International Journal of Cell Biology mitochondrial morphology and cellular viability,” Human Molecular Genetics, vol. 17, no. 2, pp. 201–214, 2008. [11] S. Y. Choi, P. Huang, G. M. Jenkins, D. C. Chan, J. Schiller, and M. A. Frohman, “A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis,” Nature Cell Biology, vol. 8, no. 11, pp. 1255–1262, 2006. [12] C. Merkwirth, S. Dargazanli, T. Tatsuta et al., “Prohibitins control cell proliferation and apoptosis by regulating OPA1- dependent cristae morphogenesis in mitochondria,” Genes and Development, vol. 22, no. 4, pp. 476–488, 2008. [13] E. Smirnova, L. Griparic, D. L. Shurland, and A. M. Van der Bliek, “Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells,” Molecular Biology of the Cell, vol. 12, no. 8, pp. 2245–2256, 2001. [14] G. M. Cereghetti, A. Stangherlin, O. Martins De Brito et al., “Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 41, pp. 15803–15808, 2008. [15] J. A. Mears, L. L. Lackner, S. Fang, E. Ingerman, J. Nunnari, and J. E. Hinshaw, “Conformational changes in Dnm1 support a contractile mechanism for mitochondrial ﬁssion,” Nature Structural and Molecular Biology, vol. 18, no. 1, pp. 20–26, 2011. [16] M. Karbowski, S. Y. Jeong, and R. J. Youle, “Endophilin B1 is required for the maintenance of mitochondrial morphology,” Journal of Cell Biology, vol. 166, no. 7, pp. 1027–1039, 2004. [17] D. Tondera, F. Czauderna, K. Paulick, R. Schwarzer, J. Kauf- mann, and A. Santel, “The mitochondrial protein MTP18 contributes to mitochondrial ﬁssion in mammalian cells,” Journal of Cell Science, vol. 118, no. 14, pp. 3049–3059, 2005. [18] Y. Eura, N. Ishihara, T. Oka, and K. Mihara, “Identiﬁcation of a novel protein that regulates mitochondrial fusion by modulating mitofusin (Mfn) protein function,” Journal of Cell Science, vol. 119, no. 23, pp. 4913–4925, 2006. [19] L. Pedrola, A. Espert, X. Wu, R. Claramunt, M. E. Shy, and F. Palau, “GDAP1, the protein causing Charcot-Marie-Tooth disease type 4A, is expressed in neurons and is associated with mitochondria,” Human Molecular Genetics, vol. 14, no. 8, pp. 1087–1094, 2005. [20] H. Otera, C. Wang, M. M. Cleland et al., “Mﬀ is an essential factor for mitochondrial recruitment of Drp1 during mito- chondrial ﬁssion in mammalian cells,” Journal of Cell Biology, vol. 191, no. 6, pp. 1141–1158, 2010. [21] J. Zhao, T. Liu, S. Jin et al., “Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochon- drial fusion rather than ﬁssion,” The EMBO Journal, vol. 30, no. 14, pp. 2762–2778, 2011. [22] J. R. Friedman, L. L. Lackner, M. West, J. R. DiBenedetto, J. Nunnari, and G. K. Voeltz, “ER tubules mark sites of mitochondrial division,” Science, vol. 334, no. 6054, pp. 358– 362, 2011. [23] R. J. Youle and D. P. Narendra, “Mechanisms of mitophagy,” Nature Reviews Molecular Cell Biology, vol. 12, no. 1, pp. 9– 14, 2011. [24] D. P. Narendra, S. M. Jin, A. Tanaka et al., “PINK1 is selectively stabilized on impaired mitochondria to activate Parkin,” PLoS Biology, vol. 8, no. 1, Article ID e1000298, 2010. [25] D. Narendra, A. Tanaka, D. F. Suen, and R. J. Youle, “Parkin is recruited selectively to impaired mitochondria and promotes their autophagy,” Journal of Cell Biology, vol. 183, no. 5, pp. 795–803, 2008. 9 [26] L. C. Gomes, G. D. Benedetto, and L. Scorrano, “During autophagy mitochondria elongate, are spared from degrada- tion and sustain cell viability,” Nature Cell Biology, vol. 13, no. 5, pp. 589–598, 2011. [27] T. Landes, L. J. Emorine, D. Courilleau, M. Rojo, P. Belenguer, and L. Arnaune´-Pelloquin, “The BH3-only Bnip3 binds to the dynamin Opa1 to promote mitochondrial fragmentation and apoptosis by distinct mechanisms,” EMBO Reports, vol. 11, no. 6, pp. 459–465, 2010. [28] V. Romanello, E. Guadagnin, L. Gomes et al., “Mitochondrial ﬁssion and remodelling contributes to muscle atrophy,” The EMBO Journal, vol. 29, no. 10, pp. 1774–1785, 2010. [29] M. V. Alavi, S. Bette, S. Schimpf et al., “A splice site mutation in the murine Opa1 gene features pathology of autosomal dominant optic atrophy,” Brain, vol. 130, no. 4, pp. 1029– 1042, 2007. [30] V. J. Davies, A. J. Hollins, M. J. Piechota et al., “Opa1 deﬁciency in a mouse model of autosomal dominant optic atrophy impairs mitochondrial morphology, optic nerve structure and visual function,” Human Molecular Genetics, vol. 16, no. 11, pp. 1307–1318, 2007. [31] N. Ishihara, M. Nomura, A. Jofuku et al., “Mitochondrial ﬁssion factor Drp1 is essential for embryonic development and synapse formation in mice,” Nature Cell Biology, vol. 11, no. 8, pp. 958–966, 2009. [32] D. Hanahan and R. A. Weinberg, “Hallmarks of cancer: the next generation,” Cell, vol. 144, no. 5, pp. 646–674, 2011. [33] B. Levine, S. Sinha, and G. Kroemer, “Bcl-2 family members: dual regulators of apoptosis and autophagy,” Autophagy, vol. 4, no. 5, pp. 600–606, 2008. [34] Y. Tsujimoto, L. R. Finger, and J. Yunis, “Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation,” Science, vol. 226, no. 4678, pp. 1097–1099, 1984. [35] A. Bakhshi, J. P. Jensen, and P. Goldman, “Cloning the chromosomal breakpoint of t(14;18) human lymphomas: clustering around J(H) on chromosome 14 and near a transcriptional unit on 18,” Cell, vol. 41, no. 3, pp. 899–906, 1985. [36] M. Crescenzi, M. Seto, G. P. Herzig, P. D. Weiss, R. C. Grif- ﬁth, and S. J. Korsmeyer, “Thermostable DNA polymerase chain ampliﬁcation of t(14;18) chromosome breakpoints and detection of minimal residual disease,” Proceedings of the National Academy of Sciences of the United States of America, vol. 85, no. 13, pp. 4869–4873, 1988. [37] 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,” Molecular Cell, vol. 21, no. 6, pp. 761–773, 2006. [38] H. Li, Y. Chen, A. F. Jones et al., “Bcl-xL induces Drp1- dependent synapse formation in cultured hippocampal neu- rons,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 6, pp. 2169–2174, 2008. [39] S. Wasiak, R. Zunino, and H. M. McBride, “Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death,” Journal of Cell Biology, vol. 177, no. 3, pp. 439–450, 2007. [40] M. Karbowski, K. L. Norris, M. M. Cleland, S. Y. Jeong, and R. J. Youle, “Role of Bax and Bak in mitochondrial morpho- genesis,” Nature, vol. 443, no. 7112, pp. 658–662, 2006. [41] J. X. Wang, Q. Li, and P. F. Li, “Apoptosis repressor with caspase recruitment domain contributes to chemotherapy