Ukr.Biochem.J. 2025; Volume 97, Issue 4, Jul-Aug, pp. 5-21

doi: https://doi.org/10.15407/ubj97.04.005

Mitogenesis, mitophagy and regulation of mitochondrial metabolism in health and disease

09.09.2025   Uncategorized   No comments

Charles G. Ward

Department of Biochemistry, Medical University of Gdańsk, Gdańsk, 80-208, Poland;
e-mail: Charles.ward@gumed.edu.pl

Received: 18 May 2025; Revised: 02 July 2025;
Accepted: 12 September 2025; Available on-line: 17 September 2025

The state of mitochondrial homeostasis, comprising the processes of mitochondrial biogenesis, selective removal of damaged or dysfunctional mitochondria, mitochondrial dynamics (fusion and fission), as well as signaling systems of mitochondrial metabolism regulation are analyzed in this review. Particular attention is paid to how the bioenergetic demands of tissues are modulated in viral SARS-CoV, hepatitis B, C infections and asthma.

Keywords: , , , , , ,

References:

  1. Bakeeva LE, Chentsov YuS, Skulachev VP. Mitochondrial framework (reticulum mitochondriale) in rat diaphragm muscle. Biochim Biophys Acta. 1978;501(3):349-369. PubMed, CrossRef
  2. Kayar SR, Claassen H, Hoppeler H, Weibel ER. Mitochondrial distribution in relation to changes in muscle metabolism in rat soleus. Respir Physiol. 1986;64(1):1-11. PubMed, CrossRef
  3. Wang L, Zhou X, Lu T. Role of mitochondria in physiological activities, diseases, and therapy. Mol Biomed. 2025;6(1):42. PubMed, PubMed, CrossRef
  4. James DI, Parone PA, Mattenberger Y, Martinou JC. hFis1, a novel component of the mammalian mitochondrial fission machinery. J Biol Chem. 2003;278(38):36373-36379. PubMed, CrossRef
  5. van der Bliek AM, Shen Q, Kawajiri S. Mechanisms of mitochondrial fission and fusion. Cold Spring Harb Perspect Biol. 2013;5(6):a011072. PubMed, PubMed, CrossRef
  6. Tokuyama T, Yanagi S. Role of Mitochondrial Dynamics in Heart Diseases. Genes (Basel). 2023;14(10):1876. PubMed, PubMed, CrossRef
  7. Zerihun M, Sukumaran S, Qvit N. The Drp1-Mediated Mitochondrial Fission Protein Interactome as an Emerging Core Player in Mitochondrial Dynamics and Cardiovascular Disease Therapy. Int J Mol Sci. 2023;24(6):5785. PubMed, PubMed, CrossRef
  8. Kitada T, Asakawa S, Hattori N, Matsumine H, Yamamura Y, Minoshima S, Yokochi M, Mizuno Y, Shimizu N. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature. 1998;392(6676):605-608. PubMed, CrossRef
  9. Valente EM, Abou-Sleiman PM, Caputo V, Muqit MM, Harvey K, Gispert S, Ali Z, Del Turco D, Bentivoglio AR, Healy DG, Albanese A, Nussbaum R, González-Maldonado R, Deller T, Salvi S, Cortelli P, Gilks WP, Latchman DS, Harvey RJ, Dallapiccola B, Auburger G, Wood NW. Hereditary early-onset Parkinson’s disease caused by mutations in PINK1. Science. 2004;304(5674):1158-1160. PubMed, CrossRef
  10. Alexander C, Votruba M, Pesch UE, Thiselton DL, Mayer S, Moore A, Rodriguez M, Kellner U, Leo-Kottler B, Auburger G, Bhattacharya SS, Wissinger B. OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. Nat Genet. 2000;26(2):211-215. PubMed, CrossRef
  11. Züchner S, Mersiyanova IV, Muglia M, Bissar-Tadmouri N, Rochelle J, Dadali EL, Zappia M, Nelis E, Patitucci A, Senderek J, Parman Y, Evgrafov O, Jonghe PD, Takahashi Y, Tsuji S, Pericak-Vance MA, Quattrone A, Battaloglu E, Polyakov AV, Timmerman V, Schröder JM, Vance JM. Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A. Nat Genet. 2004;36(5):449-451. PubMed, CrossRef
  12. Murata D, Roy S, Lutsenko S, Iijima M, Sesaki H. Slc25a3-dependent copper transport controls flickering-induced Opa1 processing for mitochondrial safeguard. Dev Cell. 2024;59(19):2578-2592.e7. PubMed, PubMed, CrossRef
  13. Meeusen SL, Nunnari J. How mitochondria fuse. Curr Opin Cell Biol. 2005;17(4):389-394. PubMed, CrossRef
  14. Meeusen S, DeVay R, Block J, Cassidy-Stone A, Wayson S, McCaffery JM, Nunnari J. Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1. Cell. 2006;127(2):383-395. PubMed, CrossRef
  15. Chan DC. Dissecting mitochondrial fusion. Dev Cell. 2006;11(5):592-594. PubMed, PubMed, CrossRef
  16. Iqbal S, Ostojic O, Singh K, Joseph AM, Hood DA. Expression of mitochondrial fission and fusion regulatory proteins in skeletal muscle during chronic use and disuse. Muscle Nerve. 2013;48(6):963-970. PubMed, CrossRef
  17. Wallace DC. Mitochondrial genetic medicine. Nat Genet. 2018;50(12):1642-1649. PubMed, CrossRef
  18. MacAlpine DM, Perlman PS, Butow RA. The high mobility group protein Abf2p influences the level of yeast mitochondrial DNA recombination intermediates in vivo. Proc Natl Acad Sci USA. 1998;95(12):6739-6743. PubMed, PubMed, CrossRef
  19. Kukat C, Wurm CA, Spåhr H, Falkenberg M, Larsson NG, Jakobs S. Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA. Proc Natl Acad Sci USA. 2011;108(33):13534-13539. PubMed, PubMed, CrossRef
  20. Copeland WC, Longley MJ. Mitochondrial genome maintenance in health and disease. DNA Repair (Amst). 2014;19:190-198. PubMed, PubMed, CrossRef
  21. Jiang M, Xie X, Zhu X, Jiang S, Milenkovic D, Misic J, Shi Y, Tandukar N, Li X, Atanassov I, Jenninger L, Hoberg E, Albarran-Gutierrez S, Szilagyi Z, Macao B, Siira SJ, Carelli V, Griffith JD, Gustafsson CM, Nicholls TJ, Filipovska A, Larsson NG, Falkenberg M. The mitochondrial single-stranded DNA binding protein is essential for initiation of mtDNA replication. Sci Adv. 2021;7(27):eabf8631. PubMed, PubMed, CrossRef
  22. Longley MJ, Clark S, Yu Wai Man C, Hudson G, Durham SE, Taylor RW, Nightingale S, Turnbull DM, Copeland WC, Chinnery PF. Mutant POLG2 disrupts DNA polymerase gamma subunits and causes progressive external ophthalmoplegia. Am J Hum Genet. 2006;78(6):1026-1034. PubMed, PubMed, CrossRef
  23. Rahman S, Copeland WC. POLG-related disorders and their neurological manifestations. Nat Rev Neurol. 2019;15(1):40-52. PubMed, PubMed, CrossRef
  24.  Xu Y, Shen J, Ran Z. Emerging views of mitophagy in immunity and autoimmune diseases. Autophagy. 2020;16(1):3-17. PubMed, PubMed, CrossRef
  25. Geisler S, Holmström KM, Skujat D, Fiesel FC, Rothfuss OC, Kahle PJ, Springer W. PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat Cell Biol. 2010;12(2):119-131. PubMed, CrossRef
  26. Matsuda N, Sato S, Shiba K, Okatsu K, Saisho K, Gautier CA, Sou YS, Saiki S, Kawajiri S, Sato F, Kimura M, Komatsu M, Hattori N, Tanaka K. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J Cell Biol. 2010;189(2):211-221. PubMed, PubMed, CrossRef
  27. Jin SM, Lazarou M, Wang C, Kane LA, Narendra DP, Youle RJ. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J Cell Biol. 2010;191(5):933-942. PubMed, PubMed, CrossRef
  28. Narendra D, Tanaka A, Suen DF, Youle RJ. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol. 2008;183(5):795-803. PubMed, PubMed, CrossRef
  29. Gegg ME, Cooper JM, Chau KY, Rojo M, Schapira AH, Taanman JW. Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum Mol Genet. 2010;19(24):4861-4870. PubMed, PubMed, CrossRef
  30. Pankiv S, Clausen TH, Lamark T, Brech A, Bruun JA, Outzen H, Øvervatn A, Bjørkøy G, Johansen T. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem. 2007;282(33):24131-24145. PubMed, CrossRef
  31. Tian X, Teng J, Chen J. New insights regarding SNARE proteins in autophagosome-lysosome fusion. Autophagy. 2021;17(10):2680-2688. PubMed, PubMed, CrossRef
  32. Nishimura T, Tooze SA. Emerging roles of ATG proteins and membrane lipids in autophagosome formation. Cell Discov. 2020;6(1):32. PubMed, PubMed, CrossRef
  33. Oshima Y, Cartier E, Boyman L, Verhoeven N, Polster BM, Huang W, Kane M, Lederer WJ, Karbowski M. Parkin-independent mitophagy via Drp1-mediated outer membrane severing and inner membrane ubiquitination. J Cell Biol. 2021;220(6):e202006043. PubMed, PubMed, CrossRef
  34. Yamada T, Murata D, Adachi Y, Itoh K, Kameoka S, Igarashi A, Kato T, Araki Y, Huganir RL, Dawson TM, Yanagawa T, Okamoto K, Iijima M, Sesaki H. Mitochondrial Stasis Reveals p62-Mediated Ubiquitination in Parkin-Independent Mitophagy and Mitigates Nonalcoholic Fatty Liver Disease. Cell Metab. 2018;28(4):588-604.e5. PubMed, PubMed, CrossRef
  35. Dorn GW 2nd. Mitochondrial pruning by Nix and BNip3: an essential function for cardiac-expressed death factors. J Cardiovasc Transl Res. 2010;3(4):374-383. PubMed, PubMed, CrossRef
  36. Sulkshane P, Ram J, Thakur A, Reis N, Kleifeld O, Glickman MH. Ubiquitination and receptor-mediated mitophagy converge to eliminate oxidation-damaged mitochondria during hypoxia. Redox Biol. 2021;45:102047. PubMed, PubMed, CrossRef
  37. Rotko D, Kunz WS, Szewczyk A, Kulawiak B. Signaling pathways targeting mitochondrial potassium channels. Int J Biochem Cell Biol. 2020;125:105792. PubMed, CrossRef
  38. Walkon LL, Strubbe-Rivera JO, Bazil JN. Calcium Overload and Mitochondrial Metabolism. Biomolecules. 2022;12(12):1891.
    PubMed, PubMed, CrossRef
  39. Del Arco A, Contreras L, Pardo B, Satrustegui J. Calcium regulation of mitochondrial carriers. Biochim Biophys Acta. 2016;1863(10):2413-2421. PubMed, CrossRef
  40. Gherardi G, Monticelli H, Rizzuto R, Mammucari C. The Mitochondrial Ca2+ Uptake and the Fine-Tuning of Aerobic Metabolism. Front Physiol. 2020;11:554904. PubMed, PubMed, CrossRef
  41. Glancy B, Balaban RS. Role of mitochondrial Ca2+ in the regulation of cellular energetics. Biochemistry. 2012;51(14):2959-2973. PubMed, PubMed, CrossRef
  42. Ahmadian M, Suh JM, Hah N, Liddle C, Atkins AR, Downes M, Evans RM. PPARγ signaling and metabolism: the good, the bad and the future. Nat Med. 2013;19(5):557-566. PubMed, PubMed, CrossRef
  43. Christofides A, Konstantinidou E, Jani C, Boussiotis VA. The role of peroxisome proliferator-activated receptors (PPAR) in immune responses. Metabolism. 2021;114:154338. PubMed, PubMed, CrossRef
  44. Wrutniak-Cabello C, Casas F, Cabello G. Thyroid hormone action in mitochondria. J Mol Endocrinol. 2001;26(1):67-77. PubMed, CrossRef
  45. Marín-García J. Thyroid hormone and myocardial mitochondrial biogenesis. Vascul Pharmacol. 2010;52(3-4):120-130. PubMed, CrossRef
  46. Yu G, Tzouvelekis A, Wang R, Herazo-Maya JD, Ibarra GH, Srivastava A, de Castro JPW, DeIuliis G, Ahangari F, Woolard T, Aurelien N, Arrojo E Drigo R, Gan Y, Graham M, Liu X, Homer RJ, Scanlan TS, Mannam P, Lee PJ, Herzog EL, Bianco AC, Kaminski N. Thyroid hormone inhibits lung fibrosis in mice by improving epithelial mitochondrial function. Nat Med. 2018;24(1):39-49. PubMed, PubMed, CrossRef
  47. Nakamura MT, Yudell BE, Loor JJ. Regulation of energy metabolism by long-chain fatty acids. Prog Lipid Res. 2014;53:124-144. PubMed, CrossRef
  48. Wu M, Melichian DS, Chang E, Warner-Blankenship M, Ghosh AK, Varga J. Rosiglitazone abrogates bleomycin-induced scleroderma and blocks profibrotic responses through peroxisome proliferator-activated receptor-gamma. Am J Pathol. 2009;174(2):519-533. PubMed, PubMed, CrossRef
  49. Barish GD, Narkar VA, Evans RM. PPAR delta: a dagger in the heart of the metabolic syndrome. J Clin Invest. 2006;116(3):590-597. PubMed, PubMed, CrossRef
  50. Vega RB, Huss JM, Kelly DP. The coactivator PGC-1 cooperates with peroxisome proliferator-activated receptor alpha in transcriptional control of nuclear genes encoding mitochondrial fatty acid oxidation enzymes. Mol Cell Biol. 2000;20(5):1868-1876. PubMed, PubMed, CrossRef
  51. Tanaka T, Yamamoto J, Iwasaki S, Asaba H, Hamura H, Ikeda Y, Watanabe M, Magoori K, Ioka RX, Tachibana K, Watanabe Y, Uchiyama Y, Sumi K, Iguchi H, Ito S, Doi T, Hamakubo T, Naito M, Auwerx J, Yanagisawa M, Kodama T, Sakai J. Activation of peroxisome proliferator-activated receptor delta induces fatty acid beta-oxidation in skeletal muscle and attenuates metabolic syndrome. Proc Natl Acad Sci USA. 2003;100(26):15924-15929. PubMed, PubMed, CrossRef
  52. Luquet S, Lopez-Soriano J, Holst D, Fredenrich A, Melki J, Rassoulzadegan M, Grimaldi PA. Peroxisome proliferator-activated receptor delta controls muscle development and oxidative capability. FASEB J. 2003;17(15):2299-2301. PubMed, CrossRef
  53. Puigserver P, Wu Z, Park CW, Graves R, Wright M, Spiegelman BM. A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell. 1998;92(6):829-839. PubMed, CrossRef
  54. Andersson U, Scarpulla RC. Pgc-1-related coactivator, a novel, serum-inducible coactivator of nuclear respiratory factor 1-dependent transcription in mammalian cells. Mol Cell Biol. 2001;21(11):3738-3749. PubMed, PubMed, CrossRef
  55. Jornayvaz FR, Shulman GI. Regulation of mitochondrial biogenesis. Essays Biochem. 2010;47:69-84. PubMed, PubMed, CrossRef
  56. Jamwal S, Blackburn JK, Elsworth JD. PPARγ/PGC1α signaling as a potential therapeutic target for mitochondrial biogenesis in neurodegenerative disorders. Pharmacol Ther. 2021;219:107705. PubMed, PubMed, CrossRef
  57. Gureev AP, Shaforostova EA, Popov VN. Regulation of Mitochondrial Biogenesis as a Way for Active Longevity: Interaction Between the Nrf2 and PGC-1α Signaling Pathways. Front Genet. 2019;10:435. PubMed, PubMed, CrossRef
  58. Herzig S, Shaw RJ. AMPK: guardian of metabolism and mitochondrial homeostasis. Nat Rev Mol Cell Biol. 2018;19(2):121-135. PubMed, PubMed, CrossRef
  59. Longo VD, Kennedy BK. Sirtuins in aging and age-related disease. Cell. 2006;126(2):257-268. PubMed, CrossRef
  60. Haigis MC, Guarente LP. Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction. Genes Dev. 2006;20(21):2913-2921. PubMed, CrossRef
  61. Schwer B, North BJ, Frye RA, Ott M, Verdin E. The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J Cell Biol. 2002;158(4):647-657. PubMed, PubMed, CrossRef
  62. Onyango P, Celic I, McCaffery JM, Boeke JD, Feinberg AP. SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria. Proc Natl Acad Sci USA. 2002;99(21):13653-13658. PubMed, PubMed, CrossRef
  63. Scher MB, Vaquero A, Reinberg D. SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev. 2007;21(8):920-928. PubMed, PubMed, CrossRef
  64. Wang S, Wan T, Ye M, Qiu Y, Pei L, Jiang R, Pang N, Huang Y, Liang B, Ling W, Lin X, Zhang Z, Yang L. Nicotinamide riboside attenuates alcohol induced liver injuries via activation of SirT1/PGC-1α/mitochondrial biosynthesis pathway. Redox Biol. 2018;17:89-98. PubMed, PubMed, CrossRef
  65. Yao J, Wang J, Xu Y, Guo Q, Sun Y, Liu J, Li S, Guo Y, Wei L. CDK9 inhibition blocks the initiation of PINK1-PRKN-mediated mitophagy by regulating the SIRT1-FOXO3-BNIP3 axis and enhances the therapeutic effects involving mitochondrial dysfunction in hepatocellular carcinoma. Autophagy. 2022;18(8):1879-1897. PubMed, PubMed, CrossRef
  66. Wang R, Xu H, Tan B, Yi Q, Sun Y, Xiang H, Chen T, Liu H, Xie Q, Wang L, Tian J, Zhu J. SIRT3 promotes metabolic maturation of human iPSC-derived cardiomyocytes via OPA1-controlled mitochondrial dynamics. Free Radic Biol Med. 2023;195:270-282. PubMed, CrossRef
  67. Polletta L, Vernucci E, Carnevale I, Arcangeli T, Rotili D, Palmerio S, Steegborn C, Nowak T, Schutkowski M, Pellegrini L, Sansone L, Villanova L, Runci A, Pucci B, Morgante E, Fini M, Mai A, Russo MA, Tafani M. SIRT5 regulation of ammonia-induced autophagy and mitophagy. Autophagy. 2015;11(2):253-270. PubMed, PubMed, CrossRef
  68. Pei S, Minhajuddin M, Adane B, Khan N, Stevens BM, Mack SC, Lai S, Rich JN, Inguva A, Shannon KM, Kim H, Tan AC, Myers JR, Ashton JM, Neff T, Pollyea DA, Smith CA, Jordan CT. AMPK/FIS1-Mediated Mitophagy Is Required for Self-Renewal of Human AML Stem Cells. Cell Stem Cell. 2018;23(1):86-100.e6. PubMed, PubMed, CrossRef
  69. Yang Y, Ouyang Y, Yang L, Beal MF, McQuibban A, Vogel H, Lu B. Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery. Proc Natl Acad Sci USA. 2008;105(19):7070-7075. PubMed, PubMed, CrossRef
  70. Wullschleger S, Loewith R, Hall MN. TOR signaling in growth and metabolism. Cell. 2006;124(3):471-484. PubMed, CrossRef
  71. Fulda S. Synthetic lethality by co-targeting mitochondrial apoptosis and PI3K/Akt/mTOR signaling. Mitochondrion. 2014;19(Pt A):85-87. PubMed, CrossRef
  72. Shirane-Kitsuji M, Nakayama KI. Mitochondria: FKBP38 and mitochondrial degradation. Int J Biochem Cell Biol. 2014;51:19-22. PubMed, CrossRef
  73. Inoki K, Zhu T, Guan KL. TSC2 mediates cellular energy response to control cell growth and survival. Cell. 2003;115(5):577-590. PubMed, CrossRef
  74. Appenzeller-Herzog C, Hall MN. Bidirectional crosstalk between endoplasmic reticulum stress and mTOR signaling. Trends Cell Biol. 2012;22(5):274-282. PubMed, CrossRef
  75. Auger JP, Zimmermann M, Faas M, Stifel U, Chambers D, Krishnacoumar B, Taudte RV, Grund C, Erdmann G, Scholtysek C, Uderhardt S, Ben Brahim O, Pascual Maté M, Stoll C, Böttcher M, Palumbo-Zerr K, Mangan MSJ, Dzamukova M, Kieler M, Hofmann M, Blüml S, Schabbauer G, Mougiakakos D, Sonnewald U, Hartmann F, Simon D, Kleyer A, Grüneboom A, Finotto S, Latz E, Hofmann J, Schett G, Tuckermann J, Krönke G. Metabolic rewiring promotes anti-inflammatory effects of glucocorticoids. Nature. 2024;629(8010):184-192. PubMed, CrossRef
  76. Psarra AM, Sekeris CE. Steroid and thyroid hormone receptors in mitochondria. IUBMB Life. 2008;60(4):210-223. PubMed, CrossRef
  77. Zhong C, Mai Y, Gao H, Zhou W, Zhou D. Mitochondrial targeting of TR3 is involved in TPA induced apoptosis in breast cancer cells. Gene. 2019;693:61-68. PubMed, CrossRef
  78. Goffart S, Wiesner RJ. Regulation and co-ordination of nuclear gene expression during mitochondrial biogenesis. Exp Physiol. 2003;88(1):33-40. PubMed, CrossRef
  79. Wakabayashi T. Wakabayashi T. Structural changes of mitochondria related to apoptosis: swelling and megamitochondria formation. Acta Biochim Pol. 1999;46(2):223-237. PubMed
  80. Karbowski M, Kurono C, Wozniak M, Ostrowski M, Teranishi M, Nishizawa Y, Usukura J, Soji T, Wakabayashi T. Free radical-induced megamitochondria formation and apoptosis. Free Radic Biol Med. 1999;26(3-4):396-409. PubMed, CrossRef
  81. Wakabayashi T. Megamitochondria formation – physiology and pathology. J Cell Mol Med. 2002;6(4):497-538. PubMed, PubMed, CrossRef
  82. Shang Y, Li Z, Cai P, Li W, Xu Y, Zhao Y, Xia S, Shao Q, Wang H. Megamitochondria plasticity: Function transition from adaption to disease. Mitochondrion. 2023;71:64-75. PubMed, CrossRef
  83. Nakahira K, Haspel JA, Rathinam VA, Lee SJ, Dolinay T, Lam HC, Englert JA, Rabinovitch M, Cernadas M, Kim HP, Fitzgerald KA, Ryter SW, Choi AM. Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat Immunol. 2011;12(3):222-230. PubMed, PubMed, CrossRef
  84. Sun Q, Sun L, Liu HH, Chen X, Seth RB, Forman J, Chen ZJ. The specific and essential role of MAVS in antiviral innate immune responses. Immunity. 2006;24(5):633-642. PubMed, CrossRef
  85. Vazquez C, Horner SM. MAVS Coordination of Antiviral Innate Immunity. J Virol. 2015;89(14):6974-6977. PubMed, PubMed, CrossRef
  86. Lamkanfi M, Dixit VM. Mechanisms and functions of inflammasomes. Cell. 2014;157(5):1013-1022. PubMed, CrossRef
  87. Martinon F, Burns K, Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell. 2002;10(2):417-426. PubMed, CrossRef
  88. Kayagaki N, Warming S, Lamkanfi M, Vande Walle L, Louie S, Dong J, Newton K, Qu Y, Liu J, Heldens S, Zhang J, Lee WP, Roose-Girma M, Dixit VM. Non-canonical inflammasome activation targets caspase-11. Nature. 2011;479(7371):117-121. PubMed, CrossRef
  89.  Kayagaki N, Stowe IB, Lee BL, O’Rourke K, Anderson K, Warming S, Cuellar T, Haley B, Roose-Girma M, Phung QT, Liu PS, Lill JR, Li H, Wu J, Kummerfeld S, Zhang J, Lee WP, Snipas SJ, Salvesen GS, Morris LX, Fitzgerald L, Zhang Y, Bertram EM, Goodnow CC, Dixit VM. Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature. 2015;526(7575):666-671. PubMed, CrossRef
  90. Yang H, Wang H, Ren J, Chen Q, Chen ZJ. cGAS is essential for cellular senescence. Proc Natl Acad Sci USA. 2017;114(23):E4612-E4620. PubMed, PubMed, CrossRef
  91. Watson RO, Bell SL, MacDuff DA, Kimmey JM, Diner EJ, Olivas J, Vance RE, Stallings CL, Virgin HW, Cox JS. The Cytosolic Sensor cGAS Detects Mycobacterium tuberculosis DNA to Induce Type I Interferons and Activate Autophagy. Cell Host Microbe. 2015;17(6):811-819. PubMed, PubMed, CrossRef
  92. Soucy-Faulkner A, Mukawera E, Fink K, Martel A, Jouan L, Nzengue Y, Lamarre D, Vande Velde C, Grandvaux N. Requirement of NOX2 and reactive oxygen species for efficient RIG-I-mediated antiviral response through regulation of MAVS expression. PLoS Pathog. 2010;6(6):e1000930. PubMed, PubMed, CrossRef
  93. Hou P, Wang X, Wang H, Wang T, Yu Z, Xu C, Zhao Y, Wang W, Zhao Y, Chu F, Chang H, Zhu H, Lu J, Zhang F, Liang X, Li X, Wang S, Gao Y, He H. The ORF7a protein of SARS-CoV-2 initiates autophagy and limits autophagosome-lysosome fusion via degradation of SNAP29 to promote virus replication. Autophagy. 2023;19(2):551-569. PubMed, PubMed, CrossRef
  94. Mozzi A, Oldani M, Forcella ME, Vantaggiato C, Cappelletti G, Pontremoli C, Valenti F, Forni D, Saresella M, Biasin M, Sironi M, Fusi P, Cagliani R. SARS-CoV-2 ORF3c impairs mitochondrial respiratory metabolism, oxidative stress, and autophagic flux. iScience. 2023;26(7):107118. PubMed, PubMed, CrossRef
  95. Li X, Hou P, Ma W, Wang X, Wang H, Yu Z, Chang H, Wang T, Jin S, Wang X, Wang W, Zhao Y, Zhao Y, Xu C, Ma X, Gao Y, He H. SARS-CoV-2 ORF10 suppresses the antiviral innate immune response by degrading MAVS through mitophagy. Cell Mol Immunol. 2022;19(1):67-78. PubMed, PubMed, CrossRef
  96. Wu KE, Fazal FM, Parker KR, Zou J, Chang HY. RNA-GPS Predicts SARS-CoV-2 RNA Residency to Host Mitochondria and Nucleolus. Cell Syst. 2020;11(1):102-108.e3. PubMed, PubMed, CrossRef
  97. Stukalov A, Girault V, Grass V, Karayel O, Bergant V, Urban C, Haas DA, Huang Y, Oubraham L, Wang A, Hamad MS, Piras A, Hansen FM, Tanzer MC, Paron I, Zinzula L, Engleitner T, Reinecke M, Lavacca TM, Ehmann R, Wölfel R, Jores J, Kuster B, Protzer U, Rad R, Ziebuhr J, Thiel V, Scaturro P, Mann M, Pichlmair A. Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV. Nature. 2021;594(7862):246-252. PubMed, CrossRef
  98. Shang C, Liu Z, Zhu Y, Lu J, Ge C, Zhang C, Li N, Jin N, Li Y, Tian M, Li X. SARS-CoV-2 Causes Mitochondrial Dysfunction and Mitophagy Impairment. Front Microbiol. 2022;12:780768. PubMed, PubMed, CrossRef
  99. Roden AC, Boland JM, Johnson TF, Aubry MC, Lo YC, Butt YM, Maleszewski JJ, Larsen BT, Tazelaar HD, Khoor A, Smith ML, Moua T, Jenkins SM, Moyer AM, Yi ES, Bois MC. Late Complications of COVID-19: A Morphologic, Imaging, and Droplet Digital Polymerase Chain Reaction Study of Lung Tissue. Arch Pathol Lab Med. 2022;146(7):791-804. PubMed, CrossRef
  100. Zollner A, Koch R, Jukic A, Pfister A, Meyer M, Rössler A, Kimpel J, Adolph TE, Tilg H. Postacute COVID-19 is Characterized by Gut Viral Antigen Persistence in Inflammatory Bowel Diseases. Gastroenterology. 2022;163(2):495-506.e8. PubMed, PubMed, CrossRef
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