Bioenergetic roles of mitochondrial fusion

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1857, Issue 8, 2016, Pages 1277-1283

  Silva Ramos, Eduardo ^a   Larsson, Nils Göran ^a,b   Mourier, Arnaud ^a,c,d  

^a MAX PLANCK INSTITUTE FOR BIOLOGY OF AGEING   (Germany)

^b KAROLINSKA INSTITUTE   (Sweden)

^c UNIVERSITÉ DE BORDEAUX   (France)

^d Institut de Biochimie et Genetique Cellulaires   (France)

Author keywords

Bioenergetics; Coenzyme Q; Mevalonate pathway; Mitochondrial dynamics; Mitofusin 2

Indexed keywords

MEVALONIC ACID; MITOCHONDRIAL DNA; MITOFUSIN 2; UBIQUINONE; EYE PROTEIN; G PROTEIN COUPLED RECEPTOR; GPR143 PROTEIN, MOUSE; GUANOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; MFN1 PROTEIN, MOUSE; MFN2 PROTEIN, MOUSE;

ANIMAL CELL; ARTICLE; BIOENERGY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; EMBRYO; ENZYME SYNTHESIS; GROWTH CURVE; IN VITRO STUDY; MITOCHONDRIAL DYNAMICS; MITOCHONDRIAL GENOME; MITOCHONDRIAL RESPIRATION; MITOCHONDRION; MOUSE; NONHUMAN; PRIORITY JOURNAL; ANIMAL; CYTOLOGY; DEFICIENCY; DRUG EFFECTS; FIBROBLAST; GENE EXPRESSION; GENETICS; KNOCKOUT MOUSE; METABOLISM; OXIDATIVE PHOSPHORYLATION; TRANSFORMED CELL LINE;

ANIMALS; CELL LINE, TRANSFORMED; EYE PROTEINS; FIBROBLASTS; GENE EXPRESSION; GENOME, MITOCHONDRIAL; GTP PHOSPHOHYDROLASES; MEMBRANE GLYCOPROTEINS; MEVALONIC ACID; MICE; MICE, KNOCKOUT; MITOCHONDRIA; MITOCHONDRIAL DYNAMICS; OXIDATIVE PHOSPHORYLATION; RECEPTORS, G-PROTEIN-COUPLED; UBIQUINONE;

EID: 84964264864     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2016.04.002     Document Type: Article

References (139)

1. [1] Benda, C., Ueber die Spermatogenese der Vertebraten und höherer Evertebraten, II. Theil: Die Histiogenese der Spermien. Arch. Anat. Physiol. 73 (1898), 393–398.
2. [2] Gilkerson, R.W., Selker, J.M.L., Capaldi, R.A., The cristal membrane of mitochondria is the principal site of oxidative phosphorylation. FEBS Lett. 546 (2003), 355–358.
3. [3] Appelhans, T., Richter, C.P., Wilkens, V., Hess, S.T., Piehler, J., Busch, K.B., Nanoscale organization of mitochondrial microcompartments revealed by combining tracking and localization microscopy. Nano Lett. 12 (2012), 610–616, 10.1021/nl203343a.
4. [4] Busch, K.B., Deckers-Hebestreit, G., Hanke, G.T., Mulkidjanian, A.Y., Dynamics of bioenergetic microcompartments. Biol. Chem. 394 (2013), 163–188, 10.1515/hsz-2012-0254.
5. [5] Mitchell, P., Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191 (1961), 144–148.
6. [6] Falkenberg, M., Larsson, N.-G., Gustafsson, C.M., DNA replication and transcription in mammalian mitochondria. Annu. Rev. Biochem. 76 (2007), 679–699, 10.1146/annurev.biochem.76.060305.152028.
7. [7] Rorbach, J., Soleimanpour-Lichaei, R., Lightowlers, R.N., Chrzanowska-Lightowlers, Z.M.A., How do mammalian mitochondria synthesize proteins?. Biochem. Soc. Trans. 35 (2007), 1290–1291, 10.1042/BST0351290.
8. [8] Bolender, N., Sickmann, A., Wagner, R., Meisinger, C., Pfanner, N., Multiple pathways for sorting mitochondrial precursor proteins. EMBO Rep. 9 (2008), 42–49, 10.1038/sj.embor.7401126.
9. [9] Tatsuta, T., Langer, T., Quality control of mitochondria: protection against neurodegeneration and ageing. EMBO J. 27 (2008), 306–314, 10.1038/sj.emboj.7601972.
10. [10] Lill, R., Mühlenhoff, U., Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 77 (2008), 669–700, 10.1146/annurev.biochem.76.052705.162653.
11. [11] Koning, A.J., Lum, P.Y., Williams, J.M., Wright, R., DiOC6 staining reveals organelle structure and dynamics in living yeast cells. Cell Motil. Cytoskeleton 25 (1993), 111–128, 10.1002/cm.970250202.
12. [12] Bereiter-Hahn, J., Vöth, M., Dynamics of mitochondria in living cells: shape changes, dislocations, fusion, and fission of mitochondria. Microsc. Res. Tech. 27 (1994), 198–219, 10.1002/jemt.1070270303.
13. [13] Chen, H., Detmer, S.A., Ewald, A.J., Griffin, E.E., Fraser, S.E., Chan, D.C., Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 160 (2003), 189–200, 10.1083/jcb.200211046.
14. [14] Hales, K.G., Fuller, M.T., Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase. Cell 90 (1997), 121–129.
15. [15] Hermann, G.J., Shaw, J.M., Mitochondrial dynamics in yeast. Annu. Rev. Cell Dev. Biol. 14 (1998), 265–303, 10.1146/annurev.cellbio.14.1.265.
16. [16] Rapaport, D., Brunner, M., Neupert, W., Westermann, B., Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998), 20150–20155.
17. [17] Okamoto, K., Shaw, J.M., Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu. Rev. Genet. 39 (2005), 503–536, 10.1146/annurev.genet.38.072902.093019.
18. [18] Wong, E.D., Wagner, J.A., Gorsich, S.W., McCaffery, J.M., Shaw, J.M., Nunnari, J., The dynamin-related GTPase, Mgm1p, is an intermembrane space protein required for maintenance of fusion competent mitochondria. J. Cell Biol. 151 (2000), 341–352.
19. [19] Herlan, M., Vogel, F., Bornhövd, C., Neupert, W., Reichert, A.S., Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA. J. Biol. Chem. 278 (2003), 27781–27788, 10.1074/jbc.M211311200.
20. [20] Griparic, L., van der Wel, N.N., Orozco, I.J., Peters, P.J., van der Bliek, A.M., Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria. J. Biol. Chem. 279 (2004), 18792–18798, 10.1074/jbc.M400920200.
21. [21] Sesaki, H., Jensen, R.E., UGO1 encodes an outer membrane protein required for mitochondrial fusion. J. Cell Biol. 152 (2001), 1123–1134.
22. [22] Sesaki, H., Jensen, R.E., Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion. J. Biol. Chem. 279 (2004), 28298–28303, 10.1074/jbc.M401363200.
23. [23] Coonrod, E.M., Karren, M.A., Shaw, J.M., Ugo1p is a multipass transmembrane protein with a single carrier domain required for mitochondrial fusion. Traffic (Copenhagen, Denmark) 8 (2007), 500–511, 10.1111/j.1600-0854.2007.00550.x.
24. [24] Santel, A., Fuller, M.T., Control of mitochondrial morphology by a human mitofusin. J. Cell Sci. 114 (2001), 867–874.
25. [25] Santel, A., Frank, S., Gaume, B., Herrler, M., Youle, R.J., Fuller, M.T., Mitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells. J. Cell Sci. 116 (2003), 2763–2774, 10.1242/jcs.00479.
26. [26] Rojo, M., Legros, F., Chateau, D., Lombès, A., Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo. J. Cell Sci. 115 (2002), 1663–1674.
27. [27] Eura, Y., Ishihara, N., Yokota, S., Mihara, K., Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion. J. Biochem. 134 (2003), 333–344.
28. [28] Debattisti, V., Pendin, D., Ziviani, E., Daga, A., Scorrano, L., Reduction of endoplasmic reticulum stress attenuates the defects caused by Drosophila mitofusin depletion. J. Cell Biol. 204 (2014), 303–312, 10.1083/jcb.201306121.
29. [29] Hwa, J.J., Hiller, M.A., Fuller, M.T., Santel, A., Differential expression of the Drosophila mitofusin genes fuzzy onions (fzo) and dmfn. Mech. Dev. 116 (2002), 213–216.
30. [30] Delettre, C., Lenaers, G., Griffoin, J.M., Gigarel, N., Lorenzo, C., Belenguer, P., et al. Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy. Nat. Genet. 26 (2000), 207–210, 10.1038/79936.
31. [31] Alexander, C., Votruba, M., Pesch, U.E., Thiselton, D.L., Mayer, S., Moore, A., et al. OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. Nat. Genet. 26 (2000), 211–215, 10.1038/79944.
32. [32] Cogliati, S., Frezza, C., Soriano, M.E., Varanita, T., Quintana-Cabrera, R., Corrado, M., et al. Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency. Cell 155 (2013), 160–171, 10.1016/j.cell.2013.08.032.
33. [33] Varanita, T., Soriano, M.E., Romanello, V., Zaglia, T., Quintana-Cabrera, R., Semenzato, M., et al. The OPA1-dependent mitochondrial cristae remodeling pathway controls atrophic, apoptotic, and ischemic tissue damage. Cell Metab. 21 (2015), 834–844, 10.1016/j.cmet.2015.05.007.
34. [34] Civiletto, G., Varanita, T., Cerutti, R., Gorletta, T., Barbaro, S., Marchet, S., et al. Opa1 overexpression ameliorates the phenotype of two mitochondrial disease mouse models. Cell Metab. 21 (2015), 845–854, 10.1016/j.cmet.2015.04.016.
35. [35] Patten, D.A., Wong, J., Khacho, M., Soubannier, V., Mailloux, R.J., Pilon-Larose, K., et al. OPA1-dependent cristae modulation is essential for cellular adaptation to metabolic demand. EMBO J. 33 (2014), 2676–2691, 10.15252/embj.201488349.
36. [36] Olichon, A., Emorine, L.J., Descoins, E., Pelloquin, L., Brichese, L., Gas, N., et al. The human dynamin-related protein OPA1 is anchored to the mitochondrial inner membrane facing the inter-membrane space. FEBS Lett. 523 (2002), 171–176.
37. [37] Ehses, S., Raschke, I., Mancuso, G., Bernacchia, A., Geimer, S., Tondera, D., et al. Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1. J. Cell Biol. 187 (2009), 1023–1036, 10.1083/jcb.200906084.
38. [38] Head, B., Griparic, L., Amiri, M., Gandre-Babbe, S., van der Bliek, A.M., Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells. J. Cell Biol. 187 (2009), 959–966, 10.1083/jcb.200906083.
39. [39] Griparic, L., Kanazawa, T., van der Bliek, A.M., Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage. J. Cell Biol. 178 (2007), 757–764, 10.1083/jcb.200704112.
40. [40] Song, Z., Chen, H., Fiket, M., Alexander, C., Chan, D.C., OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. J. Cell Biol. 178 (2007), 749–755, 10.1083/jcb.200704110.
41. [41] Anand, R., Wai, T., Baker, M.J., Kladt, N., Schauss, A.C., Rugarli, E., et al. The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission. J. Cell Biol. 204 (2014), 919–929, 10.1083/jcb.201308006.
42. [42] Otsuga, D., Keegan, B.R., Brisch, E., Thatcher, J.W., Hermann, G.J., Bleazard, W., et al. The dynamin-related GTPase, Dnm1p, controls mitochondrial morphology in yeast. J. Cell Biol. 143 (1998), 333–349.
43. [43] Bleazard, W., McCaffery, J.M., King, E.J., Bale, S., Mozdy, A., Tieu, Q., et al. The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast. Nat. Cell Biol. 1 (1999), 298–304, 10.1038/13014.
44. [44] Mozdy, A.D., McCaffery, J.M., Shaw, J.M., Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol. 151 (2000), 367–380.
45. [45] Tieu, Q., Nunnari, J., Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division. J. Cell Biol. 151 (2000), 353–366.
46. [46] Cerveny, K.L., McCaffery, J.M., Jensen, R.E., Division of mitochondria requires a novel DMN1-interacting protein, Net2p. Mol. Biol. Cell 12 (2001), 309–321.
47. [47] Tieu, Q., Okreglak, V., Naylor, K., Nunnari, J., The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission. J. Cell Biol. 158 (2002), 445–452, 10.1083/jcb.200205031.
48. [48] Cerveny, K.L., Jensen, R.E., The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division of mitochondria. Mol. Biol. Cell 14 (2003), 4126–4139, 10.1091/mbc.E03-02-0092.
49. [49] Karren, M.A., Coonrod, E.M., Anderson, T.K., Shaw, J.M., The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly. J. Cell Biol. 171 (2005), 291–301, 10.1083/jcb.200506158.
50. [50] Naylor, K., Ingerman, E., Okreglak, V., Marino, M., Hinshaw, J.E., Nunnari, J., Mdv1 interacts with assembled dnm1 to promote mitochondrial division. J. Biol. Chem. 281 (2006), 2177–2183, 10.1074/jbc.M507943200.
51. [51] Schauss, A.C., Bewersdorf, J., Jakobs, S., Fis1p and Caf4p, but not Mdv1p, determine the polar localization of Dnm1p clusters on the mitochondrial surface. J. Cell Sci. 119 (2006), 3098–3106, 10.1242/jcs.03026.
52. [52] Guo, Q., Koirala, S., Perkins, E.M., McCaffery, J.M., Shaw, J.M., The mitochondrial fission adaptors Caf4 and Mdv1 are not functionally equivalent. PLoS One, 7, 2012, e53523, 10.1371/journal.pone.0053523.
53. [53] Ingerman, E., Perkins, E.M., Marino, M., Mears, J.A., McCaffery, J.M., Hinshaw, J.E., et al. Dnm1 forms spirals that are structurally tailored to fit mitochondria. J. Cell Biol. 170 (2005), 1021–1027, 10.1083/jcb.200506078.
54. [54] Mears, J.A., Lackner, L.L., Fang, S., Ingerman, E., Nunnari, J., Hinshaw, J.E., Conformational changes in Dnm1 support a contractile mechanism for mitochondrial fission. Nat. Struct. Mol. Biol. 18 (2011), 20–26, 10.1038/nsmb.1949.
55. [55] James, D.I., Parone, P.A., Mattenberger, Y., Martinou, J.C., hFis1, a novel component of the mammalian mitochondrial fission machinery. J. Biol. Chem. 278 (2003), 36373–36379, 10.1074/jbc.M303758200.
56. [56] Smirnova, E., Griparic, L., Shurland, D.L., van der Bliek, A.M., Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol. Biol. Cell 12 (2001), 2245–2256.
57. [57] Yoon, Y., Krueger, E.W., Oswald, B.J., McNiven, M.A., The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Mol. Cell. Biol. 23 (2003), 5409–5420.
58. [58] Roy, M., Reddy, P.H., Iijima, M., Sesaki, H., Mitochondrial division and fusion in metabolism. Curr. Opin. Cell Biol. 33 (2015), 111–118, 10.1016/j.ceb.2015.02.001.
59. [59] Bertholet, A.M., Delerue, T., Millet, A.M., Moulis, M.F., David, C., Daloyau, M., et al. Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity. Neurobiol. Dis., 2015, 10.1016/j.nbd.2015.10.011.
60. [60] Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., Mihara, K., Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission. J. Biol. Chem. 282 (2007), 11521–11529, 10.1074/jbc.M607279200.
61. [61] Cribbs, J.T., Strack, S., Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBO Rep. 8 (2007), 939–944, 10.1038/sj.embor.7401062.
62. [62] Chang, C.-R., Blackstone, C., Drp1 phosphorylation and mitochondrial regulation. EMBO Rep. 8 (2007), 1088–1089, 10.1038/sj.embor.7401118 (author reply 1089–90).
63. [63] Cereghetti, G.M., Stangherlin, A., Martins de Brito, O., Chang, C.R., Blackstone, C., Bernardi, P., et al. Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 15803–15808, 10.1073/pnas.0808249105.
64. [64] Cho, D.-H., Nakamura, T., Fang, J., Cieplak, P., Godzik, A., Gu, Z., et al. S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science (New York, N.Y.) 324 (2009), 102–105, 10.1126/science.1171091.
65. [65] Nakamura, T., Cieplak, P., Cho, D.-H., Godzik, A., Lipton, S.A., S-nitrosylation of Drp1 links excessive mitochondrial fission to neuronal injury in neurodegeneration. Mitochondrion 10 (2010), 573–578, 10.1016/j.mito.2010.04.007.
66. [66] Nakamura, N., Kimura, Y., Tokuda, M., Honda, S., Hirose, S., MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Rep. 7 (2006), 1019–1022, 10.1038/sj.embor.7400790.
67. [67] Karbowski, M., Neutzner, A., Youle, R.J., The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division. J. Cell Biol. 178 (2007), 71–84, 10.1083/jcb.200611064.
68. [68] Horn, S.R., Thomenius, M.J., Johnson, E.S., Freel, C.D., Wu, J.Q., Coloff, J.L., et al. Regulation of mitochondrial morphology by APC/CCdh1-mediated control of Drp1 stability. Mol. Biol. Cell 22 (2011), 1207–1216, 10.1091/mbc.E10-07-0567.
69. [69] Wasiak, S., Zunino, R., McBride, H.M., Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death. J. Cell Biol. 177 (2007), 439–450, 10.1083/jcb.200610042.
70. [70] Braschi, E., Zunino, R., McBride, H.M., MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission. EMBO Rep. 10 (2009), 748–754, 10.1038/embor.2009.86.
71. [71] Figueroa-Romero, C., Iñiguez-Lluhí, J.A., Stadler, J., Chang, C.-R., Arnoult, D., Keller, P.J., et al. SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle. FASEB J. 23 (2009), 3917–3927, 10.1096/fj.09-136630.
72. [72] Koch, A., Thiemann, M., Grabenbauer, M., Yoon, Y., McNiven, M.A., Schrader, M., Dynamin-like protein 1 is involved in peroxisomal fission. J. Biol. Chem. 278 (2003), 8597–8605, 10.1074/jbc.M211761200.
73. [73] Li, X., Gould, S.J., The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11. J. Biol. Chem. 278 (2003), 17012–17020, 10.1074/jbc.M212031200.
74. [74] Hyde, B.B., Twig, G., Shirihai, O.S., Organellar vs cellular control of mitochondrial dynamics. Semin. Cell Dev. Biol. 21 (2010), 575–581, 10.1016/j.semcdb.2010.01.003.
75. [75] Egner, A., Jakobs, S., Hell, S.W., Fast 100-nm resolution three-dimensional microscope reveals structural plasticity of mitochondria in live yeast. Proc. Natl. Acad. Sci. U. S. A. 99 (2002), 3370–3375, 10.1073/pnas.052545099.
76. [76] Jimenez, L., Laporte, D., Duvezin-Caubet, S., Courtout, F., Sagot, I., Mitochondrial ATP synthases cluster as discrete domains that reorganize with the cellular demand for oxidative phosphorylation. J. Cell Sci. 127 (2014), 719–726, 10.1242/jcs.137141.
77. [77] Rossignol, R., Gilkerson, R., Aggeler, R., Yamagata, K., Remington, S.J., Capaldi, R.A., Energy substrate modulates mitochondrial structure and oxidative capacity in cancer cells. Cancer Res. 64 (2004), 985–993.
78. [78] Mishra, P., Carelli, V., Manfredi, G., Chan, D.C., Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation. Cell Metab. 19 (2014), 630–641, 10.1016/j.cmet.2014.03.011.
79. [79] Gomes, L.C., Di Benedetto, G., Scorrano, L., During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat. Cell Biol. 13 (2011), 589–598, 10.1038/ncb2220.
80. [80] Rambold, A.S., Kostelecky, B., Elia, N., Lippincott-Schwartz, J., Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 10190–10195, 10.1073/pnas.1107402108.
81. [81] Frank, S., Gaume, B., Bergmann-Leitner, E.S., Leitner, W.W., Robert, E.G., Catez, F., et al. The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis. Dev. Cell 1 (2001), 515–525.
82. [82] Pyakurel, A., Savoia, C., Hess, D., Scorrano, L., Extracellular regulated kinase phosphorylates mitofusin 1 to control mitochondrial morphology and apoptosis. Mol. Cell 58 (2015), 244–254, 10.1016/j.molcel.2015.02.021.
83. [83] Karbowski, M., Norris, K.L., Cleland, M.M., Jeong, S.-Y., Youle, R.J., Role of Bax and Bak in mitochondrial morphogenesis. Nature 443 (2006), 658–662, 10.1038/nature05111.
84. [84] Cassidy-Stone, A., Chipuk, J.E., Ingerman, E., Song, C., Yoo, C., Kuwana, T., et al. Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization. Dev. Cell 14 (2008), 193–204, 10.1016/j.devcel.2007.11.019.
85. [85] Meeusen, S., McCaffery, J.M., Nunnari, J., Mitochondrial fusion intermediates revealed in vitro. Science (New York, N.Y.) 305 (2004), 1747–1752, 10.1126/science.1100612.
86. [86] Legros, F., Lombès, A., Frachon, P., Rojo, M., Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins. Mol. Biol. Cell 13 (2002), 4343–4354, 10.1091/mbc.E02-06-0330.
87. [87] Malka, F., Guillery, O., Cifuentes-Diaz, C., Guillou, E., Belenguer, P., Lombès, A., et al. Separate fusion of outer and inner mitochondrial membranes. EMBO Rep. 6 (2005), 853–859, 10.1038/sj.embor.7400488.
88. [88] Sauvanet, C., Duvezin-Caubet, S., di Rago, J.-P., Rojo, M., Energetic requirements and bioenergetic modulation of mitochondrial morphology and dynamics. Semin. Cell Dev. Biol. 21 (2010), 558–565, 10.1016/j.semcdb.2009.12.006.
89. [89] Guillery, O., Malka, F., Landes, T., Guillou, E., Blackstone, C., Lombès, A., et al. Metalloprotease-mediated OPA1 processing is modulated by the mitochondrial membrane potential. Biol. Cell. 100 (2008), 315–325, 10.1042/BC20070110.
90. [90] Rainbolt, T.K., Lebeau, J., Puchades, C., Wiseman, R.L., Reciprocal degradation of YME1L and OMA1 adapts mitochondrial proteolytic activity during stress. Cell Rep., 2016, 10.1016/j.celrep.2016.02.011.
91. [91] Karavaeva, I.E., Shekhireva, K.V., Severin, F.F., Knorre, D.A., Does mitochondrial fusion require transmembrane potential?. Biochem. Mosc. 80 (2015), 549–558, 10.1134/S0006297915050053.
92. [92] Benard, G., Bellance, N., James, D., Parrone, P., Fernandez, H., Letellier, T., et al. Mitochondrial bioenergetics and structural network organization. J. Cell Sci. 120 (2007), 838–848, 10.1242/jcs.03381.
93. [93] Duvezin-Caubet, S., Jagasia, R., Wagener, J., Hofmann, S., Trifunovic, A., Hansson, A., et al. Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology. J. Biol. Chem. 281 (2006), 37972–37979, 10.1074/jbc.M606059200.
94. [94] Yang, L., Long, Q., Liu, J., Tang, H., Li, Y., Bao, F., et al. Mitochondrial fusion provides an “initial metabolic complementation” controlled by mtDNA. Cell. Mol. Life Sci. 72 (2015), 2585–2598, 10.1007/s00018-015-1863-9.
95. [95] Jones, B.A., Fangman, W.L., Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin. Genes Dev. 6 (1992), 380–389.
96. [96] Guan, K., Farh, L., Marshall, T.K., Deschenes, R.J., Normal mitochondrial structure and genome maintenance in yeast requires the dynamin-like product of the MGM1 gene. Curr. Genet. 24 (1993), 141–148.
97. [97] Pelloquin, L., Belenguer, P., Menon, Y., Gas, N., Ducommun, B., Fission yeast Msp1 is a mitochondrial dynamin-related protein. J. Cell Sci. 112:Pt 22 (1999), 4151–4161.
98. [98] Zick, M., Duvezin-Caubet, S., Schäfer, A., Vogel, F., Neupert, W., Reichert, A.S., Distinct roles of the two isoforms of the dynamin-like GTPase Mgm1 in mitochondrial fusion. FEBS Lett. 583 (2009), 2237–2243, 10.1016/j.febslet.2009.05.053.
99. [99] Hermann, G.J., Thatcher, J.W., Mills, J.P., Hales, K.G., Fuller, M.T., Nunnari, J., et al. Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p. J. Cell Biol. 143 (1998), 359–373.
100. [100] Shepard, K.A., Yaffe, M.P., The yeast dynamin-like protein, Mgm1p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance. J. Cell Biol. 144 (1999), 711–720.
101. [101] Chen, H., Vermulst, M., Wang, Y.E., Chomyn, A., Prolla, T.A., McCaffery, J.M., et al. Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations. Cell 141 (2010), 280–289, 10.1016/j.cell.2010.02.026.
102. [102] Sesaki, H., Jensen, R.E., Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape. J. Cell Biol. 147 (1999), 699–706.
103. [103] Ishihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S.O., Masuda, K., et al. Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice. Nat. Cell Biol. 11 (2009), 958–966, 10.1038/ncb1907.
104. [104] Friedman, J.R., Lackner, L.L., West, M., DiBenedetto, J.R., Nunnari, J., Voeltz, G.K., ER tubules mark sites of mitochondrial division. Science 334 (2011), 358–362, 10.1126/science.1207385.
105. [105] Murley, A., Lackner, L.L., Osman, C., West, M., Voeltz, G.K., Walter, P., et al. ER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast. Elife, 2, 2013, e00422, 10.7554/eLife.00422.
106. [106] Ban-Ishihara, R., Ishihara, T., Sasaki, N., Mihara, K., Ishihara, N., Dynamics of nucleoid structure regulated by mitochondrial fission contributes to cristae reformation and release of cytochrome c. Proc. Natl. Acad. Sci. U. S. A. 110 (2013), 11863–11868, 10.1073/pnas.1301951110.
107. [107] Chen, H., McCaffery, J.M., Chan, D.C., Mitochondrial fusion protects against neurodegeneration in the cerebellum. Cell 130 (2007), 548–562, 10.1016/j.cell.2007.06.026.
108. [108] de Brito, O.M., Scorrano, L., Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 456 (2008), 605–610, 10.1038/nature07534.
109. [109] Wasilewski, M., Semenzato, M., Rafelski, S.M., Robbins, J., Bakardjiev, A.I., Scorrano, L., Optic atrophy 1-dependent mitochondrial remodeling controls steroidogenesis in trophoblasts. Curr. Biol. 22 (2012), 1228–1234, 10.1016/j.cub.2012.04.054.
110. [110] Daniele, T., Hurbain, I., Vago, R., Casari, G., Raposo, G., Tacchetti, C., et al. Mitochondria and melanosomes establish physical contacts modulated by Mfn2 and involved in organelle biogenesis. Curr. Biol. 24 (2014), 393–403, 10.1016/j.cub.2014.01.007.
111. [111] Misko, A., Jiang, S., Wegorzewska, I., Milbrandt, J., Baloh, R.H., Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex. J. Neurosci. 30 (2010), 4232–4240, 10.1523/JNEUROSCI.6248-09.2010.
112. [112] Misko, A.L., Sasaki, Y., Tuck, E., Milbrandt, J., Baloh, R.H., Mitofusin2 mutations disrupt axonal mitochondrial positioning and promote axon degeneration. J. Neurosci. 32 (2012), 4145–4155, 10.1523/JNEUROSCI.6338-11.2012.
113. [113] Sood, A., Jeyaraju, D.V., Prudent, J., Caron, A., Lemieux, P., McBride, H.M., et al. A Mitofusin-2-dependent inactivating cleavage of Opa1 links changes in mitochondria cristae and ER contacts in the postprandial liver. Proc. Natl. Acad. Sci. U. S. A. 111 (2014), 16017–16022, 10.1073/pnas.1408061111.
114. [114] Sugiura, A., Nagashima, S., Tokuyama, T., Amo, T., Matsuki, Y., Ishido, S., et al. MITOL regulates endoplasmic reticulum-mitochondria contacts via Mitofusin2. Mol. Cell 51 (2013), 20–34, 10.1016/j.molcel.2013.04.023.
115. [115] Area-Gomez, E., Del Carmen Lara Castillo, M., Tambini, M.D., Guardia-Laguarta, C., de Groof, A.J.C., Madra, M., et al. Upregulated function of mitochondria-associated ER membranes in Alzheimer disease. EMBO J. 31 (2012), 4106–4123, 10.1038/emboj.2012.202.
116. [116] Hailey, D.W., Rambold, A.S., Satpute-Krishnan, P., Mitra, K., Sougrat, R., Kim, P.K., et al. Mitochondria supply membranes for autophagosome biogenesis during starvation. Cell 141 (2010), 656–667, 10.1016/j.cell.2010.04.009.
117. [117] Sebastián, D., Hernández-Alvarez, M.I., Segalés, J., Sorianello, E., Muñoz, J.P., Sala, D., et al. Mitofusin 2 (Mfn2) links mitochondrial and endoplasmic reticulum function with insulin signaling and is essential for normal glucose homeostasis. Proc. Natl. Acad. Sci. U. S. A. 109 (2012), 5523–5528, 10.1073/pnas.1108220109.
118. [118] Cosson, P., Marchetti, A., Ravazzola, M., Orci, L., Mitofusin-2 independent juxtaposition of endoplasmic reticulum and mitochondria: an ultrastructural study. PLoS One, 7, 2012, e46293, 10.1371/journal.pone.0046293.
119. [119] Filadi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., Pizzo, P., Mitofusin 2 ablation increases endoplasmic reticulum-mitochondria coupling. Proc. Natl. Acad. Sci. U. S. A., 2015, 10.1073/pnas.1504880112.
120. [120] Duarte, A., Poderoso, C., Cooke, M., Soria, G., Cornejo Maciel, F., Gottifredi, V., et al. Mitochondrial fusion is essential for steroid biosynthesis. PLoS One, 7, 2012, e45829, 10.1371/journal.pone.0045829.
121. [121] Lee, S., Sterky, F.H., Mourier, A., Terzioglu, M., Cullheim, S., Olson, L., et al. Mitofusin 2 is necessary for striatal axonal projections of midbrain dopamine neurons. Hum. Mol. Genet. 21 (2012), 4827–4835, 10.1093/hmg/dds352.
122. [122] Pham, A.H., Meng, S., Chu, Q.N., Chan, D.C., Loss of Mfn2 results in progressive, retrograde degeneration of dopaminergic neurons in the nigrostriatal circuit. Hum. Mol. Genet. 21 (2012), 4817–4826, 10.1093/hmg/dds311.
123. [123] Papanicolaou, K.N., Khairallah, R.J., Ngoh, G.A., Chikando, A., Luptak, I., O'Shea, K.M., et al. Mitofusin-2 maintains mitochondrial structure and contributes to stress-induced permeability transition in cardiac myocytes. Mol. Cell. Biol. 31 (2011), 1309–1328, 10.1128/MCB.00911-10.
124. [124] Papanicolaou, K.N., Ngoh, G.A., Dabkowski, E.R., O'Connell, K.A., Ribeiro, R.F., Stanley, W.C., et al. Cardiomyocyte deletion of mitofusin-1 leads to mitochondrial fragmentation and improves tolerance to ROS-induced mitochondrial dysfunction and cell death. Am. J. Physiol. Heart Circ. Physiol., 2011, 10.1152/ajpheart.00833.2011.
125. [125] Loiseau, D., Chevrollier, A., Verny, C., Guillet, V., Gueguen, N., Pou de Crescenzo, M.-A., et al. Mitochondrial coupling defect in Charcot-Marie-Tooth type 2A disease. Ann. Neurol. 61 (2007), 315–323, 10.1002/ana.21086.
126. [126] Mourier, A., Motori, E., Brandt, T., Lagouge, M., Atanassov, I., Galinier, A., et al. Mitofusin 2 is required to maintain mitochondrial coenzyme Q levels. J. Cell Biol. 208 (2015), 429–442, 10.1083/jcb.201411100.
127. [127] Guillet, V., Gueguen, N., Verny, C., Ferre, M., Homedan, C., Loiseau, D., et al. Adenine nucleotide translocase is involved in a mitochondrial coupling defect in MFN2-related Charcot-Marie-Tooth type 2A disease. Neurogenetics 11 (2010), 127–133, 10.1007/s10048-009-0207-z.
128. [128] Szkopińska, A., Ubiquinone. Biosynthesis of quinone ring and its isoprenoid side chain. Intracellular localization. Acta Biochim. Pol. 47 (2000), 469–480.
129. [129] Tran, U.C., Clarke, C.F., Endogenous synthesis of coenzyme Q in eukaryotes. Mitochondrion(7 Suppl.), 2007, S62–S71, 10.1016/j.mito.2007.03.007.
130. [130] Wang, Y., Hekimi, S., Molecular genetics of ubiquinone biosynthesis in animals. Crit. Rev. Biochem. Mol. Biol. 48 (2013), 69–88, 10.3109/10409238.2012.741564.
131. [131] Keller, G.A., Pazirandeh, M., Krisans, S., 3-Hydroxy-3-methylglutaryl coenzyme A reductase localization in rat liver peroxisomes and microsomes of control and cholestyramine-treated animals: quantitative biochemical and immunoelectron microscopical analyses. J. Cell Biol. 103 (1986), 875–886.
132. [132] Olivier, L.M., Krisans, S.K., Peroxisomal protein targeting and identification of peroxisomal targeting signals in cholesterol biosynthetic enzymes. Biochim. Biophys. Acta 1529 (2000), 89–102.
133. [133] Kovacs, W.J., Faust, P.L., Keller, G.A., Krisans, S.K., Purification of brain peroxisomes and localization of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Eur. J. Biochem. FEBS 268 (2001), 4850–4859.
134. [134] Duarte, A., Castillo, A.F., Podestá, E.J., Poderoso, C., Mitochondrial fusion and ERK activity regulate steroidogenic acute regulatory protein localization in mitochondria. PLoS One, 9, 2014, e100387, 10.1371/journal.pone.0100387.
135. [135] Amiott, E.A., Lott, P., Soto, J., Kang, P.B., McCaffery, J.M., Dimauro, S., et al. Mitochondrial fusion and function in Charcot-Marie-Tooth type 2A patient fibroblasts with mitofusin 2 mutations. Exp. Neurol. 211 (2008), 115–127, 10.1016/j.expneurol.2008.01.010.
136. [136] Takahashi, R., Ikeda, T., Hamaguchi, A., Iwasa, K., Yamada, M., Coenzyme Q10 therapy in hereditary motor sensory neuropathy type VI with novel mitofusin 2 mutation. Intern. Med. (Tokyo, Japan) 51 (2012), 791–793.
137. [137] Zhao, T., Huang, X., Han, L., Wang, X., Cheng, H., Zhao, Y., et al. Central role of mitofusin 2 in autophagosome-lysosome fusion in cardiomyocytes. J. Biol. Chem. 287 (2012), 23615–23625, 10.1074/jbc.M112.379164.
138. [138] Araki, M., Motojima, K., Hydrophobic statins induce autophagy in cultured human rhabdomyosarcoma cells. Biochem. Biophys. Res. Commun. 367 (2008), 462–467, 10.1016/j.bbrc.2007.12.166.
139. [139] Wasko, B.M., Dudakovic, A., Hohl, R.J., Bisphosphonates induce autophagy by depleting geranylgeranyl diphosphate. J. Pharmacol. Exp. Ther. 337 (2011), 540–546, 10.1124/jpet.110.175521.