T. Ahmad, K. Aggarwal, B. Pattnaik, S. Mukherjee, T. Sethi et al., Computational classification of mitochondrial shapes reflects stress and redox state, Cell Death Dis, vol.4, p.461, 2013.

K. N. Alavian, H. Li, L. Collis, L. Bonanni, L. Zeng et al., Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase, Nat Cell Biol, vol.13, pp.1224-1233, 2011.

A. A. Amchenkova, L. E. Bakeeva, Y. S. Chentsov, V. P. Skulachev, and D. B. Zorov, Coupling membranes as energy-transmitting cables. I. Filamentous mitochondria in fibroblasts and mitochondrial clusters in cardiomyocytes, J Cell Biol, vol.107, pp.481-495, 1988.

R. Anand, T. Wai, M. J. Baker, N. Kladt, A. C. Schauss et al., The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission, J Cell Biol, vol.204, pp.919-929, 2014.

V. Andreu-fernandez, M. Sancho, A. Genoves, E. Lucendo, F. Todt et al., Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes, Proc Natl Acad Sci U S A, vol.114, pp.310-315, 2017.

V. Anesti and L. Scorrano, The relationship between mitochondrial shape and function and the cytoskeleton, Biochim Biophys Acta, vol.1757, pp.692-699, 2006.

M. G. Annis, E. L. Soucie, P. J. Dlugosz, J. A. Cruz-aguado, L. Z. Penn et al., Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis, EMBO J, vol.24, pp.2096-2103, 2005.

I. Antanaviciute, K. Rysevaite, V. Liutkevicius, A. Marandykina, L. Rimkute et al., Long-distance communication between laryngeal carcinoma cells, PLoS One, vol.9, p.99196, 2014.

M. A. Aon, S. Cortassa, and B. O'rourke, Percolation and criticality in a mitochondrial network, Proc Natl Acad Sci U S A, vol.101, pp.4447-4452, 2004.

A. Aouacheria, F. Brunet, and M. Gouy, Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-Only, and BNip families of apoptotic regulators, Mol Biol Evol, vol.22, pp.2395-2416, 2005.

A. Aouacheria, C. Combet, P. Tompa, and J. M. Hardwick, Redefining the BH3 Death Domain as a 'Short Linear Motif', Trends Biochem Sci, vol.40, pp.736-748, 2015.

A. Aouacheria, V. Rech-de-laval, C. Combet, and J. M. Hardwick, Evolution of Bcl-2 homology motifs: homology versus homoplasy, Trends Cell Biol, vol.23, pp.103-111, 2013.

S. L. Archer, Mitochondrial dynamics--mitochondrial fission and fusion in human diseases, N Engl J Med, vol.369, pp.2236-2251, 2013.

E. M. Armstrong, I. A. More, D. Mcseveney, and M. Carty, The giant mitochondrionendoplasmic reticulum unit of the human endometrial glandular cell, J Anat, vol.116, pp.375-383, 1973.

G. Ashrafi, J. S. Schlehe, M. J. Lavoie, and T. L. Schwarz, Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin, J Cell Biol, vol.206, pp.655-670, 2014.

R. H. Baloh, R. E. Schmidt, A. Pestronk, and J. Milbrandt, Altered axonal mitochondrial transport in the pathogenesis of Charcot-Marie-Tooth disease from mitofusin 2 mutations, J Neurosci, vol.27, pp.422-430, 2007.

E. L. Barnhart, Mechanics of mitochondrial motility in neurons, Curr Opin Cell Biol, vol.38, pp.90-99, 2016.

G. Basanez, A. Nechushtan, O. Drozhinin, A. Chanturiya, E. Choe et al., Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations, Proc Natl Acad Sci U S A, vol.96, pp.5492-5497, 1999.

G. Basanez, J. C. Sharpe, J. Galanis, T. B. Brandt, J. M. Hardwick et al., Baxtype apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature, J Biol Chem, vol.277, pp.49360-49365, 2002.

G. Basanez, J. Zhang, B. N. Chau, G. I. Maksaev, V. A. Frolov et al., Pro-apoptotic cleavage products of Bcl-xL form cytochrome c-conducting pores in pure lipid membranes, J Biol Chem, vol.276, pp.31083-31091, 2001.

M. Beck, K. Brickley, H. L. Wilkinson, S. Sharma, M. Smith et al., Identification, molecular cloning, and characterization of a novel GABAA receptor-associated protein, GRIF-1, J Biol Chem, vol.277, pp.30079-30090, 2002.

G. Benard and R. Rossignol, Ultrastructure of the mitochondrion and its bearing on function and bioenergetics, Antioxid Redox Signal, vol.10, pp.1313-1342, 2008.

T. Bender and J. C. Martinou, Where killers meet--permeabilization of the outer mitochondrial membrane during apoptosis, Cold Spring Harb Perspect Biol, vol.5, 2013.

J. Bereiter-hahn, Behavior of mitochondria in the living cell, Int Rev Cytol, vol.122, pp.1-63, 1990.

S. B. Berman, Y. B. Chen, B. Qi, J. M. Mccaffery, E. B. Rucker et al., Bcl-x L increases mitochondrial fission, fusion, and biomass in neurons, J Cell Biol, vol.184, pp.707-719, 2009.

S. B. Berman and J. M. Hardwick, Neuronal mitochondria are different: relevance to neurodegenerative diseas, The Functions, Disease-Related Dysfunctions and Therapeutic Targeting of Neuronal Mitochondria, pp.221-239, 2015.

S. B. Berman, F. J. Pineda, and J. M. Hardwick, Mitochondrial fission and fusion dynamics: the long and short of it, Cell Death Differ, vol.15, pp.1147-1152, 2008.

A. M. Bertholet, T. Delerue, A. M. Millet, M. F. Moulis, C. David et al., Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity, Neurobiol Dis, vol.90, pp.3-19, 2016.

P. D. Bhola and A. Letai, Mitochondria-Judges and Executioners of Cell Death Sentences, Mol Cell, vol.61, pp.695-704, 2016.

L. A. Bindoff, M. A. Birch-machin, N. E. Cartlidge, W. D. Parker, . Jr et al., Respiratory chain abnormalities in skeletal muscle from patients with Parkinson's disease, J Neurol Sci, vol.104, pp.203-208, 1991.

L. Blanchet, J. A. Smeitink, S. E. Van-emst-de-vries, C. Vogels, M. Pellegrini et al., Quantifying small molecule phenotypic effects using mitochondrial morpho-functional fingerprinting and machine learning, p.8035, 2015.

S. Bleicken, G. Jeschke, C. Stegmueller, R. Salvador-gallego, A. J. Garcia-saez et al., Structural model of active Bax at the membrane, Mol Cell, vol.56, pp.496-505, 2014.

J. Blesa, I. Trigo-damas, A. Quiroga-varela, and V. R. Jackson-lewis, Oxidative stress and Parkinson's disease, Front Neuroanat, vol.9, p.91, 2015.

M. Bonora, C. Morganti, G. Morciano, C. Giorgi, M. R. Wieckowski et al., Comprehensive analysis of mitochondrial permeability transition pore activity in living cells using fluorescence-imaging-based techniques, Nat Protoc, vol.11, pp.1067-1080, 2016.

E. A. Bordt, P. Clerc, B. A. Roelofs, A. J. Saladino, L. Tretter et al., The Putative Drp1 Inhibitor mdivi-1 Is a Reversible Mitochondrial Complex I Inhibitor that Modulates Reactive Oxygen Species, Dev Cell, vol.40, pp.583-594, 2017.

T. Brandt, L. Cavellini, W. Kuhlbrandt, and M. M. Cohen, A mitofusin-dependent docking ring complex triggers mitochondrial fusion in vitro, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01550113

R. Bravo, J. M. Vicencio, V. Parra, R. Troncoso, J. P. Munoz et al., Increased ER-mitochondrial coupling promotes mitochondrial respiration and bioenergetics during early phases of ER stress, J Cell Sci, vol.124, pp.2143-2152, 2011.

P. S. Brookes, Y. Yoon, J. L. Robotham, M. W. Anders, and S. S. Sheu, Calcium, ATP, and ROS: a mitochondrial love-hate triangle, Am J Physiol Cell Physiol, vol.287, pp.817-833, 2004.

J. M. Brouwer, D. Westphal, G. Dewson, A. Y. Robin, R. T. Uren et al., Bak core and latch domains separate during activation, and freed core domains form symmetric homodimers, Mol Cell, vol.55, pp.938-946, 2014.

F. Burte, V. Carelli, P. F. Chinnery, and P. Yu-wai-man, Disturbed mitochondrial dynamics and neurodegenerative disorders, Nat Rev Neurol, vol.11, pp.11-24, 2015.

M. Cagalinec, M. Liiv, Z. Hodurova, M. A. Hickey, A. Vaarmann et al., Role of Mitochondrial Dynamics in Neuronal Development: Mechanism for Wolfram Syndrome, PLoS Biol, vol.14, 2016.
URL : https://hal.archives-ouvertes.fr/inserm-02136380

M. Cagalinec, D. Safiulina, M. Liiv, J. Liiv, V. Choubey et al., Principles of the mitochondrial fusion and fission cycle in neurons, J Cell Sci, vol.126, pp.2187-2197, 2013.

Q. Cai, M. L. Davis, and Z. H. Sheng, Regulation of axonal mitochondrial transport and its impact on synaptic transmission, Neurosci Res, vol.70, pp.9-15, 2011.

M. C. Caino, J. H. Seo, A. Aguinaldo, E. Wait, K. G. Bryant et al., A neuronal network of mitochondrial dynamics regulates metastasis, Nat Commun, vol.7, p.13730, 2016.

H. A. Cameron, C. K. Kaliszewski, and C. A. Greer, Organization of mitochondria in olfactory bulb granule cell dendritic spines, Synapse, vol.8, pp.107-118, 1991.

Y. L. Cao, S. Meng, Y. Chen, J. X. Feng, D. D. Gu et al., MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion, Nature, vol.542, pp.372-376, 2017.

K. L. Cerveny, J. M. Mccaffery, and R. E. Jensen, Division of mitochondria requires a novel DMN1-interacting protein, Net2p, Mol Biol Cell, vol.12, pp.309-321, 2001.

D. C. Chan, Fusion and fission: interlinked processes critical for mitochondrial health, Annu Rev Genet, vol.46, pp.265-287, 2012.

B. N. Chau, E. H. Cheng, D. A. Kerr, and J. M. Hardwick, Aven, a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-1, Mol Cell, vol.6, pp.31-40, 2000.

H. Chen and D. C. Chan, Physiological functions of mitochondrial fusion, Ann N Y Acad Sci, vol.1201, pp.21-25, 2010.

H. Chen, S. A. Detmer, A. J. Ewald, E. E. Griffin, S. E. Fraser et al., Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development, J Cell Biol, vol.160, pp.189-200, 2003.

H. Chen, J. M. Mccaffery, and D. C. Chan, Mitochondrial fusion protects against neurodegeneration in the cerebellum, Cell, vol.130, pp.548-562, 2007.

H. Chen, M. Vermulst, Y. E. Wang, A. Chomyn, T. A. Prolla et al., Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations, Cell, vol.141, pp.280-289, 2010.

M. Chen, Y. Li, M. Yang, X. Chen, Y. Chen et al., A new method for quantifying mitochondrial axonal transport, Protein Cell, vol.7, pp.804-819, 2016.

Y. Chen and G. W. Dorn, PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria, Science, vol.2, pp.471-475, 2013.

Y. Chen and Z. H. Sheng, Kinesin-1-syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport, J Cell Biol, vol.202, pp.351-364, 2013.

Y. B. Chen, M. A. Aon, Y. T. Hsu, L. Soane, X. Teng et al., Bcl-xL regulates mitochondrial energetics by stabilizing the inner membrane potential, J Cell Biol, vol.195, pp.263-276, 2011.

E. H. Cheng, D. G. Kirsch, R. J. Clem, R. Ravi, M. B. Kastan et al., Conversion of Bcl-2 to a Bax-like death effector by caspases, Science, vol.278, pp.1966-1968, 1997.

E. H. Cheng, B. Levine, L. H. Boise, C. B. Thompson, and J. M. Hardwick, Bax-independent inhibition of apoptosis by Bcl-XL, Nature, vol.379, pp.554-556, 1996.

E. H. Cheng, T. V. Sheiko, J. K. Fisher, W. J. Craigen, and S. J. Korsmeyer, VDAC2 inhibits BAK activation and mitochondrial apoptosis, Science, vol.301, pp.513-517, 2003.

W. C. Cheng, K. M. Leach, and J. M. Hardwick, Mitochondrial death pathways in yeast and mammalian cells, Biochim Biophys Acta, vol.1783, pp.1272-1279, 2008.

W. C. Cheng, X. Teng, H. K. Park, C. M. Tucker, M. J. Dunham et al., Fis1 deficiency selects for compensatory mutations responsible for cell death and growth control defects, Cell Death Differ, vol.15, pp.1838-1846, 2008.

E. Cherok, S. Xu, S. Li, S. Das, W. A. Meltzer et al., Novel regulatory roles of Mff and Drp1 in E3 ubiquitin ligase MARCH5-dependent degradation of MiD49 and Mcl1 and control of mitochondrial dynamics, Mol Biol Cell, vol.28, pp.396-410, 2017.

A. Chevrollier, J. Cassereau, M. Ferre, J. Alban, V. Desquiret-dumas et al., Standardized mitochondrial analysis gives new insights into mitochondrial dynamics and OPA1 function, Int J Biochem Cell Biol, vol.44, pp.980-988, 2012.

J. E. Chipuk, L. Bouchier-hayes, T. Kuwana, D. D. Newmeyer, and D. R. Green, PUMA couples the nuclear and cytoplasmic proapoptotic function of p53, Science, vol.309, pp.1732-1735, 2005.

H. W. Choi, J. H. Kim, M. K. Chung, Y. J. Hong, H. S. Jang et al., Mitochondrial and metabolic remodeling during reprogramming and differentiation of the reprogrammed cells, Stem Cells Dev, vol.24, pp.1366-1373, 2015.

R. J. Clem, E. H. Cheng, C. L. Karp, D. G. Kirsch, K. Ueno et al., Modulation of cell death by Bcl-XL through caspase interaction, Proc Natl Acad Sci U S A, vol.95, pp.554-559, 1998.

T. J. Collins, M. J. Berridge, P. Lipp, and M. D. Bootman, Mitochondria are morphologically and functionally heterogeneous within cells, EMBO J, vol.21, pp.1616-1627, 2002.

M. Corrado, L. Scorrano, and S. Campello, Mitochondrial dynamics in cancer and neurodegenerative and neuroinflammatory diseases, Int J Cell Biol, 2012.

M. Costanzo, S. Abounit, L. Marzo, A. Danckaert, Z. Chamoun et al., Transfer of polyglutamine aggregates in neuronal cells occurs in tunneling nanotubes, J Cell Sci, vol.126, pp.3678-3685, 2013.
URL : https://hal.archives-ouvertes.fr/pasteur-00874692

D. Cotter, P. Guda, E. Fahy, and S. Subramaniam, MitoProteome: mitochondrial protein sequence database and annotation system, Nucleic Acids Res, vol.32, pp.463-467, 2004.

P. E. Czabotar, D. Westphal, G. Dewson, S. Ma, C. Hockings et al., Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis, Cell, vol.152, pp.519-531, 2013.

B. D'orsi, S. M. Kilbride, G. Chen, S. Perez-alvarez, H. P. Bonner et al., Bax regulates neuronal Ca2+ homeostasis, J Neurosci, vol.35, pp.1706-1722, 2015.

G. Dalmasso, P. A. Marin-zapata, N. R. Brady, and A. Hamacher-brady, Agent-Based Modeling of Mitochondria Links Sub-Cellular Dynamics to Cellular Homeostasis and Heterogeneity, PLoS One, vol.12, 2017.

C. H. Davis, K. Y. Kim, E. A. Bushong, E. A. Mills, D. Boassa et al., Transcellular degradation of axonal mitochondria, Proc Natl Acad Sci U S A, vol.111, pp.9633-9638, 2014.

K. J. De-vos, V. J. Allan, A. J. Grierson, and M. P. Sheetz, Mitochondrial function and actin regulate dynamin-related protein 1-dependent mitochondrial fission, Curr Biol, vol.15, pp.678-683, 2005.

K. J. De-vos, A. L. Chapman, M. E. Tennant, C. Manser, E. L. Tudor et al., Familial amyotrophic lateral sclerosis-linked SOD1 mutants perturb fast axonal transport to reduce axonal mitochondria content, Hum Mol Genet, vol.16, pp.2720-2728, 2007.

P. Delivani, C. Adrain, R. C. Taylor, P. J. Duriez, and S. J. Martin, Role for CED-9 and Egl-1 as regulators of mitochondrial fission and fusion dynamics, Mol Cell, vol.21, pp.761-773, 2006.

S. P. Desai, S. N. Bhatia, M. Toner, and D. Irimia, Mitochondrial localization and the persistent migration of epithelial cancer cells, Biophys J, vol.104, pp.2077-2088, 2013.

S. A. Detmer and D. C. Chan, Functions and dysfunctions of mitochondrial dynamics, Nat Rev Mol Cell Biol, vol.8, pp.870-879, 2007.

A. A. Dukes, Q. Bai, V. S. Van-laar, Y. Zhou, V. Ilin et al., Live imaging of mitochondrial dynamics in CNS dopaminergic neurons in vivo demonstrates early reversal of mitochondrial transport following MPP(+) exposure, Neurobiol Dis, vol.95, pp.238-249, 2016.

S. Duvezin-caubet, R. Jagasia, J. Wagener, S. Hofmann, A. Trifunovic et al., Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology, J Biol Chem, vol.281, pp.37972-37979, 2006.

S. Ehses, I. Raschke, G. Mancuso, A. Bernacchia, S. Geimer et al., Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1, J Cell Biol, vol.187, pp.1023-1036, 2009.

D. M. Engelthaler, N. D. Hicks, J. D. Gillece, C. C. Roe, J. M. Schupp et al., Cryptococcus gattii in North American Pacific Northwest: whole-population genome analysis provides insights into species evolution and dispersal, MBio, vol.5, pp.1464-01414, 2014.

Y. Eura, N. Ishihara, S. Yokota, and K. Mihara, Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion, J Biochem, vol.134, pp.333-344, 2003.

Y. Fannjiang, W. C. Cheng, S. J. Lee, B. Qi, J. Pevsner et al., Mitochondrial fission proteins regulate programmed cell death in yeast, Genes Dev, vol.18, pp.2785-2797, 2004.

Y. Fannjiang, C. H. Kim, R. L. Huganir, S. Zou, T. Lindsten et al., BAK alters neuronal excitability and can switch from anti-to pro-death function during postnatal development, Dev Cell, vol.4, pp.575-585, 2003.

P. Fekkes, K. A. Shepard, and M. P. Yaffe, Gag3p, an outer membrane protein required for fission of mitochondrial tubules, J Cell Biol, vol.151, pp.333-340, 2000.

F. Ferreirinha, A. Quattrini, M. Pirozzi, V. Valsecchi, G. Dina et al., Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport, J Clin Invest, vol.113, pp.231-242, 2004.

T. A. Fiacco and K. D. Mccarthy, Intracellular astrocyte calcium waves in situ increase the frequency of spontaneous AMPA receptor currents in CA1 pyramidal neurons, J Neurosci, vol.24, pp.722-732, 2004.

L. W. Finley, J. Lee, A. Souza, V. Desquiret-dumas, K. Bullock et al., Skeletal muscle transcriptional coactivator PGC-1alpha mediates mitochondrial, but not metabolic, changes during calorie restriction, Proc Natl Acad Sci U S A, vol.109, pp.2931-2936, 2012.

K. H. Flippo and S. Strack, Mitochondrial dynamics in neuronal injury, development and plasticity, J Cell Sci, vol.130, pp.671-681, 2017.

A. Franco, R. N. Kitsis, J. A. Fleischer, E. Gavathiotis, O. S. Kornfeld et al., Correcting mitochondrial fusion by manipulating mitofusin conformations, Nature, vol.II, pp.74-79, 2016.

S. Frank, B. Gaume, E. S. Bergmann-leitner, W. W. Leitner, E. G. Robert et al., The role of dynamin-related protein 1, a mediator of mitochondrial fission, Dev Cell, vol.1, pp.515-525, 2001.
URL : https://hal.archives-ouvertes.fr/hal-00153696

S. Fransson, A. Ruusala, and P. Aspenstrom, The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking, Biochem Biophys Res Commun, vol.344, pp.500-510, 2006.

J. R. Friedman, L. L. Lackner, M. West, J. R. Dibenedetto, J. Nunnari et al., ER tubules mark sites of mitochondrial division, Science, vol.334, pp.358-362, 2011.

Y. Fujiki, N. Miyata, S. Mukai, K. Okumoto, and E. H. Cheng, BAK regulates catalase release from peroxisomes. Molecular and Cellular Oncology, 2017.

S. Gandre-babbe and A. M. Van-der-bliek, The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells, Mol Biol Cell, vol.19, pp.2402-2412, 2008.

A. J. Garcia-saez, M. Coraiola, M. D. Serra, I. Mingarro, P. Muller et al., Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores, FEBS J, vol.273, pp.971-981, 2006.

R. J. Giedt, P. Fumene-feruglio, D. Pathania, K. S. Yang, A. Kilcoyne et al., Computational imaging reveals mitochondrial morphology as a biomarker of cancer phenotype and drug response, Sci Rep, vol.6, p.32985, 2016.

A. Gimenez-cassina, L. Garcia-haro, C. S. Choi, M. A. Osundiji, E. A. Lane et al., Regulation of hepatic energy metabolism and gluconeogenesis by BAD, Cell Metab, vol.19, pp.272-284, 2014.

C. Giorgi, K. Ito, H. K. Lin, C. Santangelo, M. R. Wieckowski et al., PML regulates apoptosis at endoplasmic reticulum by modulating calcium release, Science, vol.330, pp.1247-1251, 2010.

B. Glancy, L. M. Hartnell, D. Malide, Z. X. Yu, C. A. Combs et al., Mitochondrial reticulum for cellular energy distribution in muscle, Nature, vol.523, pp.617-620, 2015.

L. C. Gomes, G. Di-benedetto, and L. Scorrano, During autophagy mitochondria elongate, are spared from degradation and sustain cell viability, Nat Cell Biol, vol.13, pp.589-598, 2011.

L. C. Gomes, G. Di-benedetto, and L. Scorrano, Essential amino acids and glutamine regulate induction of mitochondrial elongation during autophagy, Cell Cycle, vol.10, pp.2635-2639, 2011.

M. Gonzalez-garcia, I. Garcia, L. Ding, S. O'shea, L. H. Boise et al., bcl-x is expressed in embryonic and postnatal neural tissues and functions to prevent neuronal cell death, Proc Natl Acad Sci U S A, vol.92, pp.4304-4308, 1995.

A. M. Gonzalez-jamett, V. Haro-acuna, F. Momboisse, P. Caviedes, J. A. Bevilacqua et al., Dynamin-2 in nervous system disorders, J Neurochem, vol.128, pp.210-223, 2014.

D. R. Green, A BH3 Mimetic for Killing Cancer Cells, Cell, vol.165, p.1560, 2016.

I. Grigoriev, S. M. Gouveia, B. Van-der-vaart, J. Demmers, J. T. Smyth et al., STIM1 is a MT-plus-end-tracking protein involved in remodeling of the ER, Curr Biol, vol.18, pp.177-182, 2008.

L. Griparic, T. Kanazawa, and A. M. Van-der-bliek, Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage, J Cell Biol, vol.178, pp.757-764, 2007.

L. Griparic, N. N. Van-der-wel, I. J. Orozco, P. J. Peters, and A. M. Van-der-bliek, Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria, J Biol Chem, vol.279, pp.18792-18798, 2004.

A. Gross and S. G. Katz, Non-apoptotic functions of BCL-2 family proteins, Cell Death Differ, 2017.

Y. Guillemin, P. Lalle, G. Gillet, J. F. Guerin, S. Hamamah et al., Oocytes and early embryos selectively express the survival factor BCL2L10, J Mol Med, vol.87, pp.923-940, 2009.

O. Guillery, F. Malka, P. Frachon, D. Milea, M. Rojo et al., Modulation of mitochondrial morphology by bioenergetics defects in primary human fibroblasts, Neuromuscul Disord, vol.18, pp.319-330, 2008.

A. Hamacher-brady and N. R. Brady, Mitophagy programs: mechanisms and physiological implications of mitochondrial targeting by autophagy, Cell Mol Life Sci, vol.73, pp.775-795, 2016.

S. Hamner, Y. Skoglosa, and D. Lindholm, Differential expression of bcl-w and bcl-x messenger RNA in the developing and adult rat nervous system, Neuroscience, vol.91, pp.673-684, 1999.

R. A. Hanna, M. N. Quinsay, A. M. Orogo, K. Giang, S. Rikka et al., Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy, J Biol Chem, vol.287, pp.19094-19104, 2012.

J. M. Hardwick, Y. B. Chen, and E. A. Jonas, Multipolar functions of BCL-2 proteins link energetics to apoptosis, Trends Cell Biol, vol.22, pp.318-328, 2012.

J. M. Hardwick and L. Soane, Multiple functions of BCL-2 family proteins, Cold Spring Harb Perspect Biol, vol.5, 2013.

D. Harman, A. L. Hatch, W. K. Ji, R. A. Merrill, S. Strack et al., Actin filaments as dynamic reservoirs for Drp1 recruitment, J Am Geriatr Soc, vol.20, pp.3109-3121, 1972.

K. Hayakawa, E. Esposito, X. Wang, Y. Terasaki, Y. Liu et al., Transfer of mitochondria from astrocytes to neurons after stroke, Nature, vol.535, pp.551-555, 2016.

S. Hayashi and Y. Okada, Ultrafast superresolution fluorescence imaging with spinning disk confocal microscope optics, Mol Biol Cell, vol.26, pp.1743-1751, 2015.

B. Head, L. Griparic, M. Amiri, S. Gandre-babbe, and . Van-der-bliek, Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells, J Cell Biol, vol.187, pp.959-966, 2009.

M. H. Heggeness, M. Simon, and S. J. Singer, Association of mitochondria with microtubules in cultured cells, Proc Natl Acad Sci U S A, vol.75, pp.3863-3866, 1978.

J. A. Hickman, J. M. Hardwick, L. K. Kaczmarek, and E. A. Jonas, Bcl-xL inhibitor ABT-737 reveals a dual role for Bcl-xL in synaptic transmission, J Neurophysiol, vol.99, pp.1515-1522, 2008.

N. Hirokawa and Y. Tanaka, Kinesin superfamily proteins (KIFs): Various functions and their relevance for important phenomena in life and diseases, Exp Cell Res, vol.334, pp.16-25, 2015.

L. I. Hodneland-nilsson, I. K. Nitschke-pettersen, J. Nikolaisen, D. Micklem, H. Avsnes-dale et al., A new live-cell reporter strategy to simultaneously monitor mitochondrial biogenesis and morphology, Sci Rep, vol.5, p.17217, 2015.

H. Hoitzing, I. G. Johnston, and N. S. Jones, What is the function of mitochondrial networks? A theoretical assessment of hypotheses and proposal for future research, Bioessays, vol.37, pp.687-700, 2015.

G. P. Holloway, B. J. Gurd, L. A. Snook, J. Lally, and A. Bonen, Compensatory increases in nuclear PGC1alpha protein are primarily associated with subsarcolemmal mitochondrial adaptations in ZDF rats, Diabetes, vol.59, pp.819-828, 2010.

P. Holme, Temporal network structures controlling disease spreading, Phys Rev E, vol.94, p.22305, 2016.

K. I. Hosoi, N. Miyata, S. Mukai, S. Furuki, K. Okumoto et al., The VDAC2-BAK axis regulates peroxisomal membrane permeability, J Cell Biol, vol.216, pp.709-722, 2017.

X. Huang, L. Sun, S. Ji, T. Zhao, W. Zhang et al., Kissing and nanotunneling mediate intermitochondrial communication in the heart, Proc Natl Acad Sci U S A, vol.110, pp.2846-2851, 2013.

E. F. Iannetti, J. A. Smeitink, J. Beyrath, P. H. Willems, and W. J. Koopman, Multiplexed high-content analysis of mitochondrial morphofunction using live-cell microscopy, Nat Protoc, vol.11, pp.1693-1710, 2016.

D. E. Ingber, Tensegrity II. How structural networks influence cellular information processing networks, J Cell Sci, vol.116, pp.1397-1408, 2003.

N. Ishihara, Y. Fujita, T. Oka, and K. Mihara, Regulation of mitochondrial morphology through proteolytic cleavage of OPA1, EMBO J, vol.25, pp.2966-2977, 2006.

S. Iyer, F. Bell, D. Westphal, K. Anwari, J. Gulbis et al., Bak apoptotic pores involve a flexible C-terminal region and juxtaposition of the Cterminal transmembrane domains, Cell Death Differ, vol.22, pp.1665-1675, 2015.

S. P. Iyer, Y. Akimoto, and G. W. Hart, Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase, J Biol Chem, vol.278, pp.5399-5409, 2003.

R. Jagasia, P. Grote, B. Westermann, and B. Conradt, DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans, Nature, vol.433, pp.754-760, 2005.

R. E. Jensen, A. E. Hobbs, K. L. Cerveny, and H. Sesaki, Yeast mitochondrial dynamics: fusion, division, segregation, and shape, Microsc Res Tech, vol.51, pp.573-583, 2000.

Y. F. Jiang, S. S. Lin, J. M. Chen, H. Z. Tsai, T. S. Hsieh et al., Electron tomographic analysis reveals ultrastructural features of mitochondrial cristae architecture which reflect energetic state and aging, Sci Rep, vol.7, p.45474, 2017.

S. Jiao and Z. Li, Nonapoptotic function of BAD and BAX in long-term depression of synaptic transmission, Neuron, vol.70, pp.758-772, 2011.

E. A. Jonas, J. M. Hardwick, and L. K. Kaczmarek, Actions of BAX on mitochondrial channel activity and on synaptic transmission, Antioxid Redox Signal, vol.7, pp.1092-1100, 2005.

E. A. Jonas, J. A. Hickman, M. Chachar, B. M. Polster, T. A. Brandt et al., Proapoptotic N-truncated BCL-xL protein activates endogenous mitochondrial channels in living synaptic terminals, Proc Natl Acad Sci U S A, vol.101, pp.13590-13595, 2004.

E. A. Jonas, J. A. Hickman, J. M. Hardwick, and L. K. Kaczmarek, Exposure to hypoxia rapidly induces mitochondrial channel activity within a living synapse, J Biol Chem, vol.280, pp.4491-4497, 2005.

E. A. Jonas, D. Hoit, J. A. Hickman, T. A. Brandt, B. M. Polster et al., Modulation of synaptic transmission by the BCL-2 family protein BCL-xL, J Neurosci, vol.23, pp.8423-8431, 2003.

J. Kandel, P. Chou, and D. M. Eckmann, Automated detection of whole-cell mitochondrial motility and its dependence on cytoarchitectural integrity, Biotechnol Bioeng, vol.112, pp.1395-1405, 2015.

G. Kanfer, T. Courtheoux, M. Peterka, S. Meier, M. Soste et al., Mitotic redistribution of the mitochondrial network by Miro and Cenp-F, Nat Commun, vol.6, p.8015, 2015.

S. M. Karam, T. Straiton, W. M. Hassan, and C. P. Leblond, Defining epithelial cell progenitors in the human oxyntic mucosa, Stem Cells, vol.21, pp.322-336, 2003.

M. Karbowski, K. L. Norris, M. M. Cleland, S. Y. Jeong, and R. J. Youle, Role of Bax and Bak in mitochondrial morphogenesis, Nature, vol.443, pp.658-662, 2006.

M. Karbowski, J. H. Spodnik, M. Teranishi, M. Wozniak, Y. Nishizawa et al., Opposite effects of microtubule-stabilizing and microtubuledestabilizing drugs on biogenesis of mitochondria in mammalian cells, J Cell Sci, vol.114, pp.281-291, 2001.

M. Karbowski and R. J. Youle, Dynamics of mitochondrial morphology in healthy cells and during apoptosis, Cell Death Differ, vol.10, pp.870-880, 2003.

J. A. Kashatus, A. Nascimento, L. J. Myers, A. Sher, F. L. Byrne et al., Erk2 phosphorylation of Drp1 promotes mitochondrial fission and MAPK-driven tumor growth, Mol Cell, vol.57, pp.537-551, 2015.

S. Kim, C. Laschi, and B. Trimmer, Soft robotics: a bioinspired evolution in robotics, Trends Biotechnol, vol.31, pp.287-294, 2013.

D. G. Kirsch, A. Doseff, B. N. Chau, D. S. Lim, N. C. De-souza-pinto et al., Caspase-3-dependent cleavage of Bcl-2 promotes release of cytochrome c, J Biol Chem, vol.274, pp.21155-21161, 1999.

S. Kiryu-seo, N. Ohno, G. J. Kidd, H. Komuro, and B. D. Trapp, Demyelination increases axonal stationary mitochondrial size and the speed of axonal mitochondrial transport, J Neurosci, vol.30, pp.6658-6666, 2010.

A. B. Knott, G. Perkins, R. Schwarzenbacher, and E. Bossy-wetzel, Mitochondrial fragmentation in neurodegeneration, Nat Rev Neurosci, vol.9, pp.505-518, 2008.

S. Koirala, Q. Guo, R. Kalia, H. T. Bui, D. M. Eckert et al., Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission, Proc Natl Acad Sci U S A, vol.110, pp.1342-1351, 2013.

W. J. Koopman, F. Distelmaier, J. J. Esseling, J. A. Smeitink, and P. H. Willems, Computerassisted live cell analysis of mitochondrial membrane potential, morphology and calcium handling, Methods, vol.46, pp.304-311, 2008.

W. J. Koopman, H. J. Visch, J. A. Smeitink, and P. H. Willems, Simultaneous quantitative measurement and automated analysis of mitochondrial morphology, mass, potential, and motility in living human skin fibroblasts, Cytometry A, vol.69, pp.1-12, 2006.

F. Korobova, T. J. Gauvin, and H. N. Higgs, A role for myosin II in mammalian mitochondrial fission, Curr Biol, vol.24, pp.409-414, 2014.

F. Korobova, V. Ramabhadran, and H. N. Higgs, An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2, Science, vol.339, pp.464-467, 2013.

T. Koshiba, S. A. Detmer, J. T. Kaiser, H. Chen, J. M. Mccaffery et al., Structural basis of mitochondrial tethering by mitofusin complexes, Science, vol.305, pp.858-862, 2004.

M. Krajewska, J. K. Mai, J. M. Zapata, K. W. Ashwell, S. L. Schendel et al., Dynamics of expression of apoptosis-regulatory proteins Bid, Bcl-2, Bcl-X, Bax and Bak during development of murine nervous system, Cell Death Differ, vol.9, pp.145-157, 2002.

T. Kuwana, M. R. Mackey, G. Perkins, M. H. Ellisman, M. Latterich et al., Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane, Cell, vol.111, pp.331-342, 2002.

L. L. Lackner, Shaping the dynamic mitochondrial network, BMC Biol, vol.12, p.35, 2014.

L. L. Lackner, J. S. Horner, and J. Nunnari, Mechanistic analysis of a dynamin effector, Science, vol.325, pp.874-877, 2009.

M. Lavorato, V. R. Iyer, W. Dewight, R. R. Cupo, V. Debattisti et al., Increased mitochondrial nanotunneling activity, induced by calcium imbalance, affects intermitochondrial matrix exchanges, Proc Natl Acad Sci U S A, vol.114, pp.849-858, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01848140

M. Lazarou, D. A. Sliter, L. A. Kane, S. A. Sarraf, C. Wang et al., The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy, Nature, vol.524, pp.309-314, 2015.

B. Leber, J. Lin, and D. W. Andrews, Still embedded together binding to membranes regulates Bcl-2 protein interactions, Oncogene, vol.29, pp.5221-5230, 2010.

E. F. Lee, G. Dewson, B. J. Smith, M. Evangelista, A. Pettikiriarachchi et al., Crystal structure of a BCL-W domain-swapped dimer: implications for the function of BCL-2 family proteins, Structure, vol.19, pp.1467-1476, 2011.

J. E. Lee, L. M. Westrate, H. Wu, C. Page, and G. K. Voeltz, Multiple dynamin family members collaborate to drive mitochondrial division, Nature, vol.540, pp.139-143, 2016.

S. Lee, S. Y. Jeong, W. C. Lim, S. Kim, Y. Y. Park et al., Mitochondrial fission and fusion mediators, hFis1 and OPA1, modulate cellular senescence, J Biol Chem, vol.282, pp.22977-22983, 2007.

W. H. Lee, H. Higuchi, S. Ikeda, E. L. Macke, T. Takimoto et al., Mouse Tmem135 mutation reveals a mechanism involving mitochondrial dynamics, 2016.

F. Legros, A. Lombes, P. Frachon, and M. Rojo, Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins, Mol Biol Cell, vol.13, pp.4343-4354, 2002.

F. E. Lennon, G. C. Cianci, R. Kanteti, J. J. Riehm, Q. Arif et al., Unique fractal evaluation and therapeutic implications of mitochondrial morphology in malignant mesothelioma, p.24578, 2016.

A. P. Leonard, R. B. Cameron, J. L. Speiser, B. J. Wolf, Y. K. Peterson et al., Quantitative analysis of mitochondrial morphology and membrane potential in living cells using high-content imaging, machine learning, and morphological binning, Biochim Biophys Acta, vol.1853, pp.348-360, 2015.

B. Levine, Q. Huang, J. T. Isaacs, J. C. Reed, D. E. Griffin et al., Conversion of lytic to persistent alphavirus infection by the bcl-2 cellular oncogene, Nature, vol.361, pp.739-742, 1993.

J. Lewis, G. A. Oyler, K. Ueno, Y. R. Fannjiang, B. N. Chau et al., Inhibition of virus-induced neuronal apoptosis by Bax, Nat Med, vol.5, pp.832-835, 1999.

H. Li, K. N. Alavian, E. Lazrove, N. Mehta, A. Jones et al., A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics during endocytosis, Nat Cell Biol, vol.15, pp.773-785, 2013.

H. Li, Y. Chen, A. F. Jones, R. H. Sanger, L. P. Collis et al., Bcl-xL induces Drp1-dependent synapse formation in cultured hippocampal neurons, Proc Natl Acad Sci U S A, vol.105, pp.2169-2174, 2008.

S. Li, S. Xu, B. A. Roelofs, L. Boyman, W. J. Lederer et al., Transient assembly of F-actin on the outer mitochondrial membrane contributes to mitochondrial fission, J Cell Biol, vol.208, pp.109-123, 2015.

Z. Li, J. Jo, J. M. Jia, S. C. Lo, D. J. Whitcomb et al., Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization, Cell, vol.141, pp.859-871, 2010.

Z. Li, K. Okamoto, Y. Hayashi, and M. Sheng, The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses, Cell, vol.119, pp.873-887, 2004.

C. Liao, Z. Zhang, J. Kale, D. W. Andrews, J. Lin et al., Conformational Heterogeneity of Bax Helix 9 Dimer for Apoptotic Pore Formation, Sci Rep, vol.6, p.29502, 2016.

M. Liesa and O. S. Shirihai, Mitochondrial dynamics in the regulation of nutrient utilization and energy expenditure, Cell Metab, vol.17, pp.491-506, 2013.

L. A. Ligon and O. Steward, Role of microtubules and actin filaments in the movement of mitochondria in the axons and dendrites of cultured hippocampal neurons, J Comp Neurol, vol.427, pp.351-361, 2000.

E. Lihavainen, J. Makela, J. N. Spelbrink, and A. S. Ribeiro, Mytoe: automatic analysis of mitochondrial dynamics, Bioinformatics, vol.28, pp.1050-1051, 2012.

M. Y. Lin and Z. H. Sheng, Regulation of mitochondrial transport in neurons, Exp Cell Res, vol.334, pp.35-44, 2015.

T. Lindsten, J. A. Golden, W. X. Zong, J. Minarcik, M. H. Harris et al., The proapoptotic activities of Bax and Bak limit the size of the neural stem cell pool, J Neurosci, vol.23, pp.11112-11119, 2003.

X. Liu and G. Hajnoczky, Altered fusion dynamics underlie unique morphological changes in mitochondria during hypoxia-reoxygenation stress, Cell Death Differ, vol.18, pp.1561-1572, 2011.

X. Liu, D. Weaver, O. Shirihai, and G. Hajnoczky, Mitochondrial 'kiss-and-run': interplay between mitochondrial motility and fusion-fission dynamics, EMBO J, vol.28, pp.3074-3089, 2009.

I. C. Lopez-mejia and L. Fajas, Cell cycle regulation of mitochondrial function, Curr Opin Cell Biol, vol.33, pp.19-25, 2015.

O. C. Loson, R. Liu, M. E. Rome, S. Meng, J. T. Kaiser et al., The mitochondrial fission receptor MiD51 requires ADP as a cofactor, Structure, vol.22, pp.367-377, 2014.

O. C. Loson, Z. Song, H. Chen, and D. C. Chan, Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission, Mol Biol Cell, vol.24, pp.659-667, 2013.

H. H. Low, C. Sachse, L. A. Amos, and J. Lowe, Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving, Cell, vol.139, pp.1342-1352, 2009.

J. Lu, X. Zheng, F. Li, Y. Yu, Z. Chen et al., Tunneling nanotubes promote intercellular mitochondria transfer followed by increased invasiveness in bladder cancer cells, Oncotarget, 2017.

Y. Lu, S. G. Rolland, and B. Conradt, A molecular switch that governs mitochondrial fusion and fission mediated by the BCL2-like protein CED-9 of Caenorhabditis elegans, Proc Natl Acad Sci U S A, vol.108, pp.813-822, 2011.

A. F. Macaskill and J. T. Kittler, Control of mitochondrial transport and localization in neurons, Trends Cell Biol, vol.20, pp.102-112, 2010.

A. F. Macaskill, J. E. Rinholm, A. E. Twelvetrees, I. L. Arancibia-carcamo, J. Muir et al., Miro1 is a calcium sensor for glutamate receptor-dependent localization of mitochondria at synapses, Neuron, vol.61, pp.541-555, 2009.

S. Mai, M. Klinkenberg, G. Auburger, J. Bereiter-hahn, and M. Jendrach, Decreased expression of Drp1 and Fis1 mediates mitochondrial elongation in senescent cells and enhances resistance to oxidative stress through PINK1, J Cell Sci, vol.123, pp.917-926, 2010.

C. A. Mannella, Structure and dynamics of the mitochondrial inner membrane cristae, Biochim Biophys Acta, vol.1763, pp.542-548, 2006.

U. Manor, S. Bartholomew, G. Golani, E. Christenson, M. Kozlov et al., A mitochondria-anchored isoform of the actin-nucleating spire protein regulates mitochondrial division, 2015.

M. Martinez-vicente, Neuronal Mitophagy in Neurodegenerative Diseases, Front Mol Neurosci, vol.10, p.64, 2017.

H. M. Mcbride, M. Neuspiel, and S. Wasiak, Mitochondria: more than just a powerhouse, Curr Biol, vol.16, pp.551-560, 2006.

P. M. Mcclatchey, A. C. Keller, R. Bouchard, L. A. Knaub, and J. E. Reusch, Fully automated software for quantitative measurements of mitochondrial morphology, Mitochondrion, vol.26, pp.58-71, 2016.

C. J. Mcdermott, A. J. Grierson, J. D. Wood, M. Bingley, S. B. Wharton et al., Hereditary spastic paraparesis: disrupted intracellular transport associated with spastin mutation, Ann Neurol, vol.54, pp.748-759, 2003.

G. L. Mclelland, S. A. Lee, H. M. Mcbride, and E. A. Fon, Syntaxin-17 delivers PINK1/parkin-dependent mitochondrial vesicles to the endolysosomal system, J Cell Biol, vol.214, pp.275-291, 2016.

M. A. Mcnally, L. Soane, B. A. Roelofs, A. L. Hartman, and J. M. Hardwick, The N-terminal helix of Bcl-xL targets mitochondria, Mitochondrion, vol.13, pp.119-124, 2013.

S. Meeusen, J. M. Mccaffery, and J. Nunnari, Mitochondrial fusion intermediates revealed in vitro, Science, vol.305, pp.1747-1752, 2004.

I. Melentijevic, M. L. Toth, M. L. Arnold, R. J. Guasp, G. Harinath et al., 2017. C. elegans neurons jettison protein aggregates and mitochondria under neurotoxic stress, Nature, vol.542, pp.367-371

K. E. Miller, X. A. Liu, and S. V. Puthanveettil, Automated measurement of fast mitochondrial transport in neurons, Front Cell Neurosci, vol.9, p.435, 2015.

P. Mishra, V. Carelli, G. Manfredi, and D. C. Chan, Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation, Cell Metab, vol.19, pp.630-641, 2014.

K. Mitra, C. Wunder, B. Roysam, G. Lin, and J. Lippincott-schwartz, A hyperfused mitochondrial state achieved at G1-S regulates cyclin E buildup and entry into S phase, Proc Natl Acad Sci U S A, vol.106, pp.11960-11965, 2009.

A. S. Moore, Y. C. Wong, C. L. Simpson, and E. L. Holzbaur, Dynamic actin cycling through mitochondrial subpopulations locally regulates the fission-fusion balance within mitochondrial networks, Nat Commun, vol.7, p.12886, 2016.

M. Moran, H. Rivera, M. Sanchez-arago, A. Blazquez, B. Merinero et al., Mitochondrial bioenergetics and dynamics interplay in complex I-deficient fibroblasts, Biochim Biophys Acta, vol.1802, pp.443-453, 2010.

R. L. Morris and P. J. Hollenbeck, The regulation of bidirectional mitochondrial transport is coordinated with axonal outgrowth, J Cell Sci, vol.104, pp.917-927, 1993.

R. L. Morris and P. J. Hollenbeck, Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons, J Cell Biol, vol.131, pp.1315-1326, 1995.

N. Motoyama, F. Wang, K. A. Roth, H. Sawa, K. Nakayama et al., Massive cell death of immature hematopoietic cells and neurons in Bcl-x-deficient mice, Science, vol.267, pp.1506-1510, 1995.

M. Muller, S. L. Mironov, M. V. Ivannikov, J. Schmidt, and D. W. Richter, Mitochondrial organization and motility probed by two-photon microscopy in cultured mouse brainstem neurons, Exp Cell Res, vol.303, pp.114-127, 2005.

T. Murakawa, O. Yamaguchi, A. Hashimoto, S. Hikoso, T. Takeda et al., Bcl-2-like protein 13 is a mammalian Atg32 homologue that mediates mitophagy and mitochondrial fragmentation, Nat Commun, vol.6, p.7527, 2015.

K. Nakada, K. Inoue, T. Ono, K. Isobe, A. Ogura et al., Inter-mitochondrial complementation: Mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA, Nat Med, vol.7, pp.934-940, 2001.

A. Nakamura, V. Swahari, C. Plestant, I. Smith, E. Mccoy et al., Bcl-xL Is Essential for the Survival and Function of Differentiated Neurons in the Cortex That Control Complex Behaviors, J Neurosci, vol.36, pp.5448-5461, 2016.

B. R. Narayanareddy, S. Vartiainen, N. Hariri, D. K. O'dowd, and S. P. Gross, A biophysical analysis of mitochondrial movement: differences between transport in neuronal cell bodies versus processes, Traffic, vol.15, pp.762-771, 2014.

D. Narendra, A. Tanaka, D. F. Suen, and R. J. Youle, Parkin is recruited selectively to impaired mitochondria and promotes their autophagy, J Cell Biol, vol.183, pp.795-803, 2008.

C. M. Nasrallah and T. L. Horvath, Mitochondrial dynamics in the central regulation of metabolism, Nat Rev Endocrinol, vol.10, pp.650-658, 2014.

J. Nikolaisen, L. I. Nilsson, I. K. Pettersen, P. H. Willems, J. B. Lorens et al., Automated quantification and integrative analysis of 2D and 3D mitochondrial shape and network properties, PLoS One, vol.9, 2014.

J. Nixon-abell, C. J. Obara, A. V. Weigel, D. Li, W. R. Legant et al., Increased spatiotemporal resolution reveals highly dynamic dense tubular matrices in the peripheral ER, Science, vol.354, 2016.

T. Noguchi, M. Koizumi, and S. Hayashi, Sustained elongation of sperm tail promoted by local remodeling of giant mitochondria in Drosophila, Curr Biol, vol.21, pp.805-814, 2011.

I. Novak, V. Kirkin, D. G. Mcewan, J. Zhang, P. Wild et al., Nix is a selective autophagy receptor for mitochondrial clearance, EMBO Rep, vol.11, pp.45-51, 2010.

T. Nozaki, Y. Kagaya, N. Ishide, S. Kitada, M. Miura et al., Interaction between sarcomere and mitochondrial length in normoxic and hypoxic rat ventricular papillary muscles, Cardiovasc Pathol, vol.10, pp.125-132, 2001.

J. Nunnari and A. Suomalainen, Mitochondria: in sickness and in health, Cell, vol.148, pp.1145-1159, 2012.

J. W. O'neill, M. K. Manion, B. Maguire, and D. M. Hockenbery, BCL-XL dimerization by three-dimensional domain swapping, J Mol Biol, vol.356, pp.367-381, 2006.

B. Oettinghaus, D. D'alonzo, E. Barbieri, L. M. Restelli, C. Savoia et al., DRP1-dependent apoptotic mitochondrial fission occurs independently of BAX, BAK and APAF1 to amplify cell death by BID and oxidative stress, Biochim Biophys Acta, vol.1857, pp.1267-1276, 2016.

D. Ofengeim, Y. B. Chen, T. Miyawaki, H. Li, S. Sacchetti et al., Nterminally cleaved Bcl-xL mediates ischemia-induced neuronal death, Nat Neurosci, vol.15, pp.574-580, 2012.

A. Olichon, L. Baricault, N. Gas, E. Guillou, A. Valette et al., Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis, J Biol Chem, vol.278, pp.7743-7746, 2003.

T. Oltersdorf, S. W. Elmore, A. R. Shoemaker, R. C. Armstrong, D. J. Augeri et al., An inhibitor of Bcl-2 family proteins induces regression of solid tumours, Nature, vol.435, pp.677-681, 2005.

B. Onfelt, S. Nedvetzki, R. K. Benninger, M. A. Purbhoo, S. Sowinski et al., Structurally distinct membrane nanotubes between human macrophages support long-distance vesicular traffic or surfing of bacteria, J Immunol, vol.177, pp.8476-8483, 2006.

T. Ono, K. Isobe, K. Nakada, and J. I. Hayashi, Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria, Nat Genet, vol.28, pp.272-275, 2001.

H. Otera, C. Wang, M. M. Cleland, K. Setoguchi, S. Yokota et al., Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells, J Cell Biol, vol.191, pp.1141-1158, 2010.

C. S. Palmer, L. D. Osellame, D. Stojanovski, and M. T. Ryan, The regulation of mitochondrial morphology: intricate mechanisms and dynamic machinery, Cell Signal, vol.23, pp.1534-1545, 2011.

S. Pattingre, A. Tassa, X. Qu, R. Garuti, X. H. Liang et al., Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy, Cell, vol.122, pp.927-939, 2005.

M. M. Pearce, E. J. Spartz, W. Hong, L. Luo, and R. R. Kopito, Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain, Nat Commun, vol.6, p.6768, 2015.

D. Pendin, J. A. Mcnew, and A. Daga, Balancing ER dynamics: shaping, bending, severing, and mending membranes, Curr Opin Cell Biol, vol.23, pp.435-442, 2011.

J. Y. Peng, C. C. Lin, Y. J. Chen, L. S. Kao, Y. C. Liu et al., Automatic morphological subtyping reveals new roles of caspases in mitochondrial dynamics, PLoS Comput Biol, vol.7, p.1002212, 2011.

R. M. Perciavalle, D. P. Stewart, B. Koss, J. Lynch, S. Milasta et al., Anti-apoptotic MCL-1 localizes to the mitochondrial matrix and couples mitochondrial fusion to respiration, Nat Cell Biol, vol.14, pp.575-583, 2012.

A. M. Petros, E. T. Olejniczak, and S. W. Fesik, Structural biology of the Bcl-2 family of proteins, Biochim Biophys Acta, vol.1644, pp.83-94, 2004.

M. Picard, M. J. Mcmanus, G. Csordas, P. Varnai, G. W. Dorn et al., Trans-mitochondrial coordination of cristae at regulated membrane junctions, Nat Commun, vol.6, p.6259, 2015.

G. Pigino, G. Morfini, A. Pelsman, M. P. Mattson, S. T. Brady et al., Alzheimer's presenilin 1 mutations impair kinesin-based axonal transport, J Neurosci, vol.23, pp.4499-4508, 2003.

A. D. Pilling, D. Horiuchi, C. M. Lively, and W. M. Saxton, Kinesin-1 and Dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons, Mol Biol Cell, vol.17, pp.2057-2068, 2006.

O. Y. Pletjushkina, K. G. Lyamzaev, E. N. Popova, O. K. Nepryakhina, O. Y. Ivanova et al., Effect of oxidative stress on dynamics of mitochondrial reticulum, Biochim Biophys Acta, vol.1757, pp.518-524, 2006.

V. A. Popkov, E. Y. Plotnikov, K. G. Lyamzaev, D. N. Silachev, L. D. Zorova et al., Biochemistry (Mosc), vol.80, pp.532-541, 2015.

V. Popov, N. I. Medvedev, H. A. Davies, and M. G. Stewart, Mitochondria form a filamentous reticular network in hippocampal dendrites but are present as discrete bodies in axons: a three-dimensional ultrastructural study, J Comp Neurol, vol.492, pp.50-65, 2005.

J. W. Posakony, J. M. England, and G. Attardi, Mitochondrial growth and division during the cell cycle in HeLa cells, J Cell Biol, vol.74, pp.468-491, 1977.

M. Quintero, S. L. Colombo, A. Godfrey, and S. Moncada, Mitochondria as signaling organelles in the vascular endothelium, Proc Natl Acad Sci U S A, vol.103, pp.5379-5384, 2006.

S. M. Rafelski, Mitochondrial network morphology: building an integrative, geometrical view, BMC Biol, vol.11, p.71, 2013.

S. M. Rafelski and W. F. Marshall, Building the cell: design principles of cellular architecture, Nat Rev Mol Cell Biol, vol.9, pp.593-602, 2008.

S. M. Rafelski, M. P. Viana, Y. Zhang, Y. H. Chan, K. S. Thorn et al., Mitochondrial network size scaling in budding yeast, Science, vol.338, pp.822-824, 2012.

A. S. Rambold, B. Kostelecky, N. Elia, and J. Lippincott-schwartz, Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation, Proc Natl Acad Sci U S A, vol.108, pp.10190-10195, 2011.

J. C. Reed, Proapoptotic multidomain Bcl-2/Bax-family proteins: mechanisms, physiological roles, and therapeutic opportunities, Cell Death Differ, vol.13, pp.1378-1386, 2006.

G. L. Rintoul, A. J. Filiano, J. B. Brocard, G. J. Kress, and I. J. Reynolds, Glutamate decreases mitochondrial size and movement in primary forebrain neurons, J Neurosci, vol.23, pp.7881-7888, 2003.

G. Rojo, M. Chamorro, M. L. Salas, E. Vinuela, J. M. Cuezva et al., Migration of mitochondria to viral assembly sites in African swine fever virus-infected cells, J Virol, vol.72, pp.7583-7588, 1998.

K. A. Roth, C. Kuan, T. F. Haydar, C. D'sa-eipper, K. S. Shindler et al., Epistatic and independent functions of caspase-3 and Bcl-X(L) in developmental programmed cell death, Proc Natl Acad Sci U S A, vol.97, pp.466-471, 2000.

M. Roy, P. H. Reddy, M. Iijima, and H. Sesaki, Mitochondrial division and fusion in metabolism, Curr Opin Cell Biol, vol.33, pp.111-118, 2015.

E. I. Rugarli and T. Langer, Mitochondrial quality control: a matter of life and death for neurons, EMBO J, vol.31, pp.1336-1349, 2012.

Y. Rui, P. Tiwari, Z. Xie, and J. Q. Zheng, Acute impairment of mitochondrial trafficking by beta-amyloid peptides in hippocampal neurons, J Neurosci, vol.26, pp.10480-10487, 2006.

A. Santel, S. Frank, B. Gaume, M. Herrler, R. J. Youle et al., Mitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells, J Cell Sci, vol.116, pp.2763-2774, 2003.

M. Saotome, D. Safiulina, G. Szabadkai, S. Das, A. Fransson et al., Bidirectional Ca2+-dependent control of mitochondrial dynamics by the Miro GTPase, Proc Natl Acad Sci U S A, vol.105, pp.20728-20733, 2008.

F. Scholkmann, Long range physical cell-to-cell signalling via mitochondria inside membrane nanotubes: a hypothesis, Theor Biol Med Model, vol.13, p.16, 2016.

E. A. Schon and S. Przedborski, Mitochondria: the next (neurode)generation, Neuron, vol.70, pp.1033-1053, 2011.

H. Sesaki and R. E. Jensen, Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape, J Cell Biol, vol.147, pp.699-706, 1999.

L. Shao, P. Kner, E. H. Rego, and M. G. Gustafsson, Super-resolution 3D microscopy of live whole cells using structured illumination, Nat Methods, vol.8, pp.1044-1046, 2011.

S. H. Shim, C. Xia, G. Zhong, H. P. Babcock, J. C. Vaughan et al., Super-resolution fluorescence imaging of organelles in live cells with photoswitchable membrane probes, Proc Natl Acad Sci U S A, vol.109, pp.13978-13983, 2012.

K. S. Shindler, A. M. Yunker, R. Cahn, J. Zha, S. J. Korsmeyer et al., Trophic support promotes survival of bcl-x-deficient telencephalic cells in vitro, Cell Death Differ, vol.5, pp.901-910, 1998.

T. Shutt, M. Geoffrion, R. Milne, and H. M. Mcbride, The intracellular redox state is a core determinant of mitochondrial fusion, EMBO Rep, vol.13, pp.909-915, 2012.

V. P. Skulachev, Mitochondrial filaments and clusters as intracellular powertransmitting cables, Trends Biochem Sci, vol.26, pp.23-29, 2001.

E. Smirnova, D. L. Shurland, S. N. Ryazantsev, and A. M. Van-der-bliek, A human dynaminrelated protein controls the distribution of mitochondria, J Cell Biol, vol.143, pp.351-358, 1998.

Z. Song, H. Chen, M. Fiket, C. Alexander, and D. C. Chan, OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L, J Cell Biol, vol.178, pp.749-755, 2007.

V. Soubannier, P. Rippstein, B. A. Kaufman, E. A. Shoubridge, and H. M. Mcbride, Reconstitution of mitochondria derived vesicle formation demonstrates selective enrichment of oxidized cargo, PLoS One, vol.7, p.52830, 2012.

F. Stavru, A. E. Palmer, C. Wang, R. J. Youle, and P. Cossart, Atypical mitochondrial fission upon bacterial infection, Proc Natl Acad Sci U S A, vol.110, pp.16003-16008, 2013.

T. L. Stephen, N. F. Higgs, D. F. Sheehan, S. Awabdh, G. Lopez-domenech et al., Miro1 Regulates Activity-Driven Positioning of Mitochondria within Astrocytic Processes Apposed to Synapses to Regulate Intracellular Calcium Signaling, J Neurosci, vol.35, pp.15996-16011, 2015.

T. M. Stepkowski, S. Meczynska-wielgosz, and M. Kruszewski, mitoLUHMES: An Engineered Neuronal Cell Line for the Analysis of the Motility of Mitochondria, Cell Mol Neurobiol, 2016.

R. Stoica, K. J. De-vos, S. Paillusson, S. Mueller, R. M. Sancho et al., ER-mitochondria associations are regulated by the VAPB-PTPIP51 interaction and are disrupted by ALS/FTD-associated TDP-43, Nat Commun, vol.5, p.3996, 2014.

R. S. Stowers, L. J. Megeath, J. Gorska-andrzejak, I. A. Meinertzhagen, and T. L. Schwarz, Axonal transport of mitochondria to synapses depends on milton, a novel Drosophila protein, Neuron, vol.36, pp.1063-1077, 2002.

K. Stuart, Mitochondrial DNA of an African trypanosome, J Cell Biochem, vol.23, pp.13-26, 1983.

A. Sugiura, S. Mattie, J. Prudent, and H. M. Mcbride, Newly born peroxisomes are a hybrid of mitochondrial and ER-derived pre-peroxisomes, Nature, vol.542, pp.251-254, 2017.

A. Sugiura, G. L. Mclelland, E. A. Fon, and H. M. Mcbride, A new pathway for mitochondrial quality control: mitochondrial-derived vesicles, EMBO J, vol.33, pp.2142-2156, 2014.

T. C. Sung, C. Y. Li, Y. C. Lai, C. L. Hung, O. Shih et al., Solution Structure of Apoptotic BAX Oligomer: Oligomerization Likely Precedes Membrane Insertion, Structure, vol.23, pp.1878-1888, 2015.

M. C. Tal, M. Sasai, H. K. Lee, B. Yordy, G. S. Shadel et al., Absence of autophagy results in reactive oxygen species-dependent amplification of RLR signaling, Proc Natl Acad Sci U S A, vol.106, pp.2770-2775, 2009.

Y. Tanaka, Y. Kanai, Y. Okada, S. Nonaka, S. Takeda et al., Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria, Cell, vol.93, pp.1147-1158, 1998.

H. L. Tang, H. M. Tang, M. C. Fung, and J. M. Hardwick, In vivo CaspaseTracker biosensor system for detecting anastasis and non-apoptotic caspase activity, Sci Rep, vol.5, p.9015, 2015.

E. Thies and E. M. Mandelkow, Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1, J Neurosci, vol.27, pp.2896-2907, 2007.

Q. Tieu and J. Nunnari, Mdv1p is a WD repeat protein that interacts with the dynaminrelated GTPase, Dnm1p, to trigger mitochondrial division, J Cell Biol, vol.151, pp.353-366, 2000.

E. Trushina, R. B. Dyer, J. D. Badger, D. Ure, L. Eide et al., Mutant huntingtin impairs axonal trafficking in mammalian neurons in vivo and in vitro, Mol Cell Biol, vol.24, pp.8195-8209, 2004.

G. Twig, A. Elorza, A. J. Molina, H. Mohamed, J. D. Wikstrom et al., Fission and selective fusion govern mitochondrial segregation and elimination by autophagy, EMBO J, vol.27, pp.433-446, 2008.

S. B. Vafai and V. K. Mootha, Mitochondrial disorders as windows into an ancient organelle, Nature, vol.491, pp.374-383, 2012.

J. G. Valero, L. Sancey, J. Kucharczak, Y. Guillemin, D. Gimenez et al., Bax-derived membrane-active peptides act as potent and direct inducers of apoptosis in cancer cells, J Cell Sci, vol.124, pp.556-564, 2011.
URL : https://hal.archives-ouvertes.fr/inserm-00559538

J. Van-blerkom and P. Davis, High-polarized (Delta Psi m(HIGH)) mitochondria are spatially polarized in human oocytes and early embryos in stable subplasmalemmal domains: developmental significance and the concept of vanguard mitochondria, Reprod Biomed Online, vol.13, pp.246-254, 2006.

A. M. Van-der-bliek, Fussy mitochondria fuse in response to stress, EMBO J, vol.28, pp.1533-1534, 2009.

A. M. Van-der-bliek, Q. Shen, and S. Kawajiri, Mechanisms of mitochondrial fission and fusion, Cold Spring Harb Perspect Biol, vol.5, 2013.

V. S. Van-laar, B. Arnold, S. J. Cassady, C. T. Chu, E. A. Burton et al., Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization, Hum Mol Genet, vol.20, pp.927-940, 2011.

V. S. Van-laar, N. Roy, A. Liu, S. Rajprohat, B. Arnold et al., Glutamate excitotoxicity in neurons triggers mitochondrial and endoplasmic reticulum accumulation of Parkin, and, in the presence of N-acetyl cysteine, mitophagy, Neurobiol Dis, vol.74, pp.180-193, 2015.

J. R. Vanstone, A. M. Smith, S. Mcbride, T. Naas, M. Holcik et al., DNM1L-related mitochondrial fission defect presenting as refractory epilepsy, Eur J Hum Genet, vol.24, pp.1084-1088, 2016.

E. S. Vincow, G. Merrihew, R. E. Thomas, N. J. Shulman, R. P. Beyer et al., The PINK1-Parkin pathway promotes both mitophagy and selective respiratory chain turnover in vivo, Proc Natl Acad Sci U S A, vol.110, pp.6400-6405, 2013.

C. Vinegoni, L. Swisher, C. Fumene-feruglio, P. Giedt, R. J. Rousso et al., Real-time high dynamic range laser scanning microscopy, Nat Commun, vol.7, p.11077, 2016.

K. Voelz, S. A. Johnston, L. M. Smith, R. A. Hall, A. Idnurm et al., Division of labour' in response to host oxidative burst drives a fatal Cryptococcus gattii outbreak, Nat Commun, vol.5, p.5194, 2014.

J. Vowinckel, J. Hartl, R. Butler, and M. Ralser, MitoLoc: A method for the simultaneous quantification of mitochondrial network morphology and membrane potential in single cells, Mitochondrion, vol.24, pp.77-86, 2015.

T. Wai and T. Langer, Mitochondrial Dynamics and Metabolic Regulation, Trends Endocrinol Metab, vol.27, pp.105-117, 2016.

C. Wang, W. Du, Q. P. Su, M. Zhu, P. Feng et al., Dynamic tubulation of mitochondria drives mitochondrial network formation, Cell Res, vol.25, pp.1108-1120, 2015.

N. Wang, K. Naruse, D. Stamenovic, J. J. Fredberg, S. M. Mijailovich et al., Mechanical behavior in living cells consistent with the tensegrity model, Proc Natl Acad Sci U S A, vol.98, pp.7765-7770, 2001.

X. Wang and T. L. Schwarz, The mechanism of Ca2+ -dependent regulation of kinesinmediated mitochondrial motility, Cell, vol.136, pp.163-174, 2009.

W. Watanabe, T. Shimada, S. Matsunaga, D. Kurihara, K. Fukui et al., Single-organelle tracking by two-photon conversion, Opt Express, vol.15, pp.2490-2498, 2007.

H. R. Waterham, J. Koster, C. W. Van-roermund, P. A. Mooyer, R. J. Wanders et al., A lethal defect of mitochondrial and peroxisomal fission, N Engl J Med, vol.356, pp.1736-1741, 2007.

D. Weaver, V. Eisner, X. Liu, P. Varnai, L. Hunyady et al., Distribution and apoptotic function of outer membrane proteins depend on mitochondrial fusion, Mol Cell, vol.54, pp.870-878, 2014.

Y. Wei, W. C. Chiang, R. Sumpter, . Jr, P. Mishra et al., Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor, Cell, vol.168, p.210, 2017.

B. Westermann, Bioenergetic role of mitochondrial fusion and fission, Biochim Biophys Acta, vol.1817, pp.1833-1838, 2012.

D. Westphal, R. M. Kluck, and G. Dewson, Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis, Cell Death Differ, vol.21, pp.196-205, 2014.

L. M. Westrate, J. A. Drocco, K. R. Martin, W. S. Hlavacek, and J. P. Mackeigan, Mitochondrial morphological features are associated with fission and fusion events, PLoS One, vol.9, p.95265, 2014.

C. White, C. Li, J. Yang, N. B. Petrenko, M. Madesh et al., The endoplasmic reticulum gateway to apoptosis by Bcl-X(L) modulation of the InsP3R, Nat Cell Biol, vol.7, pp.1021-1028, 2005.

L. Wiemerslage and D. Lee, Quantification of mitochondrial morphology in neurites of dopaminergic neurons using multiple parameters, J Neurosci Methods, vol.262, pp.56-65, 2016.

T. J. Wilson, A. M. Slupe, and S. Strack, Cell signaling and mitochondrial dynamics: Implications for neuronal function and neurodegenerative disease, Neurobiol Dis, vol.51, pp.13-26, 2013.

K. Xiao, W. Zhao, L. Zhou, and D. C. Chang, Alpha 5/6 helix domains together with Nterminus determine the apoptotic potency of the Bcl-2 family proteins, Apoptosis, vol.21, pp.1214-1226, 2016.

Q. Xie, Q. Wu, C. M. Horbinski, W. A. Flavahan, K. Yang et al., Mitochondrial control by DRP1 in brain tumor initiating cells, Nat Neurosci, vol.18, pp.501-510, 2015.

S. I. Yamashita, X. Jin, K. Furukawa, M. Hamasaki, A. Nezu et al., Mitochondrial division occurs concurrently with autophagosome formation but independently of Drp1 during mitophagy, J Cell Biol, vol.215, pp.649-665, 2016.

K. Yasuda, T. Ishii, H. Suda, A. Akatsuka, P. S. Hartman et al., Age-related changes of mitochondrial structure and function in Caenorhabditis elegans, Mech Ageing Dev, vol.127, pp.763-770, 2006.

C. H. Yi, H. Pan, J. Seebacher, I. H. Jang, S. G. Hyberts et al., Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival, Cell, vol.146, pp.607-620, 2011.

M. Yi, D. Weaver, and G. Hajnoczky, Control of mitochondrial motility and distribution by the calcium signal: a homeostatic circuit, J Cell Biol, vol.167, pp.661-672, 2004.

R. J. Youle and D. P. Narendra, Mechanisms of mitophagy, Nat Rev Mol Cell Biol, vol.12, pp.9-14, 2011.

R. J. Youle and A. Strasser, The BCL-2 protein family: opposing activities that mediate cell death, Nat Rev Mol Cell Biol, vol.9, pp.47-59, 2008.

A. U. Zaidi, C. D'sa-eipper, J. Brenner, K. Kuida, T. S. Zheng et al., Bcl-X(L)-caspase-9 interactions in the developing nervous system: evidence for multiple death pathways, J Neurosci, vol.21, pp.169-175, 2001.

J. Zhang, Y. B. Chen, J. M. Hardwick, M. I. Miller, C. Plachez et al., Magnetic resonance diffusion tensor microimaging reveals a role for Bcl-x in brain development and homeostasis, J Neurosci, vol.25, pp.1881-1888, 2005.

Y. Zhang, S. Iqbal, M. F. O'leary, K. J. Menzies, A. Saleem et al., Altered mitochondrial morphology and defective protein import reveal novel roles for Bax and/or Bak in skeletal muscle, Am J Physiol Cell Physiol, vol.305, pp.502-511, 2013.

Z. Zhang, S. Subramaniam, J. Kale, C. Liao, B. Huang et al., BH3-in-groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes, EMBO J, vol.35, pp.208-236, 2016.

J. Zhao, T. Liu, S. Jin, X. Wang, M. Qu et al., Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission, EMBO J, vol.30, pp.2762-2778, 2011.

L. Zheng, R. E. Anderson, M. P. Agbaga, E. B. Rucker, and Y. Z. Le, Loss of BCL-XL in rod photoreceptors: Increased susceptibility to bright light stress, Invest Ophthalmol Vis Sci, vol.47, pp.5583-5589, 2006.

Y. Zhu, S. Massen, M. Terenzio, V. Lang, S. Chen-lindner et al., Modulation of serines 17 and 24 in the LC3-interacting region of Bnip3 determines pro-survival mitophagy versus apoptosis, J Biol Chem, vol.288, pp.1099-1113, 2013.

K. E. Zinsmaier, M. Babic, and G. J. Russo, Mitochondrial transport dynamics in axons and dendrites, Results Probl Cell Differ, vol.48, pp.107-139, 2009.