References
- Harman D (1956) Aging: a theory based on free radical and radiation chemistry. J Gerontol 11, 298-300 https://doi.org/10.1093/geronj/11.3.298
- Harman D (2009) Origin and evolution of the free radical theory of aging: a brief personal history, 1954-2009. Biogerontology 10, 773 https://doi.org/10.1007/s10522-009-9234-2
- Harman D (1972) The biologic clock: the mitochondria? J Am Geriatr Soc 20, 145-147 https://doi.org/10.1111/j.1532-5415.1972.tb00787.x
- Yakes FM, Van Houten B (1997) Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress. Proc Natl Acad Sci U S A 94, 514-519 https://doi.org/10.1073/pnas.94.2.514
- Kazak L, Reyes A, Holt IJ (2012) Minimizing the damage: repair pathways keep mitochondrial DNA intact. Nat Rev Mol Cell Biol 13, 659-671 https://doi.org/10.1038/nrm3439
- Kang D, Kim SH, Hamasaki N (2007) Mitochondrial transcription factor A (TFAM): roles in maintenance of mtDNA and cellular functions. Mitochondrion 7, 39-44 https://doi.org/10.1016/j.mito.2006.11.017
- Lee SR, Han J (2017) Mitochondrial nucleoid: shield and switch of the mitochondrial genome. Oxid Med Cell Longev 2017 [Epub ahead of print]
- Chen H, Vermulst M, Wang YE et al (2010) Mitochondrial Fusion Is Required for mtDNA Stability in Skeletal Muscle and Tolerance of mtDNA Mutations. Cell 141, 280-289 https://doi.org/10.1016/j.cell.2010.02.026
- Prevost CT, Peris N, Seger C et al (2018) The influence of mitochondrial dynamics on mitochondrial genome stability. Curr Genet 64, 199-214 https://doi.org/10.1007/s00294-017-0717-4
- Pickles S, Vigie P, Youle RJ (2018) Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance. Curr Biol 28, R170-R185 https://doi.org/10.1016/j.cub.2018.01.004
- Cortopassi GA, Arnheim N (1990) Detection of a specific mitochondrial DNA deletion in tissues of older humans. Nucleic Acids Res 18, 6927-6933 https://doi.org/10.1093/nar/18.23.6927
- Piko L, Hougham AJ, Bulpitt KJ (1988) Studies of sequence heterogeneity of mitochondrial DNA from rat and mouse tissues: evidence for an increased frequency of deletions/additions with aging. Mech Ageing Dev 43, 279-293 https://doi.org/10.1016/0047-6374(88)90037-1
- Larsson NG (2010) Somatic mitochondrial DNA mutations in mammalian aging. Annu Rev Biochem 79, 683-706 https://doi.org/10.1146/annurev-biochem-060408-093701
- Payne BA, Wilson IJ, Yu-Wai-Man P et al (2013) Universal heteroplasmy of human mitochondrial DNA. Hum Mol Genet 22, 384-390 https://doi.org/10.1093/hmg/dds435
- Linnane AW, Marzuki S, Ozawa T, Tanaka M (1989) Mitochondrial DNA mutations as an important contributor to ageing and degenerative diseases. Lancet 1, 642-645
- Khrapko K, Vijg J (2009) Mitochondrial DNA mutations and aging: devils in the details? Trends Genet 25, 91-98 https://doi.org/10.1016/j.tig.2008.11.007
- Rossignol R, Faustin B, Rocher C, Malgat M, Mazat JP, Letellier T (2003) Mitochondrial threshold effects. Biochem J 370, 751-762 https://doi.org/10.1042/bj20021594
- Stewart JB, Chinnery PF (2015) The dynamics of mitochondrial DNA heteroplasmy: implications for human health and disease. Nat Rev Genet 16, 530-542 https://doi.org/10.1038/nrg3966
- Kauppila TES, Kauppila JHK, Larsson NG (2017) Mammalian Mitochondria and Aging: An Update. Cell Metab 25, 57-71 https://doi.org/10.1016/j.cmet.2016.09.017
- Pomatto LCD, Davies KJA (2018) Adaptive homeostasis and the free radical theory of ageing. Free Radic Biol Med 124, 420-430 https://doi.org/10.1016/j.freeradbiomed.2018.06.016
- Unlu ES, Koc A (2007) Effects of deleting mitochondrial antioxidant genes on life span. Ann N Y Acad Sci 1100, 505-509 https://doi.org/10.1196/annals.1395.055
- Longo VD, Gralla EB, Valentine JS (1996) Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae Mitochondrial production of toxic oxygen species in vivo. J Biol Chem 271, 12275-12280 https://doi.org/10.1074/jbc.271.21.12275
- Doonan R, McElwee JJ, Matthijssens F et al (2008) Against the oxidative damage theory of aging: superoxide dismutases protect against oxidative stress but have little or no effect on life span in Caenorhabditis elegans. Genes Dev 22, 3236-3241 https://doi.org/10.1101/gad.504808
- Kirby K, Hu J, Hilliker AJ, Phillips JP (2002) RNA interference-mediated silencing of Sod2 in Drosophila leads to early adult-onset mortality and elevated endogenous oxidative stress. Proc Natl Acad Sci U S A 99, 16162-16167 https://doi.org/10.1073/pnas.252342899
- Martin I, Jones MA, Rhodenizer D et al (2009) Sod2 knockdown in the musculature has whole-organism consequences in Drosophila. Free Radic Biol Med 47, 803-813 https://doi.org/10.1016/j.freeradbiomed.2009.06.021
- Duttaroy A, Paul A, Kundu M, Belton A (2003) A Sod2 null mutation confers severely reduced adult life span in Drosophila. Genetics 165, 2295-2299 https://doi.org/10.1093/genetics/165.4.2295
- Wicks S, Bain N, Duttaroy A, Hilliker AJ, Phillips JP (2009) Hypoxia rescues early mortality conferred by superoxide dismutase deficiency. Free Radic Biol Med 46, 176-181 https://doi.org/10.1016/j.freeradbiomed.2008.09.036
- Perez VI, Bokov A, Van Remmen H et al (2009) Is the oxidative stress theory of aging dead? Biochim Biophys Acta 1790, 1005-1014 https://doi.org/10.1016/j.bbagen.2009.06.003
- Fabrizio P, Liou LL, Moy VN et al (2003) SOD2 functions downstream of Sch9 to extend longevity in yeast. Genetics 163, 35-46 https://doi.org/10.1093/genetics/163.1.35
- Cabreiro F, Ackerman D, Doonan R et al (2011) Increased life span from overexpression of superoxide dismutase in Caenorhabditis elegans is not caused by decreased oxidative damage. Free Radic Biol Med 51, 1575-1582 https://doi.org/10.1016/j.freeradbiomed.2011.07.020
- Melov S, Ravenscroft J, Malik S et al (2000) Extension of Life-Span with Superoxide Dismutase/Catalase Mimetics. Science 289, 1567-1569 https://doi.org/10.1126/science.289.5484.1567
- Curtis C, Landis GN, Folk D et al (2007) Transcriptional profiling of MnSOD-mediated lifespan extension in Drosophilareveals a species-general network of aging and metabolic genes. Genome Biol 8, R262 https://doi.org/10.1186/gb-2007-8-12-r262
- Sun J, Folk D, Bradley TJ, Tower J (2002) Induced overexpression of mitochondrial Mn-superoxide dismutase extends the life span of adult Drosophila melanogaster. Genetics 161, 661-672 https://doi.org/10.1093/genetics/161.2.661
- Parkes TL, Elia AJ, Dickinson D, Hilliker AJ, Phillips JP, Boulianne GL (1998) Extension of Drosophila lifespan by overexpression of human SOD1 in motorneurons. Nat Genet 19, 171-174 https://doi.org/10.1038/534
- Schriner SE, Linford NJ, Martin GM et al (2005) Extension of murine life span by overexpression of catalase targeted to mitochondria. Science 308, 1909-1911 https://doi.org/10.1126/science.1106653
- Lee HY, Choi CS, Birkenfeld AL et al (2010) Targeted expression of catalase to mitochondria prevents age-associated reductions in mitochondrial function and insulin resistance. Cell Metab 12, 668-674 https://doi.org/10.1016/j.cmet.2010.11.004
- Brooks AR, Harkins RN, Wang P, Qian HS, Liu P, Rubanyi GM (2004) Transcriptional silencing is associated with extensive methylation of the CMV promoter following adenoviral gene delivery to muscle. J Gene Med 6, 395-404 https://doi.org/10.1002/jgm.516
- Cooke MS, Evans MD, Dizdaroglu M, Lunec J (2003) Oxidative DNA damage: mechanisms, mutation, and disease. FASEB J 17, 1195-1214 https://doi.org/10.1096/fj.02-0752rev
- Vermulst M, Bielas JH, Kujoth GC (2007) Mitochondrial point mutations do not limit the natural lifespan of mice. Nat Genet 39, 540-543 https://doi.org/10.1038/ng1988
- Ameur A, Stewart JB, Freyer C et al (2011) Ultra-deep sequencing of mouse mitochondrial DNA: mutational patterns and their origins. PLoS Genet 7, e1002028 https://doi.org/10.1371/journal.pgen.1002028
- Kennedy SR, Salk JJ, Schmitt MW, Loeb LA (2013) Ultra-sensitive sequencing reveals an age-related increase in somatic mitochondrial mutations that are inconsistent with oxidative damage. PLoS Genet 9, e1003794 https://doi.org/10.1371/journal.pgen.1003794
- Trifunovic A, Wredenberg A, Falkenberg M et al (2004) Premature ageing in mice expressing defective mitochondrial DNA polymerase. Nature 429, 417-423 https://doi.org/10.1038/nature02517
- Edgar D, Shabalina I, Camara Y et al (2009) Random point mutations with major effects on protein-coding genes are the driving force behind premature aging in mtDNA mutator mice. Cell Metab 10, 131-138 https://doi.org/10.1016/j.cmet.2009.06.010
- Kujoth GC, Hiona A, Pugh TD et al (2005) Mitochondrial DNA Mutations, Oxidative Stress, and Apoptosis in Mammalian Aging. Science 309, 481-484 https://doi.org/10.1126/science.1112125
- Trifunovic A, Hansson A, Wredenberg A et al (2005) Somatic mtDNA mutations cause aging phenotypes without affecting reactive oxygen species production. Proc Natl Acad Sci U S A 102, 17993-17998 https://doi.org/10.1073/pnas.0508886102
- Logan A, Shabalina IG, Prime TA et al (2014) In vivo levels of mitochondrial hydrogen peroxide increase with age in mtDNA mutator mice. Aging Cell 13, 765-768 https://doi.org/10.1111/acel.12212
- DeBalsi KL, Hoff KE, Copeland WC (2017) Role of the mitochondrial DNA replication machinery in mitochondrial DNA mutagenesis, aging and age-related diseases. Ageing Res Rev 33, 89-104 https://doi.org/10.1016/j.arr.2016.04.006
- Bua E, Johnson J, Herbst A et al (2006) Mitochondrial DNA-Deletion Mutations Accumulate Intracellularly to Detrimental Levels in Aged Human Skeletal Muscle Fibers. Am J Hum Genet 79, 469-480 https://doi.org/10.1086/507132
- Cortopassi GA, Arnheim N (1990) Detection of a specific mitochondrial DNA deletion in tissues of older humans. Nucleic Acids Res 18, 6927-6933 https://doi.org/10.1093/nar/18.23.6927
- Bender A, Krishnan KJ, Morris CM et al (2006) High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease. Nat Genet 38, 515-517 https://doi.org/10.1038/ng1769
- Vermulst M, Wanagat J, Kujoth GC et al (2008) DNA deletions and clonal mutations drive premature aging in mitochondrial mutator mice. Nat Genet 40, 392-394 https://doi.org/10.1038/ng.95
- Wallace DC (2005) A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu Rev Genet 39, 359-407 https://doi.org/10.1146/annurev.genet.39.110304.095751
- Sarsour EH, Kalen AL, Goswami PC (2014) Manganese superoxide dismutase regulates a redox cycle within the cell cycle. Antioxid Redox Signal 20, 1618-1627 https://doi.org/10.1089/ars.2013.5303
- Ristow M (2014) Unraveling the truth about antioxidants: mitohormesis explains ROS-induced health benefits. Nat Med 20, 709-711 https://doi.org/10.1038/nm.3624
- Sun N, Youle RJ, Finkel T (2016) The Mitochondrial Basis of Aging. Mol Cell 61, 654-666 https://doi.org/10.1016/j.molcel.2016.01.028
- Shadel GS, Horvath TL (2015) Mitochondrial ROS signaling in organismal homeostasis. Cell 163, 560-569 https://doi.org/10.1016/j.cell.2015.10.001
- Lee SS, Lee RY, Fraser AG, Kamath RS, Ahringer J, Ruvkun G (2003) A systematic RNAi screen identifies a critical role for mitochondria in C. elegans longevity. Nat Genet 33, 40-48 https://doi.org/10.1038/ng1056
- Dillin A, Hsu AL, Arantes-Oliveira N et al (2002) Rates of behavior and aging specified by mitochondrial function during development. Science 298, 2398-2401 https://doi.org/10.1126/science.1077780
- Zarse K, Schmeisser S, Groth M et al (2012) Impaired insulin/IGF1 signaling extends life span by promoting mitochondrial L-proline catabolism to induce a transient ROS signal. Cell Metab 15, 451-465 https://doi.org/10.1016/j.cmet.2012.02.013
- Lee SJ, Hwang AB, Kenyon C (2010) Inhibition of respiration extends C. elegans life span via reactive oxygen species that increase HIF-1 activity. Curr Biol 20, 2131-2136 https://doi.org/10.1016/j.cub.2010.10.057
- Munoz-Najar U, Sedivy JM (2011) Epigenetic control of aging. Antioxid Redox Signal 14, 241-259 https://doi.org/10.1089/ars.2010.3250
- Rando TA, Chang HY (2012) Aging, rejuvenation, and epigenetic reprogramming: resetting the aging clock. Cell 148, 46-57 https://doi.org/10.1016/j.cell.2012.01.003
- Schroeder EA, Raimundo N, Shadel GS (2013) Epigenetic silencing mediates mitochondria stressinduced longevity. Cell Metab 17, 954-964 https://doi.org/10.1016/j.cmet.2013.04.003
- Shpilka T, Haynes CM (2018) The mitochondrial UPR: mechanisms, physiological functions and implications in ageing. Nat Rev Mol Cell Biol 19, 109-120 https://doi.org/10.1038/nrm.2017.110
- Nargund AM, Fiorese CJ, Pellegrino MW, Deng P, Haynes CM (2015) Mitochondrial and nuclear accumulation of the transcription factor ATFS-1 promotes OXPHOS recovery during the UPR mt. Mol Cell 58, 123-133 https://doi.org/10.1016/j.molcel.2015.02.008
- Nargund AM, Pellegrino MW, Fiorese CJ, Baker BM, Haynes CM (2012) Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science 337, 587-590 https://doi.org/10.1126/science.1223560
- Tian Y, Garcia G, Bian Q et al (2016) Mitochondrial Stress Induces Chromatin Reorganization to Promote Longevity and UPR(mt). Cell 165, 1197-1208 https://doi.org/10.1016/j.cell.2016.04.011
- Felkai S, Ewbank JJ, Lemieux J, Labbe JC, Brown GG, Hekimi S (1999) CLK-1 controls respiration, behavior and aging in the nematode Caenorhabditis elegans. EMBO J 18, 1783-1792 https://doi.org/10.1093/emboj/18.7.1783
- Liu X, Jiang N, Hughes B, Bigras E, Shoubridge E, Hekimi S (2005) Evolutionary conservation of the clk-1-dependent mechanism of longevity: loss of mclk1 increases cellular fitness and lifespan in mice. Genes Dev 19, 2424-2434 https://doi.org/10.1101/gad.1352905
- Frezza C (2017) Mitochondrial metabolites: undercover signalling molecules. Interface Focus 7, 20160100 https://doi.org/10.1098/rsfs.2016.0100
- Sullivan LB, Gui DY, Vander Heiden MG (2016) Altered metabolite levels in cancer: implications for tumour biology and cancer therapy. Nat Rev Cancer 16, 680-693 https://doi.org/10.1038/nrc.2016.85
- Menzies KJ, Zhang H, Katsyuba E, Auwerx J (2016) Protein acetylation in metabolism-metabolites and cofactors. Nat Rev Endocrinol 12, 43-60 https://doi.org/10.1038/nrendo.2015.181
- Sutendra G, Kinnaird A, Dromparis P et al (2014) A nuclear pyruvate dehydrogenase complex is important for the generation of acetyl-CoA and histone acetylation. Cell 158, 84-97 https://doi.org/10.1016/j.cell.2014.04.046
- Shi L, Tu BP (2015) Acetyl-CoA and the regulation of metabolism: mechanisms and consequences. Curr Opin Cell Biol 33, 125-131 https://doi.org/10.1016/j.ceb.2015.02.003
- Choudhary C, Weinert BT, Nishida Y, Verdin E, Mann M (2014) The growing landscape of lysine acetylation links metabolism and cell signalling. Nat Rev Mol Cell Biol 15, 536-550 https://doi.org/10.1038/nrm3841
- Xie Z, Dai J, Dai L et al (2012) Lysine succinylation and lysine malonylation in histones. Mol Cell Proteomics 11, 100-107 https://doi.org/10.1074/mcp.M111.015875
- Benayoun BA, Pollina EA, Brunet A (2015) Epigenetic regulation of ageing: linking environmental inputs to genomic stability. Nat Rev Mol Cell Biol 16, 593-610 https://doi.org/10.1038/nrm4048
- Schultz MB, Sinclair DA (2016) Why NAD+ Declines during Aging: It's Destroyed. Cell Metab 23, 965-966 https://doi.org/10.1016/j.cmet.2016.05.022
- Camacho-Pereira J, Tarrago MG, Chini CCS et al (2016) CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction through an SIRT3-Dependent Mechanism. Cell Metab 23, 1127-1139 https://doi.org/10.1016/j.cmet.2016.05.006
- Imai S-I, Guarente L (2016) It takes two to tango: NAD+ and sirtuins in aging/longevity control. NPJ Aging Mech Dis 2, 16017 https://doi.org/10.1038/npjamd.2016.17
- Gomes AP, Price NL, Ling AJ et al (2013) Declining NAD(+) induces a pseudohypoxic state disrupting nuclear-mitochondrial communication during aging. Cell 155, 1624-1638 https://doi.org/10.1016/j.cell.2013.11.037
- Mouchiroud L, Houtkooper RH, Moullan N et al (2013) The NAD+/sirtuin pathway modulates longevity through activation of mitochondrial UPR and FOXO signaling. Cell 154, 430-441 https://doi.org/10.1016/j.cell.2013.06.016
- Yoshino J, Mills KF, Yoon MJ, Imai S (2011) Nicotinamide mononucleotide, a key NAD+ intermediate, treats the pathophysiology of diet-and age-induced diabetes in mice. Cell Metab 14, 528-536 https://doi.org/10.1016/j.cmet.2011.08.014
- Quiros PM, Mottis A, Auwerx J (2016) Mitonuclear communication in homeostasis and stress. Nat Rev Mol Cell Biol 17, 213-226 https://doi.org/10.1038/nrm.2016.23
- Mammucari C, Gherardi G, Zamparo I et al (2015) The mitochondrial calcium uniporter controls skeletal muscle trophism in vivo. Cell Rep 10, 1269-1279 https://doi.org/10.1016/j.celrep.2015.01.056
- Franceschi C, Garagnani P, Parini P, Giuliani C, Santoro A (2018) Inflammaging: a new immune-metabolic viewpoint for age-related diseases. Nat Rev Endocrinol 14, 576-590 https://doi.org/10.1038/s41574-018-0059-4
- Davis BK, Wen H, Ting JP (2011) The inflammasome NLRs in immunity, inflammation, and associated diseases. Annu Rev Immunol 29, 707-735 https://doi.org/10.1146/annurev-immunol-031210-101405
- Wenceslau CF, McCarthy CG, Szasz T et al (2014) Mitochondrial damage-associated molecular patterns and vascular function. Eur Heart J 35, 1172-1177 https://doi.org/10.1093/eurheartj/ehu047
- Zhang Q, Raoof M, Chen Y et al (2010) Circulating mitochondrial DAMPs cause inflammatory responses to injury. Nature 464, 104-107 https://doi.org/10.1038/nature08780
- Grazioli S, Pugin J (2018) Mitochondrial Damage-Associated Molecular Patterns: From Inflammatory Signaling to Human Diseases. Front Immunol 9, 832 https://doi.org/10.3389/fimmu.2018.00832
- Pinti M, Cevenini E, Nasi M et al (2014) Circulating mitochondrial DNA increases with age and is a familiar trait: Implications for "inflamm-aging". Eur J Immunol 44, 1552-1562 https://doi.org/10.1002/eji.201343921
- Furman D, Chang J, Lartigue L et al (2017) Expression of specific inflammasome gene modules stratifies older individuals into two extreme clinical and immunological states. Nat Med 23, 174-184 https://doi.org/10.1038/nm.4267
- Franceschi C, Garagnani P, Parini P, Giuliani C, Santoro A (2018) Inflammaging: a new immune-metabolic viewpoint for age-related diseases. Nat Rev Endocrinol 14, 576-590 https://doi.org/10.1038/s41574-018-0059-4
- Kim SJ, Xiao J, Wan J, Cohen P, Yen K (2017) Mitochondrially derived peptides as novel regulators of metabolism. J Physiol 595, 6613-6621 https://doi.org/10.1113/JP274472
- Hashimoto Y, Niikura T, Tajima H et al (2001) A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer's disease genes and Abeta. Proc Natl Acad Sci U S A 98, 6336-6341 https://doi.org/10.1073/pnas.101133498
- Ikonen M, Liu B, Hashimoto Y et al (2003) Interaction between the Alzheimer's survival peptide humanin and insulin-like growth factor-binding protein 3 regulates cell survival and apoptosis. Proc Natl Acad Sci U S A 100, 13042-13047 https://doi.org/10.1073/pnas.2135111100
- Guo B, Zhai D, Cabezas E et al (2003) Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature 423, 456-461 https://doi.org/10.1038/nature01627
- Cobb LJ, Lee C, Xiao J et al (2016) Naturally occurring mitochondrial-derived peptides are age-dependent regulators of apoptosis, insulin sensitivity, and inflammatory markers. Aging 8, 796-809 https://doi.org/10.18632/aging.100943
- Zarse K, Ristow M (2015) A mitochondrially encoded hormone ameliorates obesity and insulin resistance. Cell Metab 21, 355-356 https://doi.org/10.1016/j.cmet.2015.02.013
- Lee C, Zeng J, Drew BG et al (2015) The mitochondrialderived peptide MOTS-c promotes metabolic homeostasis and reduces obesity and insulin resistance. Cell Metab 21, 443-454 https://doi.org/10.1016/j.cmet.2015.02.009
- Lee C, Kim KH, Cohen P (2016) MOTS-c: A novel mitochondrial-derived peptide regulating muscle and fat metabolism. Free Radic Biol Med 100, 182-187 https://doi.org/10.1016/j.freeradbiomed.2016.05.015
- Kim KH, Son JM, Benayoun BA, Lee C (2018) The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress. Cell Metab 28, 516-524 https://doi.org/10.1016/j.cmet.2018.06.008
- Mangalhara KC, Shadel GS (2018) A Mitochondrial-Derived Peptide Exercises the Nuclear Option. Cell Metab 28, 330-331 https://doi.org/10.1016/j.cmet.2018.08.017
- Wong W (2018) Going nuclear with stress. Science Signaling 11, eaav4285 https://doi.org/10.1126/scisignal.aav4285
- Muzumdar RH, Huffman DM, Atzmon G et al (2009) Humanin: a novel central regulator of peripheral insulin action. PLoS One 4, e6334 https://doi.org/10.1371/journal.pone.0006334
- Lee C, Wan J, Miyazaki B et al (2014) IGF-I regulates the age-dependent signaling peptide humanin. Aging Cell 13, 958-961 https://doi.org/10.1111/acel.12243
- Fuku N, Pareja-Galeano H, Zempo H et al (2015) The mitochondrial-derived peptide MOTS-c: a player in exceptional longevity? Aging Cell 14, 921-923 https://doi.org/10.1111/acel.12389
- Zempo H, Fuku N, Nishida Y et al (2016) Relation between type 2 diabetes and m. 1382 A> C polymorphism which occurs amino acid replacement (K14Q) of mitochondria-derived MOTS-c. FASEB J 30, 956.1
- Price NL, Gomes AP, Ling AJ et al (2012) SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function. Cell Metab 15, 675-690 https://doi.org/10.1016/j.cmet.2012.04.003
- Canto C, Gerhart-Hines Z, Feige JN et al (2009) AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature 458, 1056-1060 https://doi.org/10.1038/nature07813
- Dunham-Snary KJ, Ballinger SW (2015) GENETICS. Mitochondrial-nuclear DNA mismatch matters. Science 349, 1449-1450 https://doi.org/10.1126/science.aac5271
- Rand DM (2017) Fishing for adaptive epistasis using mitonuclear interactions. PLoS Genet 13, e1006662 https://doi.org/10.1371/journal.pgen.1006662
- Tranah GJ (2011) Mitochondrial-nuclear epistasis: Implications for human aging and longevity. Ageing Res Rev 10, 238-252 https://doi.org/10.1016/j.arr.2010.06.003
- McManus MJ, Picard M, Chen HW et al (2018) Mitochondrial DNA Variation Dictates Expressivity and Progression of Nuclear DNA Mutations Causing Cardiomyopathy. Cell Metab [Epub ahead of print]
- Deuse T, Wang D, Stubbendorff M et al (2015) SCNT-derived ESCs with mismatched mitochondria trigger an immune response in allogeneic hosts. Cell Stem Cell 16, 33-38 https://doi.org/10.1016/j.stem.2014.11.003
- Betancourt AM, King AL, Fetterman JL et al (2014) Mitochondrial-nuclear genome interactions in non-alcoholic fatty liver disease in mice. Biochemical J 461, 223-232 https://doi.org/10.1042/BJ20131433
- Fetterman JL, Zelickson BR, Johnson LW et al (2013) Mitochondrial genetic background modulates bioenergetics and susceptibility to acute cardiac volume overload. Biochemical J 455, 157-167 https://doi.org/10.1042/BJ20130029
- Raimundo N, Krisko A (2018) Cross-organelle communication at the core of longevity. Aging 10, 15-16 https://doi.org/10.18632/aging.101373
- Rieusset J (2018) The role of endoplasmic reticulummitochondria contact sites in the control of glucose homeostasis: an update. Cell Death Dis 9, 388 https://doi.org/10.1038/s41419-018-0416-1
- Janikiewicz J, Szymanski J, Malinska D et al (2018) Mitochondria-associated membranes in aging and senescence: structure, function, and dynamics. Cell Death Dis 9, 332 https://doi.org/10.1038/s41419-017-0105-5
- Wang CH, Chen YF, Wu CY et al (2014) Cisd2 modulates the differentiation and functioning of adipocytes by regulating intracellular Ca2+ homeostasis. Hum Mol Genet 23, 4770-4785 https://doi.org/10.1093/hmg/ddu193
- Chen YF, Kao CH, Chen YT et al (2009) Cisd2 deficiency drives premature aging and causes mitochondriamediated defects in mice. Genes Dev 23, 1183-1194 https://doi.org/10.1101/gad.1779509
- Titorenko VI, Terlecky SR (2011) Peroxisome metabolism and cellular aging. Traffic 12, 252-259 https://doi.org/10.1111/j.1600-0854.2010.01144.x
- Sebastian D, Palacin M, Zorzano A (2017) Mitochondrial dynamics: coupling mitochondrial fitness with healthy aging. Trends Mol Med 23, 201-215 https://doi.org/10.1016/j.molmed.2017.01.003
- Koepke JI, Nakrieko KA, Wood CS et al (2007) Restoration of peroxisomal catalase import in a model of human cellular aging. Traffic 8, 1590-1600 https://doi.org/10.1111/j.1600-0854.2007.00633.x
-
Santos MJ, Quintanilla RA, Toro A et al (2005) Peroxisomal proliferation protects from
${\beta}$ -amyloid neurodegeneration. J Biol Chem 280, 41057-41068 https://doi.org/10.1074/jbc.M505160200 - Nell HJ, Au JL, Giordano CR et al (2017) Targeted Antioxidant, Catalase-SKL, Reduces Beta-Amyloid Toxicity in the Rat Brain. Brain Pathol 27, 86-94 https://doi.org/10.1111/bpa.12368
- Yoboue ED, Sitia R, Simmen T (2018) Redox crosstalk at endoplasmic reticulum (ER) membrane contact sites (MCS) uses toxic waste to deliver messages. Cell Death Dis 9, 331 https://doi.org/10.1038/s41419-017-0033-4
- Carmona-Gutierrez D, Hughes AL, Madeo F, Ruckenstuhl C (2016) The crucial impact of lysosomes in aging and longevity. Ageing Res Rev 32, 2-12 https://doi.org/10.1016/j.arr.2016.04.009
- Soto-Heredero G, Baixauli F, Mittelbrunn M (2017) Interorganelle communication between mitochondria and the endolysosomal system. Front Cell Dev Biol 5, 95 https://doi.org/10.3389/fcell.2017.00095
- Hughes AL, Gottschling DE (2012) An early age increase in vacuolar pH limits mitochondrial function and lifespan in yeast. Nature 492, 261-265 https://doi.org/10.1038/nature11654
- Elbaz-Alon Y, Rosenfeld-Gur E, Shinder V, Futerman AH, Geiger T, Schuldiner M (2014) A dynamic interface between vacuoles and mitochondria in yeast. Dev Cell 30, 95-102 https://doi.org/10.1016/j.devcel.2014.06.007
- Klecker T, Westermann B (2014) Mitochondria Are Clamped to Vacuoles for Lipid Transport. Dev Cell 30, 1-2 https://doi.org/10.1016/j.devcel.2014.06.024
- Murley A, Sarsam RD, Toulmay A, Yamada J, Prinz WA, Nunnari J (2015) Ltc1 is an ER-localized sterol transporter and a component of ER-mitochondria and ER-vacuole contacts. J Cell Biol 209, 539-548 https://doi.org/10.1083/jcb.201502033
- Honscher C, Mari M, Auffarth K et al (2014) Cellular metabolism regulates contact sites between vacuoles and mitochondria. Dev Cell 30, 86-94 https://doi.org/10.1016/j.devcel.2014.06.006
- Durieux J, Wolff S, Dillin A (2011) The cell-nonautonomous nature of electron transport chain-mediated longevity. Cell 144, 79-91 https://doi.org/10.1016/j.cell.2010.12.016
- Woo DK, Shadel GS (2011) Mitochondrial stress signals revise an old aging theory. Cell 144, 11-12 https://doi.org/10.1016/j.cell.2010.12.023
- Zhang Q, Wu X, Chen P et al (2018) The mitochondrial unfolded protein response is mediated cell-nonautonomously by retromer-dependent Wnt signaling. Cell 174, 870-883.e817 https://doi.org/10.1016/j.cell.2018.06.029
- Owusu-Ansah E, Song W, Perrimon N (2013) Muscle mitohormesis promotes longevity via systemic repression of insulin signaling. Cell 155, 699-712 https://doi.org/10.1016/j.cell.2013.09.021
- Kim KH, Jeong YT, Oh H et al (2012) Autophagy deficiency leads to protection from obesity and insulin resistance by inducing Fgf21 as a mitokine. Nat Med 19, 83-92 https://doi.org/10.1038/nm.3014
- Berendzen KM, Durieux J, Shao LW et al (2016) Neuroendocrine coordination of mitochondrial stress signaling and proteostasis. Cell 166, 1553-1563.e1510 https://doi.org/10.1016/j.cell.2016.08.042
- Shao L-W, Niu R, Liu Y (2016) Neuropeptide signals cell non-autonomous mitochondrial unfolded protein response. Cell Res 26, 1182-1196 https://doi.org/10.1038/cr.2016.118
- da Cunha FM, Torelli NQ, Kowaltowski AJ (2015) Mitochondrial Retrograde Signaling: Triggers, Pathways, and Outcomes. Oxid Med Cell Longev 2015, 482582
- Lee C, Kim KH, Cohen P (2016) MOTS-c: a novel mitochondrial-derived peptide regulating muscle and fat metabolism. Free Radic Biol Med 100, 182-187 https://doi.org/10.1016/j.freeradbiomed.2016.05.015
- Bachar AR, Scheffer L, Schroeder AS et al (2010) Humanin is expressed in human vascular walls and has a cytoprotective effect against oxidized LDL-induced oxidative stress. Cardiovasc Res 88, 360-366 https://doi.org/10.1093/cvr/cvq191
- Guevara-Aguirre J, Balasubramanian P, Guevara-Aguirre M et al (2011) Growth hormone receptor deficiency is associated with a major reduction in pro-aging signaling, cancer, and diabetes in humans. Sci Transl Med 3, 70ra13 https://doi.org/10.1126/scitranslmed.3001845
- Cobb LJ, Lee C, Xiao J et al (2016) Naturally occurring mitochondrial-derived peptides are age-dependent regulators of apoptosis, insulin sensitivity, and inflammatory markers. Aging 8, 796-809 https://doi.org/10.18632/aging.100943