10 resistance by abolishing mitochondrial ﬁssion mediated by dynamin-related protein-1,” Cancer Research, vol. 69, no. 2, pp. 492–500, 2009. [42] H. Chen, A. Chomyn, and D. C. Chan, “Disruption of fusion results in mitochondrial heterogeneity and dysfunction,” The Journal of Biological Chemistry, vol. 280, no. 28, pp. 26185–26192, 2005. [43] S. Pich, D. Bach, P. Briones et al., “The Charcot-Marie-Tooth type 2A gene product, Mfn2, up-regulates fuel oxidation through expression of OXPHOS system,” Human Molecular Genetics, vol. 14, no. 11, pp. 1405–1415, 2005. [44] S. Kobashigawa, K. Suzuki, and S. Yamashita, “Ionizing radiation accelerates Drp1-dependent mitochondrial ﬁssion, which involves delayed mitochondrial reactive oxygen species production in normal human ﬁbroblast-like cells,” Biochemical and Biophysical Research Communications, vol. 414, no. 4, pp. 795–800, 2011. [45] S. Campello, R. A. Lacalle, M. Bettella, S. Man˜es, L. Scorrano, and A. Viola, “Orchestration of lymphocyte chemotaxis by mitochondrial dynamics,” Journal of Experimental Medicine, vol. 203, no. 13, pp. 2879–2886, 2006. [46] C. R. Hackenbrock, “Ultrastructural bases for metabolically linked mechanical activity in mitochondria. I. Reversible ultrastructural changes with change in metabolic steady state in isolated liver mitochondria,” Journal of Cell Biology, vol. 30, no. 2, pp. 269–297, 1966. [47] C. R. Hackenbrock, “Energy-linked ultrastructural transformations in isolated liver mitochondria and mitoplasts. Preservation of conﬁgurations by freeze-cleaving compared to chemical ﬁxation,” Journal of Cell Biology, vol. 53, no. 2, pp. 450–465, 1972. [48] J. Chiche, M. Rouleau, P. Gounon, M. C. Brahimi-Horn, J. Pouysse´gur, and N. M. Mazure, “Hypoxic enlarged mito- chondria protect cancer cells from apoptotic stimuli,” Journal of Cellular Physiology, vol. 222, no. 3, pp. 648–657, 2010. [49] F. Legros, A. Lombe`s, P. Frachon, and M. Rojo, “Mitochon- drial fusion in human cells is eﬃcient, requires the inner membrane potential, and is mediated by mitofusins,” Molec- ular Biology of the Cell, vol. 13, no. 12, pp. 4343–4354, 2002. [50] G. Bernard, N. Bellance, D. James et al., “Mitochondrial bioenergetics and structural network organization,” Journal of Cell Science, vol. 120, no. 5, pp. 838–848, 2007. [51] S. Barni, L. Sciola, A. Spano, and P. Pippia, “Static cytoﬂuorometry and ﬂuorescence morphology of mitochondria and DNA in proliferating ﬁbroblasts,” Biotechnic and Histochemistry, vol. 71, no. 2, pp. 66–70, 1996. [52] D. H. Margineantu, W. Gregory Cox, L. Sundell, S. W. Sherwood, J. M. Beechem, and R. A. Capaldi, “Cell cycle dependent morphology changes and associated mitochon- drial DNA redistribution in mitochondria of human cell lines,” Mitochondrion, vol. 1, no. 5, pp. 425–435, 2002. [53] N. Taguchi, N. Ishihara, A. Jofuku, T. Oka, and K. Mihara, “Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial ﬁssion,” The Journal of Biological Chemistry, vol. 282, no. 15, pp. 11521–11529, 2007. [54] L. Behrend, G. Henderson, and R. M. Zwacka, “Reactive oxygen species in oncogenic transformation,” Biochemical Society Transactions, vol. 31, no. 6, pp. 1441–1444, 2003. [55] D. C. Wallace, “A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine,” Annual Review of Genetics, vol. 39, pp. 359–407, 2005. International Journal of Cell Biology [56] Y. Y. Chiang, S. L. Chen, Y. T. Hsiao et al., “Nuclear expression of dynamin-related protein 1 in lung adenocarcinomas,” Modern Pathology, vol. 22, no. 9, pp. 1139–1150, 2009. [57] J. P. White, K. A. Baltgalvis, M. J. Puppa, S. Sato, J. W. Baynes, and J. A. Carson, “Muscle oxidative capacity during IL-6- dependent cancer cachexia,” American Journal of Physiology, vol. 300, no. 2, pp. R201–R211, 2011. [58] D. M. Su, Q. Zhang, X. Wang et al., “Two types of human malignant melanoma cell lines revealed by expression patterns of mitochondrial and survival-apoptosis genes: implications for malignant melanoma therapy,” Molecular Cancer Therapeutics, vol. 8, no. 5, pp. 1292–1304, 2009. [59] A. Prigione, B. Fauler, R. Lurz, H. Lehrach, and J. Adjaye, “The senescence-related mitochondrial/oxidative stress pathway is repressed in human induced pluripotent stem cells,” Stem Cells, vol. 28, no. 4, pp. 721–733, 2010. [60] L. R. Todd, R. Gomathinayagam, and U. Sankar, “A novel Gfer-Drp1 link in preserving mitochondrial dynamics and function in pluripotent stem cells,” Autophagy, vol. 6, no. 6, pp. 821–822, 2010. [61] E. A. Schon and S. Przedborski, “Mitochondria: the next (neurode) generation,” Neuron, vol. 70, no. 6, pp. 1033–1053, 2011. [62] P. Verstreken, C. V. Ly, K. J. T. Venken, T. W. Koh, Y. Zhou, and H. J. Bellen, “Synaptic mitochondria are critical for mobilization of reserve pool vesicles at Drosophila neuromuscular junctions,” Neuron, vol. 47, no. 3, pp. 365–378, 2005. [63] P. J. Hollenbeck and W. M. Saxton, “The axonal transport of mitochondria,” Journal of Cell Science, vol. 118, no. 23, pp. 5411–5419, 2005. [64] G. B. Stokin, C. Lillo, T. L. Falzone et al., “Axonopathy and transport deﬁcits early in the pathogenesis of Alzheimer’s diseases,” Science, vol. 307, no. 5713, pp. 1282–1288, 2005. [65] K. J. De vos, A. L. Chapman, M. E. Tennant et al., “Familial amyotrophic lateral sclerosis-linked SOD1 mutants perturb fast axonal transport to reduce axonal mitochondria content,” Human Molecular Genetics, vol. 16, no. 22, pp. 2720–2728, 2007. [66] P. Shi, A. L. Stro¨m, J. Gal, and H. Zhu, “Eﬀects of ALS-related SOD1 mutants on dynein- and KIF5-mediated retrograde and anterograde axonal transport,” Biochimica et Biophysica Acta, vol. 1802, no. 9, pp. 707–716, 2010. [67] S. Millecamps, B. J. Gentil, F. Gros-Louis, G. Rouleau, and J. P. Julien, “Alsin is partially associated with centrosome in human cells,” Biochimica et Biophysica Acta, vol. 1745, no. 1, pp. 84–100, 2005. [68] X. Shan, P. M. Chiang, D. L. Price, and P. C. Wong, “Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 37, pp. 16325–16330, 2010. [69] X. Wang, B. Su, L. Zheng, G. Perry, M. A. Smith, and X. Zhu, “The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer’s disease,” Journal of Neurochemistry, vol. 109, no. 1, pp. 153–159, 2009. [70] X. Wang, B. Su, H. G. Lee et al., “Impaired balance of mitochondrial ﬁssion and fusion in Alzheimer’s disease,” Journal of Neuroscience, vol. 29, no. 28, pp. 9090–9103, 2009. [71] D. T. W. Chang, G. L. Rintoul, S. Pandipati, and I. J. Reynolds, “Mutant huntingtin aggregates impair mitochondrial