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      Mitochondrial stress management: a dynamic journey

      review-article
      Author(s): 1 , 2 , 1 , 2 , *
      Publication date (Electronic, pub):
      Publication date (Electronic, collection):
      Journal: Cell Stress
      Publisher: Shared Science Publishers OG
      Keywords: mitochondria, mitochondrial dynamics, oxidative stress, unfolded protein response, mitophagy, mitochondrial biogenesis

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          Abstract

          Mitochondria undergo continuous challenges in the course of their life, from their generation to their degradation. These challenges include the management of reactive oxygen species, the proper assembly of mitochondrial respiratory complexes and the need to balance potential mutations in the mitochondrial DNA. The detection of damage and the ability to keep it under control is critical to fine-tune mitochondrial function to the organismal energy needs. In this review, we will analyze the multiple mechanisms that safeguard mitochondrial function in light of in crescendo damage. This sequence of events will include initial defense against excessive reactive oxygen species production, compensation mechanisms by the unfolded protein response (UPR mt), mitochondrial dynamics and elimination by mitophagy.

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          The integrated stress response.

          Karolina Pakos-Zebrucka, Izabela Koryga, Katarzyna Mnich … (2016)
          In response to diverse stress stimuli, eukaryotic cells activate a common adaptive pathway, termed the integrated stress response (ISR), to restore cellular homeostasis. The core event in this pathway is the phosphorylation of eukaryotic translation initiation factor 2 alpha (eIF2α) by one of four members of the eIF2α kinase family, which leads to a decrease in global protein synthesis and the induction of selected genes, including the transcription factor ATF4, that together promote cellular recovery. The gene expression program activated by the ISR optimizes the cellular response to stress and is dependent on the cellular context, as well as on the nature and intensity of the stress stimuli. Although the ISR is primarily a pro-survival, homeostatic program, exposure to severe stress can drive signaling toward cell death. Here, we review current understanding of the ISR signaling and how it regulates cell fate under diverse types of stress.
          Article 0 comments Cited 927 times – based on 0 reviews     Review now
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            AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha.

            Sibylle Jager, Christoph Handschin, Julie St-Pierre … (2007)
            Activation of AMP-activated kinase (AMPK) in skeletal muscle increases glucose uptake, fatty acid oxidation, and mitochondrial biogenesis by increasing gene expression in these pathways. However, the transcriptional components that are directly targeted by AMPK are still elusive. The peroxisome-proliferator-activated receptor gamma coactivator 1alpha (PGC-1alpha) has emerged as a master regulator of mitochondrial biogenesis; furthermore, it has been shown that PGC-1alpha gene expression is induced by exercise and by chemical activation of AMPK in skeletal muscle. Using primary muscle cells and mice deficient in PGC-1alpha, we found that the effects of AMPK on gene expression of glucose transporter 4, mitochondrial genes, and PGC-1alpha itself are almost entirely dependent on the function of PGC-1alpha protein. Furthermore, AMPK phosphorylates PGC-1alpha directly both in vitro and in cells. These direct phosphorylations of the PGC-1alpha protein at threonine-177 and serine-538 are required for the PGC-1alpha-dependent induction of the PGC-1alpha promoter. These data indicate that AMPK phosphorylation of PGC-1alpha initiates many of the important gene regulatory functions of AMPK in skeletal muscle.
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              Superoxide radical and superoxide dismutases.

              I Fridovich (1995)
              O2- oxidizes the [4Fe-4S] clusters of dehydratases, such as aconitase, causing-inactivation and release of Fe(II), which may then reduce H2O2 to OH- +OH.. SODs inhibit such HO. production by scavengingO2-, but Cu, ZnSODs, by virtue of a nonspecific peroxidase activity, may peroxidize spin trapping agents and thus give the appearance of catalyzing OH. production from H2O2. There is a glycosylated, tetrameric Cu, ZnSOD in the extracellular space that binds to acidic glycosamino-glycans. It minimizes the reaction of O2- with NO. E. coli, and other gram negative microorganisms, contain a periplasmic Cu, ZnSOD that may serve to protect against extracellular O2-. Mn(III) complexes of multidentate macrocyclic nitrogenous ligands catalyze the dismutation of O2- and are being explored as potential pharmaceutical agents. SOD-null mutants have been prepared to reveal the biological effects of O2-. SodA, sodB E. coli exhibit dioxygen-dependent auxotrophies and enhanced mutagenesis, reflecting O2(-)-sensitive biosynthetic pathways and DNA damage. Yeast, lacking either Cu, ZnSOD or MnSOD, are oxygen intolerant, and the double mutant was hypermutable and defective in sporulation and exhibited requirements for methionine and lysine. A Cu, ZnSOD-null Drosophila exhibited a shortened lifespan.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Cell Stress
                Journal ID (iso-abbrev): Cell Stress
                Journal ID (pmc): Cell Stress
                Journal ID (publisher-id): Cell Stress
                Title: Cell Stress
                Publisher: Shared Science Publishers OG
                ISSN (Electronic): 2523-0204
                Publication date (Electronic, pub): 08 October 2018
                Publication date (Electronic, collection): October 2018
                Volume: 2
                Issue: 10
                Pages: 253-274
                Affiliations
                [1 ]Nestlé Institute of Health Sciences (NIHS), EPFL Innovation Park, 1015 Lausanne.
                [2 ]School of Life Sciences, EPFL, 1015 Lausanne.
                Author notes

                Conflict of interest: MV‐A and CC are employees of the Nestlé Institute of Health Sciences S.A.

                Please cite this article as: Miriam Valera-Alberni and Carles Canto ( 2018). Mitochondrial stress management: a dynamic journey. Cell Stress2 (10): 253-274. doi: 10.15698/cst2018.10.158

                Article
                Publisher ID: CST0178E132
                DOI: 10.15698/cst2018.10.158
                PMC ID: 6551641
                PubMed ID: 31225450
                SO-VID: ea2d0821-e9ce-412f-a509-29937d05a3eb
                Copyright © Copyright: © 2018 Valera-Alberni and Canto
                License:

                This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.

                History
                Date received : 08 June 2018
                Date revision received : 12 September 2018
                Date accepted : 19 September 2018
                Categories
                Subject: Review
                Subject: Mitochondria
                Subject: Mitochondrial Dynamics
                Subject: Oxidative Stress
                Subject: Unfolded Protein Response
                Subject: Mitophagy
                Subject: Mitochondrial Biogenesis

                Keywords: mitochondria,mitochondrial dynamics,oxidative stress,unfolded protein response,mitophagy,mitochondrial biogenesis
                Data availability:
                Keywords: mitochondria, mitochondrial dynamics, oxidative stress, unfolded protein response, mitophagy, mitochondrial biogenesis

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