Mitochondrial Physiology of Cellular Redox Regulations

. 2024 Aug 30 ; 73 (S1) : S217-S242. [epub] 20240422

Jazyk angličtina Země Česko Médium print-electronic

Typ dokumentu časopisecké články, přehledy

Perzistentní odkaz   https://www.medvik.cz/link/pmid38647168

Mitochondria (mt) represent the vital hub of the molecular physiology of the cell, being decision-makers in cell life/death and information signaling, including major redox regulations and redox signaling. Now we review recent advances in understanding mitochondrial redox homeostasis, including superoxide sources and H2O2 consumers, i.e., antioxidant mechanisms, as well as exemplar situations of physiological redox signaling, including the intramitochondrial one and mt-to-cytosol redox signals, which may be classified as acute and long-term signals. This review exemplifies the acute redox signals in hypoxic cell adaptation and upon insulin secretion in pancreatic beta-cells. We also show how metabolic changes under these circumstances are linked to mitochondrial cristae narrowing at higher intensity of ATP synthesis. Also, we will discuss major redox buffers, namely the peroxiredoxin system, which may also promote redox signaling. We will point out that pathological thresholds exist, specific for each cell type, above which the superoxide sources exceed regular antioxidant capacity and the concomitant harmful processes of oxidative stress subsequently initiate etiology of numerous diseases. The redox signaling may be impaired when sunk in such excessive pro-oxidative state.

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Brand MD. Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling. Free Radic Biol Med. 2016;100:14–31. doi: 10.1016/j.freeradbiomed.2016.04.001. PubMed DOI

Brand MD. Riding the tiger - physiological and pathological effects of superoxide and hydrogen peroxide generated in the mitochondrial matrix. Crit Rev Biochem Mol Biol. 2020;55:592–661. doi: 10.1080/10409238.2020.1828258. PubMed DOI

Fang J, Wong HS, Brand MD. Production of superoxide and hydrogen peroxide in the mitochondrial matrix is dominated by site IQ of complex I in diverse cell lines. Redox Biol. 2020;37:101722. doi: 10.1016/j.redox.2020.101722. PubMed DOI PMC

Quinlan CL, Perevoshchikova IV, Hey-Mogensen M, Orr AL, Brand MD. Sites of reactive oxygen species generation by mitochondria oxidizing different substrates. Redox Biol. 2013;1:304–312. doi: 10.1016/j.redox.2013.04.005. PubMed DOI PMC

Ježek P, Hlavatá L. Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism. Int J Biochem Cell Biol. 2005;37:2478–2503. doi: 10.1016/j.biocel.2005.05.013. PubMed DOI

Ježek P, Holendová B, Plecitá-Hlavatá L. Redox Signaling from Mitochondria: Signal Propagation and Its Targets. Biomolecules. 2020;10:93. doi: 10.3390/biom10010093. PubMed DOI PMC

Ježek P, Jabůrek M, Holendová B, Engstová H, Dlasková A. Mitochondrial Cristae Morphology Reflecting Metabolism, Superoxide Formation, Redox Homeostasis, and Pathology. Antioxid Redox Signal. 2023;39:635–683. doi: 10.1089/ars.2022.0173. PubMed DOI PMC

Kawano I, Bazila B, Ježek P, Dlasková A. Mitochondrial dynamics and cristae shape changes during metabolic re-programming. Antioxid Redox Signal. 2023;39:684–707. doi: 10.1089/ars.2023.0268. PubMed DOI

Ježek P. Pitfalls of Mitochondrial Redox Signaling Research. Antioxidants (Basel) 2023;12:1696. doi: 10.3390/antiox12091696. PubMed DOI PMC

Ohnishi ST, Shinzawa-Itoh K, Ohta K, Yoshikawa S, Ohnishi T. New insights into the superoxide generation sites in bovine heart NADH-ubiquinone oxidoreductase (Complex I): the significance of protein-associated ubiquinone and the dynamic shifting of generation sites between semiflavin and semiquinone radicals. Biochim Biophys Acta. 2010;1797:1901–1909. doi: 10.1016/j.bbabio.2010.05.012. PubMed DOI

Hirst J, Roessler MM. Energy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex I. Biochim Biophys Acta. 2016;1857:872–883. doi: 10.1016/j.bbabio.2015.12.009. PubMed DOI PMC

Chouchani ET, Pell VR, Gaude E, Aksentijević D, Sundier SY, Robb EL, Logan A, Nadtochiy SM, Ord ENJ, Smith AC, Eyassu F, Shirley R, Hu CH, Dare AJ, James AM, Rogatti S, Hartley RC, Eaton S, Costa ASH, Brookes PS, Davidson SM, Duchen MR, Saeb-Parsy K, Shattock MJ, Robinson AJ, Work LM, Frezza C, Krieg T, Murphy MP. Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS. Nature. 2014;515:431–435. doi: 10.1038/nature13909. PubMed DOI PMC

Robb EL, Hall AR, Prime TA, Eaton S, Szibor M, Viscomi C, James AM, Murphy MP. Control of mitochondrial superoxide production by reverse electron transport at complex I. J Biol Chem. 2018;293:9869–9879. doi: 10.1074/jbc.RA118.003647. PubMed DOI PMC

Dlasková A, Hlavatá L, Ježek P. Oxidative stress caused by blocking of mitochondrial complex I H(+) pumping as a link in aging/disease vicious cycle. Int J Biochem Cell Biol. 2008;40:1792–1805. doi: 10.1016/j.biocel.2008.01.012. PubMed DOI

Dlasková A, Hlavatá L, Ježek J, Ježek P. Mitochondrial Complex I superoxide production is attenuated by uncoupling. Int J Biochem Cell Biol. 2008;40:2098–2109. doi: 10.1016/j.biocel.2008.02.007. PubMed DOI

Ježek P, Žáčková M, Růžička M, Škobisová E, Jabůrek M. Mitochondrial uncoupling proteins--facts and fantasies. Physiol Res. 2004;53(Suppl 1):S199–S211. doi: 10.33549/physiolres.930000.53.S199. PubMed DOI

Ježek P, Olejár T, Smolková K, Ježek J, Dlasková A, Plecitá-Hlavatá L, Zelenka J, Špaček T, Engstová H, Pajuelo Reguera D, Jabůrek M. Antioxidant and regulatory role of mitochondrial uncoupling protein UCP2 in pancreatic beta-cells. Physiol Res. 2014;63(Suppl 1):S73–S91. doi: 10.33549/physiolres.932633. PubMed DOI

Ježek P, Holendová B, Jabůrek M, Dlasková A, Plecitá-Hlavatá L. Contribution of Mitochondria to Insulin Secretion by Various Secretagogues. Antioxid Redox Signal. 2022;36:920–952. doi: 10.1089/ars.2021.0113. PubMed DOI PMC

Brand MD, Affourtit C, Esteves TC, Green K, Lambert AJ, Miwa S, Pakay JL, Parker N. Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins. Free Radic Biol Med. 2004;37:755–767. doi: 10.1016/j.freeradbiomed.2004.05.034. PubMed DOI

Muller FL, Roberts AG, Bowman MK, Kramer DM. Architecture of the Qo site of the cytochrome bc1 complex probed by superoxide production. Biochemistry. 2003;42:6493–6499. doi: 10.1021/bi0342160. PubMed DOI

Muller FL, Liu Y, Van Remmen H. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J Biol Chem. 2004;279:49064–49073. doi: 10.1074/jbc.M407715200. PubMed DOI

Husen P, Nielsen C, Martino CF, Solov’yov IA. Molecular Oxygen Binding in the Mitochondrial Electron Transfer Flavoprotein. J Chem Inf Model. 2019;59:4868–4879. doi: 10.1021/acs.jcim.9b00702. PubMed DOI

Reichart G, Mayer J, Zehm C, Kirschstein T, Tokay T, Lange F, Baltrusch S, Tiedge M, Fuellen G, Ibrahim S, Köhling R. Mitochondrial complex IV mutation increases reactive oxygen species production and reduces lifespan in aged mice. Acta Physiol (Oxf) 2019;225:e13214. doi: 10.1111/apha.13214. PubMed DOI

Grivennikova VG, Kozlovsky VS, Vinogradov AD. Respiratory complex II: ROS production and the kinetics of ubiquinone reduction. Biochim Biophys Acta. 2017;1858:109–117. doi: 10.1016/j.bbabio.2016.10.008. PubMed DOI

St-Pierre J, Buckingham JA, Roebuck SJ, Brand MD. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J Biol Chem. 2002;277:44784–44790. doi: 10.1074/jbc.M207217200. PubMed DOI

Perevoshchikova IV, Quinlan CL, Orr AL, Gerencser AA, Brand MD. Sites of superoxide and hydrogen peroxide production during fatty acid oxidation in rat skeletal muscle mitochondria. Free Radic Biol Med. 2013;61:298–309. doi: 10.1016/j.freeradbiomed.2013.04.006. PubMed DOI PMC

Quinlan CL, Treberg JR, Perevoshchikova IV, Orr AL, Brand MD. Native rates of superoxide production from multiple sites in isolated mitochondria measured using endogenous reporters. Free Radic Biol Med. 2012;53:1807–1817. doi: 10.1016/j.freeradbiomed.2012.08.015. PubMed DOI PMC

Trewin AJ, Bahr LL, Almast A, Berry BJ, Wei AY, Foster TH, Wojtovich AP. Mitochondrial Reactive Oxygen Species Generated at the Complex-II Matrix or Intermembrane Space Microdomain Have Distinct Effects on Redox Signaling and Stress Sensitivity in Caenorhabditis elegans. Antioxid Redox Signal. 2019;31:594–607. doi: 10.1089/ars.2018.7681. PubMed DOI PMC

Siebels I, Dröse S. Q-site inhibitor induced ROS production of mitochondrial complex II is attenuated by TCA cycle dicarboxylates. Biochim Biophys Acta. 2013;1827:1156–1164. doi: 10.1016/j.bbabio.2013.06.005. PubMed DOI

Manhas N, Duong QV, Lee P, Richardson JD, Robertson JD, Moxley MA, Bazil JN. Computationally modeling mammalian succinate dehydrogenase kinetics identifies the origins and primary determinants of ROS production. J Biol Chem. 2020;295:15262–15279. doi: 10.1074/jbc.RA120.014483. PubMed DOI PMC

Quinlan CL, Goncalves RL, Hey-Mogensen M, Yadava N, Bunik VI, Brand MD. The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I. J Biol Chem. 2014;289:8312–8325. doi: 10.1074/jbc.M113.545301. PubMed DOI PMC

McDonald AE, Pichaud N, Darveau CA. “Alternative” fuels contributing to mitochondrial electron transport: Importance of non-classical pathways in the diversity of animal metabolism. Comp Biochem Physiol B Biochem Mol Biol. 2018;224:185–194. doi: 10.1016/j.cbpb.2017.11.006. PubMed DOI

Orr AL, Quinlan CL, Perevoshchikova IV, Brand MD. A refined analysis of superoxide production by mitochondrial sn-glycerol 3-phosphate dehydrogenase. J Biol Chem. 2012;287:42921–42935. doi: 10.1074/jbc.M112.397828. PubMed DOI PMC

Orr AL, Vargas L, Turk CN, Baaten JE, Matzen JT, Dardov VJ, Attle SJ, Li J, Quackenbush DC, Goncalves RL, Perevoshchikova IV, Petrassi HM, Meeusen SL, Ainscow EK, Brand MD. Suppressors of superoxide production from mitochondrial complex III. Nat Chem Biol. 2015;11:834–836. doi: 10.1038/nchembio.1910. PubMed DOI PMC

Boukalova S, Hubackova S, Milosevic M, Ezrova Z, Neuzil J, Rohlena J. Dihydroorotate dehydrogenase in oxidative phosphorylation and cancer. Biochim Biophys Acta. 2020;1866:165759. doi: 10.1016/j.bbadis.2020.165759. PubMed DOI

Valentine JS, Doucette PA, Zittin Potter S. Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu Rev Biochem. 2005;74:563–593. doi: 10.1146/annurev.biochem.72.121801.161647. PubMed DOI

Ozden O, Park SH, Kim HS, Jiang H, Coleman MC, Spitz DR, Gius D. Acetylation of MnSOD directs enzymatic activity responding to cellular nutrient status or oxidative stress. Aging. 2011;3:102–107. doi: 10.18632/aging.100291. PubMed DOI PMC

Park SH, Ozden O, Jiang H, Cha YI, Pennington JD, Aykin-Burns N, Spitz DR, Gius D, Kim HS. Sirt3, mitochondrial ROS, ageing, and carcinogenesis. Int J Mol Sci. 2011;12:6226–6239. doi: 10.3390/ijms12096226. PubMed DOI PMC

Salvatori I, Valle C, Ferri A, Carrì MT. SIRT3 and mitochondrial metabolism in neurodegenerative diseases. Neurochem Int. 2017;109:184–192. doi: 10.1016/j.neuint.2017.04.012. PubMed DOI

Tao R, Vassilopoulos A, Parisiadou L, Yan Y, Gius D. Regulation of MnSOD enzymatic activity by Sirt3 connects the mitochondrial acetylome signaling networks to aging and carcinogenesis. Antioxid Redox Signal. 2014;20:1646–1654. doi: 10.1089/ars.2013.5482. PubMed DOI PMC

Anamika Roy A, Trigun SK. Hippocampus mitochondrial MnSOD activation by a SIRT3 activator, honokiol, correlates with its deacetylation and upregulation of FoxO3a and PGC1α in a rat model of ammonia neurotoxicity. J Cell Biochem. 2023;124:606–618. doi: 10.1002/jcb.30393. PubMed DOI

Gao E, Sun X, Thorne RF, Zhang XD, Li J, Shao F, Ma J, Wu M. NIPSNAP1 directs dual mechanisms to restrain senescence in cancer cells. J Transl Med. 2023;21:401. doi: 10.1186/s12967-023-04232-1. PubMed DOI PMC

Liu X, Xie X, Li D, Liu Z, Zhang B, Zang Y, Yuan H, Shen C. Sirt3-dependent regulation of mitochondrial oxidative stress and apoptosis contributes to the dysfunction of pancreatic islets after severe burns. Free Radic Biol Med. 2023;198:59–67. doi: 10.1016/j.freeradbiomed.2023.01.027. PubMed DOI

Ma C, Sun Y, Pi C, Wang H, Sun H, Yu X, Shi Y, He X. Sirt3 Attenuates Oxidative Stress Damage and Rescues Cellular Senescence in Rat Bone Marrow Mesenchymal Stem Cells by Targeting Superoxide Dismutase 2. Front Cell Dev Biol. 2020;8:599376. doi: 10.3389/fcell.2020.599376. PubMed DOI PMC

Mohan MS, Aswani SS, Aparna NS, Boban PT, Sudhakaran PR, Saja K. Effect of acute cold exposure on cardiac mitochondrial function: role of sirtuins. Mol Cell Biochem. 2023;478:2257–2270. doi: 10.1007/s11010-022-04656-1. PubMed DOI

Dlasková A, Engstová H, Špaček T, Kahancová A, Pavluch V, Smolková K, Špačková J, Bartoš M, Hlavatá L, Ježek P. 3D super-resolution microscopy reflects mitochondrial cristae alternations and mtDNA nucleoid size and distribution. Biochim Biophys Acta. 2018;1859:829–844. doi: 10.1016/j.bbabio.2018.04.013. PubMed DOI

Ježek P, Plecitá-Hlavatá L. Mitochondrial reticulum network dynamics in relation to oxidative stress, redox regulation, and hypoxia. Int J Biochem Cell Biol. 2009;41:1790–1804. doi: 10.1016/j.biocel.2009.02.014. PubMed DOI

Plecitá-Hlavatá L, Ježek P. Integration of superoxide formation and cristae morphology for mitochondrial redox signaling. Int J Biochem Cell Biol. 2016;80:31–50. doi: 10.1016/j.biocel.2016.09.010. PubMed DOI

Dlasková A, Špaček T, Šantorová J, Plecitá-Hlavatá L, Berková Z, Saudek F, Lessard M, Bewersdorf J, Ježek P. 4Pi microscopy reveals an impaired three-dimensional mitochondrial network of pancreatic islet beta-cells, an experimental model of type-2 diabetes. Biochim Biophys Acta. 2010;1797:1327–1341. doi: 10.1016/j.bbabio.2010.02.003. PubMed DOI

Dlasková A, Engstová H, Plecitá-Hlavatá L, Lessard M, Alán L, Reguera DP, Jabůrek M, Ježek P. Distribution of mitochondrial DNA nucleoids inside the linear tubules vs. bulk parts of mitochondrial network as visualized by 4Pi microscopy. J Bioenerg Biomembr. 2015;47:255–263. doi: 10.1007/s10863-015-9610-3. PubMed DOI

Plecitá-Hlavatá L, Lessard M, Šantorová J, Bewersdorf J, Ježek P. Mitochondrial oxidative phosphorylation and energetic status are reflected by morphology of mitochondrial network in INS-1E and HEP-G2 cells viewed by 4Pi microscopy. Biochim Biophys Acta. 2008;1777:834–846. doi: 10.1016/j.bbabio.2008.04.002. PubMed DOI

Glancy B, Hartnell LM, Malide D, Yu ZX, Combs CA, Connelly PS, Subramaniam S, Balaban RS. Mitochondrial reticulum for cellular energy distribution in muscle. Nature. 2015;523:617–620. doi: 10.1038/nature14614. PubMed DOI PMC

Eisner V, Cupo RR, Gao E, Csordás G, Slovinsky WS, Paillard M, Cheng L, Ibetti J, Chen SR, Chuprun JK, Hoek JB, Koch WJ, Hajnóczky G. Mitochondrial fusion dynamics is robust in the heart and depends on calcium oscillations and contractile activity. Proc Natl Acad Sci U S A. 2017;114:E859–E868. doi: 10.1073/pnas.1617288114. PubMed DOI PMC

Twig G, Elorza A, Molina AJ, Mohamed H, Wikstrom JD, Walzer G, Stiles L, Haigh SE, Katz S, Las G, Alroy J, Wu M, Py BF, Yuan J, Deeney JT, Corkey BE, Shirihai OS. Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. EMBO J. 2008;27:433–446. doi: 10.1038/sj.emboj.7601963. PubMed DOI PMC

Picard M, Shirihai OS. Mitochondrial signal transduction. Cell Metab. 2022;34:1620–1653. doi: 10.1016/j.cmet.2022.10.008. PubMed DOI PMC

Kondadi AK, Anand R, Hänsch S, Urbach J, Zobel T, Wolf DM, Segawa M, Liesa M, Shirihai OS, Weidtkamp-Peters S, Reichert AS. Cristae undergo continuous cycles of membrane remodelling in a MICOS-dependent manner. EMBO Rep. 2020;21:e49776. doi: 10.15252/embr.201949776. PubMed DOI PMC

Bohnert M, Wenz LS, Zerbes RM, Horvath SE, Stroud DA, von der Malsburg K, Müller JM, Oeljeklaus S, Perschil I, Warscheid B, Chacinska A, Veenhuis M, van der Klei IJ, Daum G, Wiedemann N, Becker T, Pfanner N, van der Laan M. Role of mitochondrial inner membrane organizing system in protein biogenesis of the mitochondrial outer membrane. Mol Biol Cell. 2012;23:3948–3956. doi: 10.1091/mbc.e12-04-0295. PubMed DOI PMC

Pfanner N, van der Laan M, Amati P, Capaldi RA, Caudy AA, Chacinska A, Darshi M, Deckers M, Hoppins S, Icho T, Jakobs S, Ji J, Kozjak-Pavlovic V, Meisinger C, Odgren PR, Park SK, Rehling P, Reichert AS, Sheikh MS, Taylor SS, Tsuchida N, van der Bliek AM, van der Klei IJ, Weissman JS, Westermann B, Zha J, Neupert W, Nunnari J. Uniform nomenclature for the mitochondrial contact site and cristae organizing system. J Cell Biol. 2014;204:1083–1086. doi: 10.1083/jcb.201401006. PubMed DOI PMC

Zerbes RM, Bohnert M, Stroud DA, von der Malsburg K, Kram A, Oeljeklaus S, Warscheid B, Becker T, Wiedemann N, Veenhuis M, van der Klei IJ, Pfanner N, van der Laan M. Role of MINOS in mitochondrial membrane architecture: cristae morphology and outer membrane interactions differentially depend on mitofilin domains. J Mol Biol. 2012;422:183–191. doi: 10.1016/j.jmb.2012.05.004. PubMed DOI

Plecitá-Hlavatá L, Engstová H, Alán L, Špaček T, Dlasková A, Smolková K, Špačková J, Tauber J, Strádalová V, Malínský J, Lessard M, Bewersdorf J, Ježek P. Hypoxic HepG2 cell adaptation decreases ATP synthase dimers and ATP production in inflated cristae by mitofilin down-regulation concomitant to MICOS clustering. FASEB J. 2016;30:1941–1957. doi: 10.1096/fj.201500176. PubMed DOI

Davies KM, Strauss M, Daum B, Kief JH, Osiewacz HD, Rycovska A, Zickermann V, Kühlbrandt W. Macromolecular organization of ATP synthase and complex I in whole mitochondria. Proc Natl Acad Sci U S A. 2011;108:14121–14126. doi: 10.1073/pnas.1103621108. PubMed DOI PMC

Davies KM, Anselmi C, Wittig I, Faraldo-Gómez JD, Kühlbrandt W. Structure of the yeast F1Fo-ATP synthase dimer and its role in shaping the mitochondrial cristae. Proc Natl Acad Sci U S A. 2012;109:13602–13607. doi: 10.1073/pnas.1204593109. PubMed DOI PMC

Dlasková A, Špaček T, Engstová H, Špačková J, Schröfel A, Holendová B, Smolková K, Plecitá-Hlavatá L, Ježek P. Mitochondrial cristae narrowing upon higher 2-oxoglutarate load. Biochim Biophys Acta. 2019;1860:659–678. doi: 10.1016/j.bbabio.2019.06.015. PubMed DOI

Dudkina NV, Oostergetel GT, Lewejohann D, Braun HP, Boekema EJ. Row-like organization of ATP synthase in intact mitochondria determined by cryo-electron tomography. Biochim Biophys Acta. 2010;1797:272–277. doi: 10.1016/j.bbabio.2009.11.004. PubMed DOI

Gu J, Zhang L, Zong S, Guo R, Liu T, Yi J, Wang P, Zhuo W, Yang M. Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1. Science. 2019;364:1068–1075. doi: 10.1126/science.aaw4852. PubMed DOI

Guo H, Bueler SA, Rubinstein JL. Atomic model for the dimeric FO region of mitochondrial ATP synthase. Science. 2017;358:936–940. doi: 10.1126/science.aao4815. PubMed DOI PMC

Nesterov S, Chesnokov Y, Kamyshinsky R, Panteleeva A, Lyamzaev K, Vasilov R, Yaguzhinsky L. Ordered Clusters of the Complete Oxidative Phosphorylation System in Cardiac Mitochondria. Int J Mol Sci. 2021;22:1462. doi: 10.3390/ijms22031462. PubMed DOI PMC

Blum TB, Hahn A, Meier T, Davies KM, Kühlbrandt W. Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows. Proc Natl Acad Sci U S A. 2019;116:4250–4255. doi: 10.1073/pnas.1816556116. PubMed DOI PMC

Daum B, Walter A, Horst A, Osiewacz HD, Kühlbrandt W. Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria. Proc Natl Acad Sci U S A. 2013;110:15301–15306. doi: 10.1073/pnas.1305462110. PubMed DOI PMC

Spikes TE, Montgomery MG, Walker JE. Structure of the dimeric ATP synthase from bovine mitochondria. Proc Natl Acad Sci U S A. 2020;117:23519–23526. doi: 10.1073/pnas.2013998117. PubMed DOI PMC

Rampelt H, Bohnert M, Zerbes RM, Horvath SE, Warscheid B, Pfanner N, van der Laan M. Mic10, a Core Subunit of the Mitochondrial Contact Site and Cristae Organizing System, Interacts with the Dimeric F1Fo-ATP Synthase. J Mol Biol. 2017;429:1162–1170. doi: 10.1016/j.jmb.2017.03.006. PubMed DOI

Eydt K, Davies KM, Behrendt C, Wittig I, Reichert AS. Cristae architecture is determined by an interplay of the MICOS complex and the F1FO ATP synthase via Mic27 and Mic10. Microb Cell. 2017;4:259–272. doi: 10.15698/mic2017.08.585. PubMed DOI PMC

Lenaz G, Tioli G, Falasca AI, Genova ML. Complex I function in mitochondrial supercomplexes. Biochim Biophys Acta. 2016;1857:991–1000. doi: 10.1016/j.bbabio.2016.01.013. PubMed DOI

Letts JA, Fiedorczuk K, Sazanov LA. The architecture of respiratory supercomplexes. Nature. 2016;537:644–648. doi: 10.1038/nature19774. PubMed DOI

Lobo-Jarne T, Ugalde C. Respiratory chain supercomplexes: Structures, function and biogenesis. Semin Cell Dev Biol. 2018;76:179–190. doi: 10.1016/j.semcdb.2017.07.021. PubMed DOI PMC

Giacomello M, Pyakurel A, Glytsou C, Scorrano L. The cell biology of mitochondrial membrane dynamics. Nat Rev Mol Cell Biol. 2020;21:204–224. doi: 10.1038/s41580-020-0210-7. PubMed DOI

Pernas L, Scorrano L. Mito-Morphosis: Mitochondrial Fusion, Fission, and Cristae Remodeling as Key Mediators of Cellular Function. Annu Rev Physiol. 2016;78:505–531. doi: 10.1146/annurev-physiol-021115-105011. PubMed DOI

Faelber K, Dietrich L, Noel JK, Wollweber F, Pfitzner AK, Mühleip A, Sánchez R, Kudryashev M, Chiaruttini N, Lilie H, Schlegel J, Rosenbaum E, Hessenberger M, Matthaeus C, Kunz S, von der Malsburg A, Noé F, Roux A, van der Laan M, Kühlbrandt W, Daumke O. Structure and assembly of the mitochondrial membrane remodelling GTPase Mgm1. Nature. 2019;571:429–433. doi: 10.1038/s41586-019-1372-3. PubMed DOI PMC

Tatsuta T, Langer T. Prohibitins. Curr Biol. 2017;27:R629–R631. doi: 10.1016/j.cub.2017.04.030. PubMed DOI

Barbot M, Jans DC, Schulz C, Denkert N, Kroppen B, Hoppert M, Jakobs S, Meinecke M. Mic10 oligomerizes to bend mitochondrial inner membranes at cristae junctions. Cell Metab. 2015;21:756–763. doi: 10.1016/j.cmet.2015.04.006. PubMed DOI

Bohnert M, Zerbes RM, Davies KM, Mühleip AW, Rampelt H, Horvath SE, Boenke T, Kram A, Perschil I, Veenhuis M, Kühlbrandt W, van der Klei IJ, Pfanner N, van der Laan M. Central role of Mic10 in the mitochondrial contact site and cristae organizing system. Cell Metab. 2015;21:747–755. doi: 10.1016/j.cmet.2015.04.007. PubMed DOI

Wang L, Yan Z, Vihinen H, Eriksson O, Wang W, Soliymani R, Lu Y, Xue Y, Jokitalo E, Li J, Zhao H. FAM92A1 is a BAR domain protein required for mitochondrial ultrastructure and function. J Cell Biol. 2019;218:97–111. doi: 10.1083/jcb.201806191. PubMed DOI PMC

Frezza C, Cipolat S, Martins de Brito O, Micaroni M, Beznoussenko GV, Rudka T, Bartoli D, Polishuck RS, Danial NN, De Strooper B, Scorrano L. OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell. 2006;126:177–189. doi: 10.1016/j.cell.2006.06.025. PubMed DOI

Deponte M. Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes. Biochim Biophys Acta. 2013;1830:3217–3266. doi: 10.1016/j.bbagen.2012.09.018. PubMed DOI

Sies H, Jones DP. Reactive oxygen species (ROS) as pleiotropic physiological signalling agents. Nat Rev Mol Cell Biol. 2020;21:363–383. doi: 10.1038/s41580-020-0230-3. PubMed DOI

Merrins MJ, Corkey BE, Kibbey RG, Prentki M. Metabolic cycles and signals for insulin secretion. Cell Metab. 2022;34:947–968. doi: 10.1016/j.cmet.2022.06.003. PubMed DOI PMC

Rorsman P, Ashcroft FM. Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men. Physiol Rev. 2018;98:117–214. doi: 10.1152/physrev.00008.2017. PubMed DOI PMC

Ježek P, Holendová B, Jabůrek M, Tauber J, Dlasková A, Plecitá-Hlavatá L. The Pancreatic β-Cell: The Perfect Redox System. Antioxidants. 2021;10:197. doi: 10.3390/antiox10020197. PubMed DOI PMC

Brigelius-Flohe R, Maiorino M. Glutathione peroxidases. Biochim Biophys Acta. 2013;1830:3289–3303. doi: 10.1016/j.bbagen.2012.11.020. PubMed DOI

Ighodaro OM, Akinloye OA. First line defence antioxidants-superoxide dismutase (SOD), catalase (CAT) and gluta-thione peroxidase (GPX): Their fundamental role in the entire antioxidant defence grid. Alex J Med. 2018;54:287–293. doi: 10.1016/j.ajme.2017.09.001. DOI

Herbette S, Roeckel-Drevet P, Drevet JR. Seleno-independent glutathione peroxidases. More than simple antioxidant scavengers. FEBS J. 2007;274:2163–2180. doi: 10.1111/j.1742-4658.2007.05774.x. PubMed DOI

Bolduc J, Koruza K, Luo T, Malo Pueyo J, Vo TN, Ezeriņa D, Messens J. Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities. Redox Biol. 2021;42:101959. doi: 10.1016/j.redox.2021.101959. PubMed DOI PMC

Liu Y, Wang P, Hu W, Chen D. New insights into the roles of peroxiredoxins in cancer. Biomed Pharmacother. 2023;164:114896. doi: 10.1016/j.biopha.2023.114896. PubMed DOI

Rhee SG. Overview on Peroxiredoxin. Mol Cells. 2016;39:1–5. doi: 10.14348/molcells.2016.2368. PubMed DOI PMC

Rhee SG, Kang SW, Chang TS, Jeong W, Kim K. Peroxiredoxin, a novel family of peroxidases. IUBMB Life. 2001;52:35–41. doi: 10.1080/15216540252774748. PubMed DOI

Rhee SG, Woo HA. Multiple functions of 2-Cys peroxiredoxins, I and II, and their regulations via post-translational modifications. Free Radic Biol Med. 2020;152:107–115. doi: 10.1016/j.freeradbiomed.2020.02.028. PubMed DOI

Thapa P, Jiang H, Ding N, Hao Y, Alshahrani A, Wei Q. The Role of Peroxiredoxins in Cancer Development. Biology (Basel) 2023;12:666. doi: 10.3390/biology12050666. PubMed DOI PMC

Villar SF, Ferrer-Sueta G, Denicola A. The multifaceted nature of peroxiredoxins in chemical biology. Curr Opin Chem Biol. 2023;76:102355. doi: 10.1016/j.cbpa.2023.102355. PubMed DOI

Knoops B, Goemaere J, Van der Eecken V, Declercq JP. Peroxiredoxin 5: structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin. Antioxid Redox Signal. 2011;15:817–829. doi: 10.1089/ars.2010.3584. PubMed DOI

Sabharwal SS, Waypa GB, Marks JD, Schumacker PT. Peroxiredoxin-5 targeted to the mitochondrial intermembrane space attenuates hypoxia-induced reactive oxygen species signalling. Biochem J. 2013;456:337–346. doi: 10.1042/BJ20130740. PubMed DOI PMC

Sabharwal SS, Dudley VJ, Landwerlin C, Schumacker PT. H2O2 transit through the mitochondrial intermembrane space promotes tumor cell growth in vitro and in vivo. J Biol Chem. 2023;299:104624. doi: 10.1016/j.jbc.2023.104624. PubMed DOI PMC

López-Grueso MJ, Lagal DJ, García-Jiménez ÁF, Tarradas RM, Carmona-Hidalgo B, Peinado J, Requejo-Aguilar R, Bárcena JA, Padilla CA. Knockout of PRDX6 induces mitochondrial dysfunction and cell cycle arrest at G2/M in HepG2 hepatocarcinoma cells. Redox Biol. 2020;37:101737. doi: 10.1016/j.redox.2020.101737. PubMed DOI PMC

Ma S, Zhang X, Zheng L, Li Z, Zhao X, Lai W, Shen H, Lv J, Yang G, Wang Q, Ji J. Peroxiredoxin 6 Is a Crucial Factor in the Initial Step of Mitochondrial Clearance and Is Upstream of the PINK1-Parkin Pathway. Antioxid Redox Signal. 2016;24:486–501. doi: 10.1089/ars.2015.6336. PubMed DOI

Pacifici F, Della-Morte D, Capuani B, Coppola A, Scioli MG, Donadel G, Andreadi A, Ciccosanti F, Fimia GM, Bellia A, Orlandi A, Lauro D. Peroxiredoxin 6 Modulates Insulin Secretion and Beta Cell Death via a Mitochondrial Dynamic Network. Front Endocrinol. 2022;13:842575. doi: 10.3389/fendo.2022.842575. PubMed DOI PMC

Bachnoff N, Trus M, Atlas D. Alleviation of oxidative stress by potent and selective thioredoxin-mimetic peptides. Free Radic Biol Med. 2011;50:1355–1367. doi: 10.1016/j.freeradbiomed.2011.02.026. PubMed DOI

Jeong SJ, Park JG, Oh GT. Peroxiredoxins as Potential Targets for Cardiovascular Disease. Antioxidants. 2021;10:1244. doi: 10.3390/antiox10081244. PubMed DOI PMC

Szeliga M. Peroxiredoxins in Neurodegenerative Diseases. Antioxidants. 2020;9:1203. doi: 10.3390/antiox9121203. PubMed DOI PMC

Stancill JS, Corbett JA. The Role of Thioredoxin/Peroxiredoxin in the β-Cell Defense Against Oxidative Damage. Front Endocrinol. 2021;12:718235. doi: 10.3389/fendo.2021.718235. PubMed DOI PMC

Rhee SG, Kil IS. Mitochondrial H2O2 signaling is controlled by the concerted action of peroxiredoxin III and sulfiredoxin: Linking mitochondrial function to circadian rhythm. Free Radic Biol Med. 2016;100:73–80. doi: 10.1016/j.freeradbiomed.2016.10.011. PubMed DOI

Mishra M, Jiang H, Wu L, Chawsheen HA, Wei Q. The sulfiredoxin-peroxiredoxin (Srx-Prx) axis in cell signal transduction and cancer development. Cancer Lett. 2015;366:150–159. doi: 10.1016/j.canlet.2015.07.002. PubMed DOI PMC

Reczek CR, Chandel NS. ROS-dependent signal transduction. Curr Opin Cell Biol. 2015;33:8–13. doi: 10.1016/j.ceb.2014.09.010. PubMed DOI PMC

Woo HA, Yim SH, Shin DH, Kang D, Yu DY, Rhee SG. Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. Cell. 2010;140:517–528. doi: 10.1016/j.cell.2010.01.009. PubMed DOI

Heo S, Kim S, Kang D. The Role of Hydrogen Peroxide and Peroxiredoxins throughout the Cell Cycle. Antioxidants. 2020;9:280. doi: 10.3390/antiox9040280. PubMed DOI PMC

Jarvis RM, Hughes SM, Ledgerwood EC. Peroxiredoxin 1 functions as a signal peroxidase to receive, transduce, and transmit peroxide signals in mammalian cells. Free Radic Biol Med. 2012;53:1522–1530. doi: 10.1016/j.freeradbiomed.2012.08.001. PubMed DOI

Rhee SG, Woo HA, Kang D. The Role of Peroxiredoxins in the Transduction of H2O2 Signals. Antioxid Redox Signal. 2018;28:537–557. doi: 10.1089/ars.2017.7167. PubMed DOI

Rhee SG. A catalytic career: Studies spanning glutamine synthetase, phospholipase C, peroxiredoxin, and the intracellular messenger role of hydrogen peroxide. J Biol Chem. 2019;294:5169–5180. doi: 10.1074/jbc.X119.007975. PubMed DOI PMC

Sobotta MC, Liou W, Stocker S, Talwar D, Oehler M, Ruppert T, Scharf AN, Dick TP. Peroxiredoxin-2 and STAT3 form a redox relay for H2O2 signaling. Nat Chem Biol. 2015;11:64–70. doi: 10.1038/nchembio.1695. PubMed DOI

Stocker S, Van Laer K, Mijuskovic A, Dick TP. The Conundrum of Hydrogen Peroxide Signaling and the Emerging Role of Peroxiredoxins as Redox Relay Hubs. Antioxid Redox Signal. 2018;28:558–573. doi: 10.1089/ars.2017.7162. PubMed DOI

Ježek P, Holendová B, Garlid KD, Jabůrek M. Mitochondrial Uncoupling Proteins: Subtle Regulators of Cellular Redox Signaling. Antioxid Redox Signal. 2018;29:667–714. doi: 10.1089/ars.2017.7225. PubMed DOI PMC

Jabůrek M, Průchová P, Holendová B, Galkin A, Ježek P. Antioxidant Synergy of Mitochondrial Phospholipase PNPLA8/iPLA2γ with Fatty Acid-Conducting SLC25 Gene Family Transporters. Antioxidants. 2021;10:678. doi: 10.3390/antiox10050678. PubMed DOI PMC

Průchová P, Gotvaldová K, Smolková K, Alán L, Holendová B, Tauber J, Galkin A, Ježek P, Jabůrek M. Antioxidant Role and Cardiolipin Remodeling by Redox-Activated Mitochondrial Ca2+-Independent Phospholipase A2γ in the Brain. Antioxidants. 2022;11:198. doi: 10.3390/antiox11020198. PubMed DOI PMC

Fedorenko A, Lishko PV, Kirichok Y. Mechanism of fatty-acid-dependent UCP1 uncoupling in brown fat mitochondria. Cell. 2012;151:400–413. doi: 10.1016/j.cell.2012.09.010. PubMed DOI PMC

Ježek J, Dlasková A, Zelenka J, Jabůrek M, Ježek P. H2O2-Activated Mitochondrial Phospholipase iPLA2γ Prevents Lipotoxic Oxidative Stress in Synergy with UCP2, Amplifies Signaling via G-Protein-Coupled Receptor GPR40, and Regulates Insulin Secretion in Pancreatic β-Cells. Antioxid Redox Signal. 2015;23:958–972. doi: 10.1089/ars.2014.6195. PubMed DOI PMC

Korshunov SS, Skulachev VP, Starkov AA. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 1997;416:15–18. doi: 10.1016/S0014-5793(97)01159-9. PubMed DOI

Arsenijevic D, Onuma H, Pecqueur C, Raimbault S, Manning BS, Miroux B, Couplan E, Alves-Guerra MC, Goubern M, Surwit R, Bouillaud F, Richard D, Collins S, Ricquier D. Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production. Nat Genet. 2000;26:435–439. doi: 10.1038/82565. PubMed DOI

Nègre-Salvayre A, Hirtz C, Carrera G, Cazenave R, Troly M, Salvayre R, Pénicaud L, Casteilla L. A role for uncoupling protein-2 as a regulator of mitochondrial hydrogen peroxide generation. FASEB J. 1997;11:809–815. doi: 10.1096/fasebj.11.10.9271366. PubMed DOI

Duval C, Nègre-Salvayre A, Dogilo A, Salvayre R, Pénicaud L, Casteilla L. Increased reactive oxygen species production with antisense oligonucleotides directed against uncoupling protein 2 in murine endothelial cells. Biochem Cell Biol. 2002;80:757–764. doi: 10.1139/o02-158. PubMed DOI

Blanc J, Alves-Guerra MC, Esposito B, Rousset S, Gourdy P, Ricquier D, Tedgui A, Miroux B, Mallat Z. Protective role of uncoupling protein 2 in atherosclerosis. Circulation. 2003;107:388–390. doi: 10.1161/01.CIR.0000051722.66074.60. PubMed DOI

Ježek J, Jabůrek M, Zelenka J, Ježek P. Mitochondrial phospholipase A2 activated by reactive oxygen species in heart mitochondria induces mild uncoupling. Physiol Res. 2010;59:737–747. doi: 10.33549/physiolres.931905. PubMed DOI

Jabůrek M, Ježek J, Zelenka J, Ježek P. Antioxidant activity by a synergy of redox-sensitive mitochondrial phospholipase A2 and uncoupling protein-2 in lung and spleen. Int J Biochem Cell Biol. 2013;45:816–825. doi: 10.1016/j.biocel.2013.01.010. PubMed DOI

Chandel N. Evolution of mitochondria as signaling organelles. Cell Metab. 2015;22:204–206. doi: 10.1016/j.cmet.2015.05.013. PubMed DOI

Nunnari J, Suomalainen A. Mitochondria: in sickness and in health. Cell. 2012;148:1145–1159. doi: 10.1016/j.cell.2012.02.035. PubMed DOI PMC

Durieux J, Wolff S, Dillin A. The cell-non-autonomous nature of electron transport chain-mediated longevity. Cell. 2011;144:79–91. doi: 10.1016/j.cell.2010.12.016. PubMed DOI PMC

Forsstrom S, Jackson CB, Carroll CJ, Kuronen M, Pirinen E, Pradhan S, Marmyleva A, Auranen M, Kleine IM, Khan NA, Roivainen A, Marjamäki P, Liljenbäck H, Wang L, Battersby BJ, Richter U, Velagapudi V, Nikkanen J, Euro L, Suomalainen A. Fibroblast growth factor 21 drives dynamics of local and systemic stress responses in mitochondrial myopathy with mtDNA deletions. Cell Metab. 2019;30:1040–1054.e7. doi: 10.1016/j.cmet.2019.08.019. PubMed DOI

Tyynismaa H, Carroll CJ, Raimundo N, Ahola-Erkkila S, Wenz T, Ruhanen H, Guse K, Hemminki A, Peltola-Mjosund KE, Tulkki V, Oresic M, Moraes CT, Pietiläinen K, Hovatta I, Suomalainen A. Mitochondrial myopathy induces a starvation-like response. Hum Mol Genet. 2010;19:3948–3958. doi: 10.1093/hmg/ddq310. PubMed DOI

Cardamone MD, Tanasa B, Cederquist CT, Huang J, Mahdaviani K, Li W, Rosenfeld MG, Liesa M, Perissi V. Mitochondrial retrograde signaling in mammals is mediated by the transcriptional cofactor GPS2 via direct mitochondria-to-nucleus translocation. Mol Cell. 2018;69:757–772.e7. doi: 10.1016/j.molcel.2018.01.037. PubMed DOI PMC

Kim KH, Son JM, Benayoun BA, Lee C. The mitochondrial-encoded peptide MOTS-c translocates to the nucleus to regulate nuclear gene expression in response to metabolic stress. Cell Metab. 2018;28:516–524.e7. doi: 10.1016/j.cmet.2018.06.008. PubMed DOI PMC

Nargund AM, Pellegrino MW, Fiorese CJ, Baker BM, Haynes CM. Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science. 2012;337:587–590. doi: 10.1126/science.1223560. PubMed DOI PMC

West AP, Khoury-Hanold W, Staron M, Tal MC, Pineda CM, Lang SM, Bestwick M, Duguay BA, Raimundo N, MacDuff DA, Kaech SM, Smiley JR, Means RE, Iwasaki A, Shadel GS. Mitochondrial DNA stress primes the antiviral innate immune response. Nature. 2015;520:553–557. doi: 10.1038/nature14156. PubMed DOI PMC

Lozoya OA, Martinez-Reyes I, Wang T, Grenet D, Bushel P, Li J, Chandel N, Woychik RP, Santos JH. Mitochondrial nicotinamide adenine dinucleotide reduced (NADH) oxidation links the tricarboxylic acid (TCA) cycle with methionine metabolism and nuclear DNA methylation. PLoS Biol. 2018;16:e2005707. doi: 10.1371/journal.pbio.2005707. PubMed DOI PMC

Picard M, Zhang J, Hancock S, Derbeneva O, Golhar R, Golik P, O’Hearn S, Levy S, Potluri P, Lvova M, Davila A, Lin CS, Perin JC, Rappaport EF, Hakonarson H, Trounce IA, Procaccio V, Wallace DC. Progressive increase in mtDNA 3243A>G heteroplasmy causes abrupt transcriptional reprogramming. Proc Natl Acad Sci U S A. 2014;111:E4033–E4042. doi: 10.1073/pnas.1414028111. PubMed DOI PMC

Smiraglia D, Kulawiec M, Bistulfi GL, Ghoshal S, Singh KK. A novel role for mitochondria in regulating epigenetic modifications in the nucleus. Cancer Biol Ther. 2008;7:1182–1190. doi: 10.4161/cbt.7.8.6215. PubMed DOI PMC

Tian Y, Garcia G, Bian Q, Steffen K, Joe L, Wolff S, Meyer B, Dillin A. Mitochondrial stress induces chromatin reorganization to promote longevity and UPR(mt) Cell. 2016;165:1197–1208. doi: 10.1016/j.cell.2016.04.011. PubMed DOI PMC

Vizioli MG, Liu T, Miller KN, Robertson NA, Gilroy K, Lagnado AB, Perez-Garcia A, Kiourtis C, Dasgupta N, Lei X, Kruger PJ, Nixon C, Clark W, Jurk D, Bird TG, Passos JF, Berger SL, Dou Z, Adams PD. Mitochondria-to-nucleus retrograde signaling drives formation of cytoplasmic chromatin and inflammation in senescence. Genes Dev. 2020;34:428–445. doi: 10.1101/gad.331272.119. PubMed DOI PMC

Qian W, Kumar N, Roginskaya V, Fouquerel E, Opresko PL, Shiva S, Watkins SC, Kolodieznyi D, Bruchez MP, Van Houten B. Chemoptogenetic damage to mitochondria causes rapid telomere dysfunction. Proc Natl Acad Sci U S A. 2019;116:18435–18444. doi: 10.1073/pnas.1910574116. PubMed DOI PMC

Lozoya OA, Xu F, Grenet D, Wang T, Grimm SA, Godfrey V, Waidyanatha S, Woychik RP, Santos JH. Single nucleotide resolution analysis reveals pervasive, long-lasting DNA methylation changes by developmental exposure to a mitochondrial toxicant. Cell Rep. 2020;32:108131. doi: 10.1016/j.celrep.2020.108131. PubMed DOI PMC

Correia-Melo C, Marques FD, Anderson R, Hewitt G, Hewitt R, Cole J, Carroll BM, Miwa S, Birch J, Merz A, Rushton MD, Charles M, Jurk D, Tait SW, Czapiewski R, Greaves L, Nelson G, Bohlooly-Y M, Rodriguez-Cuenca S, Vidal-Puig A, Mann D, Saretzki G, Quarato G, Green DR, Adams PD, von Zglinicki T, Korolchuk VI, Passos JF. Mitochondria are required for pro-ageing features of the senescent phenotype. EMBO J. 2016;35:724–742. doi: 10.15252/embj.201592862. PubMed DOI PMC

Nelson G, Kucheryavenko O, Wordsworth J, von Zglinicki T. The senescent bystander effect is caused by ROS-activated NF-kB signalling. Mech Ageing Dev. 2018;170:30–36. doi: 10.1016/j.mad.2017.08.005. PubMed DOI PMC

da Silva PFL, Ogrodnik M, Kucheryavenko O, Glibert J, Miwa S, Cameron K, Ishaq A, Saretzki G, Nagaraja-Grellscheid S, Nelson G, von Zglinicki T. The bystander effect contributes to the accumulation of senescent cells in vivo. Aging Cell. 2019;18:e12848. doi: 10.1111/acel.12848. PubMed DOI PMC

Ježek P, Jabůrek M. Plecitá-Hlavatá L. Contribution of oxidative stress and impaired biogenesis of pancreatic beta-cells to type 2 diabetes. Antioxid Redox Signal. 2019;31:722–751. doi: 10.1089/ars.2018.7656. PubMed DOI PMC

Balaban RS, Nemoto S, Finkel T. Mitochondria, oxidants, and aging. Cell. 2005;120:483–495. doi: 10.1016/j.cell.2005.02.001. PubMed DOI

Shadel G, Horvath T. Mitochondrial ROS signaling in organismal homeostasis. Cell. 2015;163:560–569. doi: 10.1016/j.cell.2015.10.001. PubMed DOI PMC

Al-Mehdi AB, Pastukh VM, Swiger BM, Reed DJ, Patel MR, Bardwell GC, Pastukh VV, Alexeyev MF, Gillespie MN. Perinuclear mitochondrial clustering creates an oxidant-rich nuclear domain required for hypoxia-induced transcription. Sci Signal. 2012;5:ra47. doi: 10.1126/scisignal.2002712. PubMed DOI PMC

Desai R, East DA, Hardy L, Faccenda D, Rigon M, Crosby J, Alvarez MS, Singh A, Mainenti M, Hussey LK, Bentham R, Szabadkai G, Zappulli V, Dhoot GK, Romano LE, Xia D, Coppens I, Hamacher-Brady A, Chapple JP, Abeti R, Fleck RA, Vizcay-Barrena G, Smith K, Campanella M. Mitochondria form contact sites with the nucleus to couple prosurvival retrograde response. Sci Adv. 2020;6:eabc9955. doi: 10.1126/sciadv.abc9955. PubMed DOI PMC

Chouchani ET, Kazak L, Jedrychowski MP, Lu GZ, Erickson BK, Szpyt J, Pierce KA, Laznik-Bogoslavski D, Vetrivelan R, Clish CB, Robinson AJ, Gygi SP, Spiegelman BM. Mitochondrial ROS regulate thermogenic energy expenditure and sulfenylation of UCP1. Nature. 2016;532:112–116. doi: 10.1038/nature17399. PubMed DOI PMC

Ježek P, Jabůrek M, Porter RK. Uncoupling mechanism and redox regulation of mitochondrial uncoupling protein 1 (UCP1) Biochim Biophys Acta. 2019;1860:259–269. doi: 10.1016/j.bbabio.2018.11.007. PubMed DOI

Fu ZX, Tan X, Fang H, Lau PM, Wang X, Cheng H, Bi GQ. Dendritic mitoflash as a putative signal for stabilizing long-term synaptic plasticity. Nat Commun. 2017;8:31. doi: 10.1038/s41467-017-00043-3. PubMed DOI PMC

Horn A, Raavicharla S, Shah S, Cox D, Jaiswal JK. Mitochondrial fragmentation enables localized signaling required for cell repair. J Cell Biol. 2020;219:e201909154. doi: 10.1083/jcb.201909154. PubMed DOI PMC

Fuhrmann DC, Brune B. Mitochondrial composition and function under the control of hypoxia. Redox Biol. 2017;12:208–215. doi: 10.1016/j.redox.2017.02.012. PubMed DOI PMC

Pan Y, Mansfield KD, Bertozzi CC, Rudenko V, Chan DA, Giaccia AJ, Simon MC. Multiple factors affecting cellular redox status and energy metabolism modulate hypoxia-inducible factor prolyl hydroxylase activity in vivo and in vitro. Mol Cell Biol. 2007;27:912–925. doi: 10.1128/MCB.01223-06. PubMed DOI PMC

Appelhoff RJ, Tian YM, Raval RR, Turley H, Harris AL, Pugh CW, Ratcliffe PJ, Gleadle JM. Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. J Biol Chem. 2004;279:38458–38465. doi: 10.1074/jbc.M406026200. PubMed DOI

Lu H, Dalgard CL, Mohyeldin A, McFate T, Tait AS, Verma A. Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1. J Biol Chem. 2005;280:41928–41939. doi: 10.1074/jbc.M508718200. PubMed DOI

Samanta D, Semenza GL. Maintenance of redox homeostasis by hypoxia-inducible factors. Redox Biol. 2017;13:331–335. doi: 10.1016/j.redox.2017.05.022. PubMed DOI PMC

Ivan M, Kondo K, Yang H, Kim W, Valiando J, Ohh M, Salic A, Asara JM, Lane WS, Kaelin WG., Jr HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: Implications for O2 sensing. Science. 2001;292:464–468. doi: 10.1126/science.1059817. PubMed DOI

Jaakkola P, Mole DR, Tian YM, Wilson MI, Gielbert J, Gaskell SJ, von Kriegsheim A, Hebestreit HF, Mukherji M, Schofield CJ, Maxwell PH, Pugh CW, Ratcliffe PJ. Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science. 2001;292:468–472. doi: 10.1126/science.1059796. PubMed DOI

Semenza GL. Regulation of Erythropoiesis by the Hypoxia-Inducible Factor Pathway: Effects of Genetic and Pharmacological Perturbations. Annu Rev Med. 2023;74:307–319. doi: 10.1146/annurev-med-042921-102602. PubMed DOI

Brocato J, Chervona Y, Costa M. Molecular responses to hypoxia-inducible factor 1alpha and beyond. Mol Pharmacol. 2014;85:651–657. doi: 10.1124/mol.113.089623. PubMed DOI PMC

Schodel J, Oikonomopoulos S, Ragoussis J, Pugh CW, Ratcliffe PJ, Mole DR. High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq. Blood. 2011;117:e207–e217. doi: 10.1182/blood-2010-10-314427. PubMed DOI PMC

Semenza GL. Hypoxia-inducible factors in physiology and medicine. Cell. 2012;148:399–408. doi: 10.1016/j.cell.2012.01.021. PubMed DOI PMC

Semenza GL. The Genomics and Genetics of Oxygen Homeostasis. Annu Rev Genomics Hum Genet. 2020;21:183–204. doi: 10.1146/annurev-genom-111119-073356. PubMed DOI

Wicks EE, Semenza GL. Hypoxia-inducible factors: cancer progression and clinical translation. J Clin Invest. 2022;132:e159839. doi: 10.1172/JCI159839. PubMed DOI PMC

Zepeda AB, Pessoa A, Jr, Castillo RL, Figueroa CA, Pulgar VM, Farias JG. Cellular and molecular mechanisms in the hypoxic tissue: Role of HIF-1 and ROS. Cell Biochem Funct. 2013;31:451–459. doi: 10.1002/cbf.2985. PubMed DOI

Gerald D, Berra E, Frapart YM, Chan DA, Giaccia AJ, Mansuy D, Pouyssegur J, Yaniv M, Mechta-Grigoriou F. JunD reduces tumor angiogenesis by protecting cells from oxidative stress. Cell. 2004;118:781–794. doi: 10.1016/j.cell.2004.08.025. PubMed DOI

Briggs KJ, Koivunen P, Cao S, Backus KM, Olenchock BA, Patel H, Zhang Q, Signoretti S, Gerfen GJ, Richardson AL, Witkiewicz AK, Cravatt BF, Clardy J, Kaelin WG., Jr Paracrine Induction of HIF by Glutamate in Breast Cancer: EglN1 Senses Cysteine. Cell. 2016;166:126–139. doi: 10.1016/j.cell.2016.05.042. PubMed DOI PMC

Chowdhury R, Flashman E, Mecinovic J, Kramer HB, Kessler BM, Frapart YM, Boucher JL, Clifton IJ, McDonough MA, Schofield CJ. Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1) J Mol Biol. 2011;410:268–279. doi: 10.1016/j.jmb.2011.04.075. PubMed DOI

Lee G, Won HS, Lee YM, Choi JW, Oh TI, Jang JH, Choi DK, Lim BO, Kim YJ, Park JW, Puigserver P, Lim JH. Oxidative Dimerization of PHD2 is Responsible for its Inactivation and Contributes to Metabolic Reprogramming via HIF-1alpha Activation. Sci Rep. 2016;6:18928. doi: 10.1038/srep18928. PubMed DOI PMC

Hewitson KS, Lienard BM, McDonough MA, Clifton IJ, Butler D, Soares AS, Oldham NJ, McNeill LA, Schofield CJ. Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates. J Biol Chem. 2007;282:3293–3301. doi: 10.1074/jbc.M608337200. PubMed DOI

Koivunen P, Hirsila M, Remes AM, Hassinen IE, Kivirikko KI, Myllyharju J. Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: Possible links between cell metabolism and stabilization of HIF. J Biol Chem. 2007;282:4524–4532. doi: 10.1074/jbc.M610415200. PubMed DOI

Martínez-Reyes I, Diebold LP, Kong H, Schieber M, Huang H, Hensley CT, Mehta MM, Wang T, Santos JH, Woychik R, Dufour E, Spelbrink JN, Weinberg SE, Zhao Y, DeBerardinis RJ, Chandel NS. TCA Cycle and Mitochondrial Membrane Potential Are Necessary for Diverse Biological Functions. Mol Cell. 2016;61:199–209. doi: 10.1016/j.molcel.2015.12.002. PubMed DOI PMC

Bell EL, Klimova TA, Eisenbart J, Moraes CT, Murphy MP, Budinger GR, Chandel NS. The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production. J Cell Biol. 2007;177:1029–1036. doi: 10.1083/jcb.200609074. PubMed DOI PMC

Nguyen LK, Cavadas MA, Scholz CC, Fitzpatrick SF, Bruning U, Cummins EP, Tambuwala MM, Manresa MC, Kholodenko BN, Taylor CT, Cheong A. A dynamic model of the hypoxia-inducible factor 1alpha (HIF-1alpha) network. J Cell Sci. 2013;126:1454–1463. doi: 10.1242/jcs.119974. PubMed DOI

Plecitá-Hlavatá L, Ježek J, Ježek P. Aglycemia keeps mitochondrial oxidative phosphorylation under hypoxic conditions in HepG2 cells. J Bioenerg Biomembr. 2015;47:467–476. doi: 10.1007/s10863-015-9628-6. PubMed DOI

Hernansanz-Agustín P, Ramos E, Navarro E, Parada E, Sánchez-López N, Peláez-Aguado L, Cabrera-García JD, Tello D, Buendia I, Marina A, Egea J, López MG, Bogdanova A, Martínez-Ruiz A. Mitochondrial complex I deactivation is related to superoxide production in acute hypoxia. Redox Biol. 2017;12:1040–1051. doi: 10.1016/j.redox.2017.04.025. PubMed DOI PMC

Chandel NS, Maltepe E, Goldwasser E, Mathieu CE, Simon MC, Schumacker PT. Mitochondrial reactive oxygen species trigger hypoxia-induced transcription. Proc Natl Acad Sci U S A. 1998;95:11715–11720. doi: 10.1073/pnas.95.20.11715. PubMed DOI PMC

Comito G, Calvani M, Giannoni E, Bianchini F, Calorini L, Torre E, Migliore C, Giordano S, Chiarugi P. HIF-1alpha stabilization by mitochondrial ROS promotes Met-dependent invasive growth and vasculogenic mimicry in melanoma cells. Free Radic Biol Med. 2011;51:893–904. doi: 10.1016/j.freeradbiomed.2011.05.042. PubMed DOI

Guzy RD, Hoyos B, Robin E, Chen H, Liu L, Mansfield KD, Simon MC, Hammerling U, Schumacker PT. Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing. Cell Metab. 2005;1:401–408. doi: 10.1016/j.cmet.2005.05.001. PubMed DOI

Schroedl C, McClintock DS, Budinger GR, Chandel NS. Hypoxic but not anoxic stabilization of HIF-1alpha requires mitochondrial reactive oxygen species. Am J Physiol. 2002;283:L922–L931. doi: 10.1152/ajplung.00014.2002. PubMed DOI

Ježek J, Plecitá-Hlavatá L, Ježek P. Aglycemic HepG2 cells switch from aminotransferase glutaminolytic pathway of pyruvate utilization to complete Krebs cycle at hypoxia. Front Endocrinol. 2018;9:637. doi: 10.3389/fendo.2018.00637. PubMed DOI PMC

Patten DA, Lafleur VN, Robitaille GA, Chan DA, Giaccia AJ, Richard DE. Hypoxia-inducible factor-1 activation in nonhypoxic conditions: The essential role of mitochondrial-derived reactive oxygen species. Mol Biol Cell. 2010;21:3247–3257. doi: 10.1091/mbc.e10-01-0025. PubMed DOI PMC

Brunelle JK, Bell EL, Quesada NM, Vercauteren K, Tiranti V, Zeviani M, Scarpulla RC, Chandel NS. Oxygen sensing requires mitochondrial ROS but not oxidative phosphorylation. Cell Metab. 2005;1:409–414. doi: 10.1016/j.cmet.2005.05.002. PubMed DOI

Pi J, Bai Y, Zhang Q, Wong V, Floering LM, Daniel K, Reece JM, Deeney JT, Andersen ME, Corkey BE, Collins S. Reactive oxygen species as a signal in glucose-stimulated insulin secretion. Diabetes. 2007;56:1783–1791. doi: 10.2337/db06-1601. PubMed DOI

Ashcroft FM, Rorsman P. Diabetes mellitus and the β cell: the last ten years. Cell. 2012;148:1160–1171. doi: 10.1016/j.cell.2012.02.010. PubMed DOI PMC

Ho T, Potapenko E, Davis DB, Merrins MJ. A plasma membrane-associated glycolytic metabolon is functionally coupled to KATP channels in pancreatic α and β cells from humans and mice. Cell Rep. 2023;42:112394. doi: 10.1016/j.celrep.2023.112394. PubMed DOI PMC

Plecitá-Hlavatá L, Jabůrek M, Holendová B, Tauber J, Pavluch V, Berková Z, Cahová M, Schröder K, Brandes RP, Siemen D, Ježek P. Glucose-Stimulated Insulin Secretion Fundamentally Requires H2O2 Signaling by NADPH Oxidase 4. Diabetes. 2020;69:1341–1354. doi: 10.2337/db19-1130. PubMed DOI

Yosida M, Dezaki K, Uchida K, Kodera S, Lam NV, Ito K, Rita RS, Yamada H, Shimomura K, Ishikawa SE, Sugawara H, Kawakami M, Tominaga M, Yada T, Kakei M. Involvement of cAMP/EPAC/TRPM2 activation in glucose- and incretin-induced insulin secretion. Diabetes. 2014;63:3394–3403. doi: 10.2337/db13-1868. PubMed DOI

Spégel P, Sharoyko VV, Goehring I, Danielsson AP, Malmgren S, Nagorny CL, Andersson LE, Koeck T, Sharp GW, Straub SG, Wollheim CB, Mulder H. Time-resolved metabolomics analysis of β-cells implicates the pentose phosphate pathway in the control of insulin release. Biochem J. 2013;450:595–605. doi: 10.1042/BJ20121349. PubMed DOI

Plecitá-Hlavatá L, Engstová H, Holendová B, Tauber J, Špaček T, Petrásková L, Křen V, Špačková J, Gotvaldová K, Ježek J, Dlasková A, Smolková K, Ježek P. Mitochondrial Superoxide Production Decreases on Glucose-Stimulated Insulin Secretion in Pancreatic β Cells Due to Decreasing Mitochondrial Matrix NADH/NAD+ Ratio. Antioxid Redox Signal. 2020;33:789–815. doi: 10.1089/ars.2019.7800. PubMed DOI PMC

Jitrapakdee S, Wutthisathapornchai A, Wallace JC, MacDonald MJ. Regulation of insulin secretion: role of mitochondrial signalling. Diabetologia. 2010;53:1019–1032. doi: 10.1007/s00125-010-1685-0. PubMed DOI PMC

Smolková K, Dvořák A, Zelenka J, Vítek L, Ježek P. Reductive carboxylation and 2-hydroxyglutarate formation by wild-type IDH2 in breast carcinoma cells. Int J Biochem Cell Biol. 2015;65:125–133. doi: 10.1016/j.biocel.2015.05.012. PubMed DOI

Lenzen S, Drinkgern J, Tiedge M. Low antioxidant enzyme gene expression in pancreatic islets compared with various other mouse tissues. Free Radic Biol Med. 1996;20:463–466. doi: 10.1016/0891-5849(96)02051-5. PubMed DOI

Ježek P, Dlasková A, Plecitá-Hlavatá L. Redox Homeostasis in Pancreatic β Cells. Oxid Med Cell Longev. 2012;2012:932838. doi: 10.1155/2012/932838. PubMed DOI PMC

Lenzen S. Oxidative stress: the vulnerable beta-cell. Biochem Soc Trans. 2008;36:343–347. doi: 10.1042/BST0360343. PubMed DOI

Prentki M, Matschinsky FM, Madiraju SR. Metabolic signaling in fuel-induced insulin secretion. Cell Metab. 2013;18:162–185. doi: 10.1016/j.cmet.2013.05.018. PubMed DOI

Carpinelli AR, Picinato MC, Stevanato E, Oliveira HR, Curi R. Insulin secretion induced by palmitate-a process fully dependent on glucose concentration. Diabetes Metab. 2002;28(3):S37–44. PubMed

Gehrmann W, Elsner M, Lenzen S. Role of metabolically generated reactive oxygen species for lipotoxicity in pancreatic β-cells. Diab Obes Metab. 2010;12(Suppl 2):149–158. doi: 10.1111/j.1463-1326.2010.01265.x. PubMed DOI

Graciano MF, Valle MM, Kowluru A, Curi R, Carpinelli AR. Regulation of insulin secretion and reactive oxygen species production by free fatty acids in pancreatic islets. Islets. 2011;3:213–223. doi: 10.4161/isl.3.5.15935. PubMed DOI

Cen J, Sargsyan E, Bergsten P. Fatty acids stimulate insulin secretion from human pancreatic islets at fasting glucose concentrations via mitochondria-dependent and -independent mechanisms. Nutr Metab (Lond) 2016;13:59. doi: 10.1186/s12986-016-0119-5. PubMed DOI PMC

Fernandez J, Valdeolmillos M. Increased levels of free fatty acids in fasted mice stimulate in vivo beta-cell electrical activity. Diabetes. 1998;47:1707–1712. doi: 10.2337/diabetes.47.11.1707. PubMed DOI

Hauke S, Keutler K, Phapale P, Yushchenko DA, Schultz C. Endogenous Fatty Acids Are Essential Signaling Factors of Pancreatic β-Cells and Insulin Secretion. Diabetes. 2018;67:1986–1998. doi: 10.2337/db17-1215. PubMed DOI

Ježek P, Jabůrek M, Holendová B, Plecitá-Hlavatá L. Fatty Acid-Stimulated Insulin Secretion vs. Lipotoxicity. Molecules. 2018;23:1483. doi: 10.3390/molecules23061483. PubMed DOI PMC

Saadeh M, Ferrante TC, Kane A, Shirihai O, Corkey BE, Deeney JT. Reactive oxygen species stimulate insulin secretion in rat pancreatic islets: studies using mono-oleoyl-glycerol. PLoS One. 2012;7:e30200. doi: 10.1371/journal.pone.0030200. PubMed DOI PMC

Leloup C, Tourrel-Cuzin C, Magnan C, Karaca M, Castel J, Carneiro L, Colombani AL, Ktorza A, Casteilla L, Pénicaud L. Mitochondrial reactive oxygen species are obligatory signals for glucose-induced insulin secretion. Diabetes. 2009;58:673–681. doi: 10.2337/db07-1056. PubMed DOI PMC

Yang HQ, Martinez-Ortiz W, Hwang J, Fan X, Cardozo TJ, Coetzee WA. Palmitoylation of the K(ATP)channel Kir6.2 subunit promotes channel opening by regulating PIP(2) sensitivity. Proc Natl Acad Sci U S A. 2020;117:10593–10602. doi: 10.1073/pnas.1918088117. PubMed DOI PMC

Shigeto M, Ramracheya R, Tarasov AI, Cha CY, Chibalina MV, Hastoy B, Philippaert K, Reinbothe T, Rorsman N, Salehi A, Sones WR, Vergari E, Weston C, Gorelik J, Katsura M, Nikolaev VO, Vennekens R, Zaccolo M, Galione A, Johnson PR, Kaku K, Ladds G, Rorsman P. GLP-1 stimulates insulin secretion by PKC-dependent TRPM4 and TRPM5 activation. J Clin Invest. 2015;125:4714–4728. doi: 10.1172/JCI81975. PubMed DOI PMC

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