymatic activities of respiratory chain complexes I, III, IV, and V. However, mitochondrial membrane permeability—evaluated using calcein AM‐cobalt staining—was increased in Usp2 KO cells. The membrane potential of Usp2 KO cells was clearly decreased. Usp2 KO cells accumulated reactive oxygen species (ROS) in the mitochondria. The USP2‐selective inhibitor ML364 also increased the levels of mitochondrial ROS, and modulated the membrane potential and morphology of the mitochondria. These effects were followed by a decrement in the intracellular content of ATP. Based on these findings, we speculate that USP2 may be involved in maintaining the integrity of the mitochondrial membrane. This process ensures the supply of ATP in myoblasts, presumably leading to proliferation and differentiation.

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Section: Discussionmentioning

confidence: 99%

Inhibition of ubiquitin‐specific protease 2 causes accumulation of reactive oxygen species, mitochondria dysfunction, and intracellular ATP decrement in C2C12 myoblasts

et al. 2019

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“…Mitochondria are highly dynamic organelles. Continuous fission and fusion events preserve the optimal functioning of mitochondria [ 109 , 110 ]. Whereas fission enable segregation and removal of damaged mitochondrial constituents through mitophagy, fusion facilitates exchange of material between the healthy organelles [ 11 , 107 , 108 , 109 , 110 ].…”

Section: Aaa Proteases Maintain Functional and Healthy Mitochondrimentioning

confidence: 99%

“…Continuous fission and fusion events preserve the optimal functioning of mitochondria [ 109 , 110 ]. Whereas fission enable segregation and removal of damaged mitochondrial constituents through mitophagy, fusion facilitates exchange of material between the healthy organelles [ 11 , 107 , 108 , 109 , 110 ]. The balance between mitochondrial fusion and fission is regulated by the relative abundance of unprocessed OPA1 (L-OPA1) and its shorter forms (S-OPA1) [ 107 , 108 , 109 , 110 ].…”

Section: Aaa Proteases Maintain Functional and Healthy Mitochondrimentioning

confidence: 99%

AAA Proteases: Guardians of Mitochondrial Function and Homeostasis

Opalińska

Jańska

2018

Cells

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Mitochondria are dynamic, semi-autonomous organelles that execute numerous life-sustaining tasks in eukaryotic cells. Functioning of mitochondria depends on the adequate action of versatile proteinaceous machineries. Fine-tuning of mitochondrial activity in response to cellular needs involves continuous remodeling of organellar proteome. This process not only includes modulation of various biogenetic pathways, but also the removal of superfluous proteins by adenosine triphosphate (ATP)-driven proteolytic machineries. Accordingly, all mitochondrial sub-compartments are under persistent surveillance of ATP-dependent proteases. Particularly important are highly conserved two inner mitochondrial membrane-bound metalloproteases known as m-AAA and i-AAA (ATPases associated with diverse cellular activities), whose mis-functioning may lead to impaired organellar function and consequently to development of severe diseases. Herein, we discuss the current knowledge of yeast, mammalian, and plant AAA proteases and their implications in mitochondrial function and homeostasis maintenance.

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“…The progressive accumulation of functional impairments in mitochondrial function has been widely recognized as one of the main hallmarks of aging and age-related diseases [1,2]. The age-related mitochondrial decline is partially due to a failure in the fine-tune coordination of mitochondrial turnover mechanisms that regulate the morphology, the size and the number of functional mitochondria under a wide variety of both physiological and non-physiological conditions [3][4][5]. These mechanisms include the increase of mitochondrial mass (biogenesis), the division of a mitochondrion in two or more daughter organelles (fission), the merging of healthy and damaged mitochondria (fusion) and the selective clearance of damaged mitochondria via the autophagic pathway (mitophagy) [4,6,7].…”

Section: Introductionmentioning

confidence: 99%

“…The accumulation of dysfunctional mitochondria leads the drop of mitochondrial energy production, the loss of mitochondrial membrane potential, the burst of damage to cellular macromolecules by mitochondrial Reactive Oxygen Species (ROS), the dysregulation of calcium homeostasis, and alteration in cell growth and death [8]. It follows that the progressive loss in mitochondrial quality control system is decisive in driving toward the overall physiological unbalance typical of aging process [4,5].…”

Section: Introductionmentioning

confidence: 99%

Multi-Tissue DNA Methylation Remodeling at Mitochondrial Quality Control Genes According to Diet in Rat Aging Models

et al. 2020

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An adequate mitochondrial quality control system ensures the maintenance of a healthy mitochondrial pool so as to slow down the progressive accumulation of damage affecting mitochondrial function during aging and diseases. The amount and quality of nutrients availability were demonstrated to induce a process of bioenergetics adaptation by influencing the above system via epigenetic modifications. Here, we analyzed DNA samples from differently-aged rats fed a standard or low-calorie diet to evaluate tissue-specific changes in DNA methylation of CpG sites falling within Polg, Polg2, Tfam, Fis1, and Opa1 genes. We found significant changes according to age and tissue type and the administration of the low-calorie diet is responsible for a prevalent increase in DNA methylation levels. Particularly, this increase was more appreciable when this diet was administered during adulthood and at old age. Regression analysis demonstrated that DNA methylation patterns of the analyzed genes were negatively correlated with their expression levels. Data we obtained provide the first evidence about changes in DNA methylation patterns of genes involved in the mitochondrial biogenesis in response to specific diets and demonstrated that epigenetic modifications are involved in the modulation of mitochondrial dynamics driven by age and nutrition.

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Mechanisms Orchestrating Mitochondrial Dynamics for Energy Homeostasis

Cited by 131 publications

References 179 publications

Inhibition of ubiquitin‐specific protease 2 causes accumulation of reactive oxygen species, mitochondria dysfunction, and intracellular ATP decrement in C2C12 myoblasts

Inhibition of ubiquitin‐specific protease 2 causes accumulation of reactive oxygen species, mitochondria dysfunction, and intracellular ATP decrement in C2C12 myoblasts

AAA Proteases: Guardians of Mitochondrial Function and Homeostasis

Multi-Tissue DNA Methylation Remodeling at Mitochondrial Quality Control Genes According to Diet in Rat Aging Models

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