2018
DOI: 10.1016/bs.ircmb.2018.05.003
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Coordinating Mitochondrial Biology Through the Stress-Responsive Regulation of Mitochondrial Proteases

Abstract: Proteases are localized throughout mitochondria and function as critical regulators of all aspects of mitochondrial biology. As such, the activities of these proteases are sensitively regulated through transcriptional and post-translational mechanisms to adapt mitochondrial function to specific cellular demands. Here, we discuss the stress-responsive mechanisms responsible for regulating mitochondrial protease activity and the implications of this regulation on mitochondrial function. Furthermore, we describe … Show more

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Cited by 20 publications
(13 citation statements)
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References 225 publications
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“…These changes are expected to result in reduced oxidative damage to proteins and, due to reduced accumulation of protein aggregates, in the higher protein turnover rates observed in JNK gain‐of‐function conditions. While JNK‐induced NADPH production thus likely directly prevents oxidation‐induced protein misfolding and aggregation (Dahl, Gray, & Jakob, ), we cannot rule out the possibility that changes in neuronal carbon flux also influence the activity of specific parts of the proteostasis network, including proteasome activity, autophagy flux, and/or mitochondrial proteostasis by, for example, influencing the activity of Lon protease (Lebeau, Rainbolt, & Wiseman, ). Interestingly, the master regulator of the antioxidant response, CncC (the Drosophila homologue of Nrf2), transcriptionally regulates proteasome levels in flies (Grimberg, Beskow, Lundin, Davis, & Young, ).…”
Section: Discussionmentioning
confidence: 98%
“…These changes are expected to result in reduced oxidative damage to proteins and, due to reduced accumulation of protein aggregates, in the higher protein turnover rates observed in JNK gain‐of‐function conditions. While JNK‐induced NADPH production thus likely directly prevents oxidation‐induced protein misfolding and aggregation (Dahl, Gray, & Jakob, ), we cannot rule out the possibility that changes in neuronal carbon flux also influence the activity of specific parts of the proteostasis network, including proteasome activity, autophagy flux, and/or mitochondrial proteostasis by, for example, influencing the activity of Lon protease (Lebeau, Rainbolt, & Wiseman, ). Interestingly, the master regulator of the antioxidant response, CncC (the Drosophila homologue of Nrf2), transcriptionally regulates proteasome levels in flies (Grimberg, Beskow, Lundin, Davis, & Young, ).…”
Section: Discussionmentioning
confidence: 98%
“…Therefore, N-terminomics approaches have been used to characterize the new N-termini in various organisms, from yeast to mammals (10)(11)(12). These studies have shown that besides the major mitochondrial processing peptidase that cleaves the transit peptide, the system includes aminopeptidases that trim the N-terminal end to create ragged termini and stabilize the proteins (10,13). Mitochondrial proteomics has also been used to investigate the modulations of the mitochondrial proteome in response to various biological situations, ranging from alterations of mitochondrial DNA (14,15) to various physiopathological situations such as aging (16)(17)(18), exposure to ionizing radiations (19), metal toxicity (20) and various metabolic (21)(22)(23)(24)(25) and iatrogenic (21,(26)(27)(28)(29) perturbations.…”
Section: Introductionmentioning
confidence: 99%
“…Mitochondrial proteases function to eliminate damaged or misfolded proteins inside mitochondria. There are four AAA+-ATP-dependent proteases responsible for mitochondrial protein quality control, including the i-AAA protease, the m-AAA protease, LON, and ClpXP (Lebeau et al, 2018), which localize to the inner membrane or the mitochondrial matrix. Irreparable proteins are unfolded through an ATP-dependent process mediated by the AAA+ domains of these proteases (Puchades et al, 2017) and are, subsequently, translocated to a protected proteolytic core for degradation.…”
Section: Mitochondrial Proteostasismentioning
confidence: 99%