For general information on mitochondrial dynamics:

Chen, H., and Chan, D.C. (2017). Mitochondrial Dynamics in Regulating the Unique Phenotypes of Cancer and Stem Cells. Cell Metab 26, 39-48. [PDF]

Mishra, P., and Chan, D.C. (2016). Metabolic regulation of mitochondrial dynamics. J Cell Biol 212, 379-387. [PDF]

Carelli, V., and Chan, D.C. (2014). Mitochondrial DNA: impacting central and peripheral nervous systems. Neuron 84, 1126-1142. [PDF]

Mishra, P., and Chan, D.C. (2014). Mitochondrial dynamics and inheritance during cell division, development and disease. Nat Rev Mol Cell Biol 15, 634-646. [PDF]

Chan, D.C. (2012). Fusion and fission: interlinked processes critical for mitochondrial health. Annual Review of Genetics 46, 265-287. [PDF]

Chen, H., and Chan, D.C. (2009). Mitochondrial dynamics--fusion, fission, movement, and mitophagy--in neurodegenerative diseases. Hum Mol Genet 18, R169-176. [PDF]

Chan, D. C. (2006). Mitochondria: dynamic organelles in disease, aging, and development. Cell 125, 1241-1252. [PDF]


Selected Publications (see full publication list on PubMed)

Zhang, T., Mishra, P., Hay, B.A., Chan, D., and Guo, M. (2017). Valosin-containing protein (VCP/p97) inhibitors relieve Mitofusin-dependent mitochondrial defects due to VCP disease mutants. Elife 6.

Liu, R., and Chan, D.C. (2017). OPA1 and cardiolipin team up for mitochondrial fusion. Nat Cell Biol 19, 760-762. PMCID: PMC5757513. [PDF]

Cao, Y.L. et al. (2017). MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion. Nature 542, 372-376. [PDF]

Shin, C.S., Mishra, P., Watrous, J.D., Carelli, V., D'Aurelio, M., Jain, M., and Chan, D.C. (2017). The glutamate/cystine xCT antiporter antagonizes glutamine metabolism and reduces nutrient flexibility. Nat Commun 8, 15074. [PDF]

Del Dotto V, Mishra P, Vidoni S, Fogazza M, Maresca A, Caporali L, et al. (2017) OPA1 Isoforms in the Hierarchical Organization of Mitochondrial Functions. Cell Rep 20, 2557–71.

Rojansky, R., Cha, M.Y., and Chan, D.C. (2016). Elimination of paternal mitochondria in mouse embryos occurs through autophagic degradation dependent on PARKIN and MUL1. Elife 5. [PDF]

Toyama, E.Q. et al. (2016). Metabolism. AMP-activated protein kinase mediates mitochondrial fission in response to energy stress. Science 351, 275-281. [PDF]

Fahrner, J.A., Liu, R., Perry, M.S., Klein, J., and Chan, D.C. (2016). A novel de novo dominant negative mutation in DNM1L impairs mitochondrial fission and presents as childhood epileptic encephalopathy. Am J Med Genet A 170, 2002-2011. [PDF]

Chen, H., Ren, S., Clish, C., Jain, M., Mootha, V., McCaffery, J.M., and Chan, D.C. (2015). Titration of mitochondrial fusion rescues Mff-deficient cardiomyopathy. J Cell Biol 211, 795-805. [PDF]

Loson, O.C., Meng, S., Ngo, H., Liu, R., Kaiser, J.T., and Chan, D.C. (2015). Crystal structure and functional analysis of MiD49, a receptor for the mitochondrial fission protein Drp1. Protein Sci 24, 386-394. [PDF]

Liu, R., and Chan, D.C. (2015). The mitochondrial fission receptor Mff selectively recruits oligomerized Drp1. Mol Biol Cell 26, 4466-4477. [PDF]

Mishra, P., Varuzhanyan, G., Pham, A.H., and Chan, D.C. (2015). Mitochondrial Dynamics Is a Distinguishing Feature of Skeletal Muscle Fiber Types and Regulates Organellar Compartmentalization. Cell Metab 22, 1033-1044. [PDF]

Mishra, P., Carelli, V., Manfredi, G., and Chan, D.C. (2014). Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation. Cell Metabolism 19, 630-641. [PDF]

Loson, O.C., Liu, R., Rome, M.E., Meng, S., Kaiser, J.T., Shan, S.O., and Chan, D.C. (2014). The mitochondrial fission receptor MiD51 requires ADP as a cofactor. Structure 22, 367-377. [PDF]

Ngo, H.B., Lovely, G.A., Phillips, R., and Chan, D.C. (2014). Distinct structural features of TFAM drive mitochondrial DNA packaging versus transcriptional activation. Nature Communications 5, 3077. [PDF]

Chan, N.C., den Besten, W., Sweredoski, M.J., Hess, S., Deshaies, R.J., and Chan, D.C. (2014). Degradation of the Deubiquitinating Enzyme USP33 Is Mediated by p97 and the Ubiquitin Ligase HERC2. J Biol Chem 289, 19789-19798. [PDF]

Wang, Y.E., Marinov, G.K., Wold, B.J., and Chan, D.C. (2013). Genome-wide analysis reveals coating of the mitochondrial genome by TFAM. PloS One8, e74513. [PDF]

Loson, O.C., Song, Z., Chen, H., and Chan, D.C. (2013). Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission. Mol Biol Cell24, 659-667. [PDF]

Chan, D.C. (2012). Fusion and fission: interlinked processes critical for mitochondrial health. Annual Review of Genetics 46, 265-287. [PDF]

Pham, A.H., McCaffery, J.M., and Chan, D.C. (2012a). Mouse lines with photo-activatable mitochondria to study mitochondrial dynamics. Genesis 50, 833-843. [PDF]

Pham, A.H., Meng, S., Chu, Q.N., and Chan, D.C. (2012b). Loss of Mfn2 results in progressive, retrograde degeneration of dopaminergic neurons in the nigrostriatal circuit. Hum Mol Genet 21, 4817-4826. [PDF]

Chan, D.C., and Schon, E.A. (2012). Eliminating mitochondrial DNA from sperm. Dev Cell 22, 469-470. [PDF]

Zhang, Y., Chan, N.C., Ngo, H.B., Gristick, H., and Chan, D.C. (2012). Crystal structure of mitochondrial fission complex reveals scaffolding function for mitochondrial division 1 (Mdv1) coiled coil. J Biol Chem 287, 9855-9861. [PDF]

Aravin, A.A., and Chan, D.C. (2011). piRNAs meet mitochondria. Dev Cell 20, 287-288. [PDF]

Chan, N.C., and Chan, D.C. (2011). Parkin uses the UPS to ship off dysfunctional mitochondria. Autophagy 7, 771-772. 

Ngo, H.B., Kaiser, J.T., and Chan, D.C. (2011). The mitochondrial transcription and packaging factor Tfam imposes a U-turn on mitochondrial DNA. Nature structural & molecular biology 18, 1290-1296. [PDF]

Chan, N.C., Salazar, A.M., Pham, A.H., Sweredoski, M.J., Kolawa, N.J., Graham, R.L., Hess, S., and Chan, D.C. (2011). Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy. Hum Mol Genet 20, 1726-1737. [PDF]

Chen, H., Vermulst, M., Wang, Y.E., Chomyn, A., Prolla, T.A., McCaffery, J.M., Chan, D.C. (2010). Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutation. Cell 141, 280–289. [PDF]  

Ban, T., Heymann, JA., Song, Z., Hinshaw, JE., Chan, D.C. (2010). OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation. Hum Mol Genet. [PDF]

Song, Z., Ghochani, M., McCaffery, J.M., Frey, T.G., and Chan, D.C. (2009). Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion. Mol Biol Cell 20, 3525-353. [PDF]

Detmer, S.A., Velde, C.V., Cleveland, D.W., and Chan, D.C. (2008). Hindlimb gait defects due to motor axon loss and reduced distal muscles in a transgenic mouse model of Charcot-Marie-Tooth type 2A. Hum Mol Genet 17, 367-375. [PDF

Zhang, Y., and Chan, D.C. (2007). Structural basis for recruitment of mitochondrial fission complexes by Fis1. Proc Natl Acad Sci U S A 104, 18526-18530. [PDF]

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

Chen, H., McCaffery, J.M., and Chan, D.C. (2007). Mitochondrial fusion protects against neurodegeneration in the cerebellum. Cell 130, 548-562. [PDF

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

Chan, D.C. (2007). Mitochondrial dynamics in disease. The New England Journal of Medicine 356, 1707-1709. [PDF

Detmer, S. A., and Chan, D. C. (2007). Complementation between mouse Mfn1 and Mfn2 protects mitochondrial fusion defects caused by CMT2A disease mutations. J Cell Biol 176, 405-414. [PDF]

Chan, D. C. (2006). Mitochondria: dynamic organelles in disease, aging, and development. Cell 125, 1241-1252. [PDF]

Chan, D. C. (2006). Mitochondrial fusion and fission in mammals. Annu Rev Cell Dev Biol 22, 79-99. [PDF]

Griffin, E. E., Detmer, S. A., and Chan, D. C. (2006). Molecular mechanism of mitochondrial membrane fusion. Biochim Biophys Acta 1763, 482-489. [PDF]

Griffin, E. E., and Chan, D. C. (2006). Domain interactions within Fzo1 oligomers are essential for mitochondrial fusion. J Biol Chem 281, 16599-16606. [PDF]

Chen, H., and Chan, D. C. (2005). Emerging functions of mammalian mitochondrial fusion and fission. Hum Mol Genet 14 Spec No. 2, R283-289. [PDF]

Griffin, E. E., Graumann, J., and Chan, D. C. (2005). The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria. J Cell Biol 170, 237-248. [PDF]

Chen, H., Chomyn, A., and Chan, D. C. (2005). Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J Biol Chem 280, 26185-26192. [PDF]

Suntoke, T. R., and Chan, D. C. (2005). The fusion activity of HIV-1 gp41 depends on interhelical interactions. J Biol Chem 280, 19852-19857. [PDF]

Koshiba, T., Detmer, S. A., Kaiser, J. T., Chen, H., McCaffery, J. M., and Chan, D. C. (2004). Structural basis of mitochondrial tethering by mitofusin complexes. Science 305, 858-862. [PDF]

Karbowski, M., Arnoult, D., Chen, H., Chan, D. C., Smith, C. L., and Youle, R. J. (2004). Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis. J Cell Biol 164, 493-499. 

Chen, H., and Chan, D. C. (2004). Mitochondrial dynamics in mammals. Curr Top Dev Biol 59, 119-144. [PDF

Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., and Chan, D. C. (2003). Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J Cell Biol 160, 189-200. [PDF]

Koshiba, T., and Chan, D. C. (2003). The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions. J Biol Chem 278, 7573-7579. [PDF]

Chan, D. C., and Kim, P. S. (1998). HIV entry and its inhibition. Cell 93, 681-684. [PDF]

Chan, D. C., Chutkowski, C. T., and Kim, P. S. (1998). Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc Natl Acad Sci U S A 95, 15613-15617. [PDF]

Malashkevich, V. N., Chan, D. C., Chutkowski, C. T., and Kim, P. S. (1998). Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: conserved helical interactions underlie the broad inhibitory activity of gp41 peptides. Proc Natl Acad Sci U S A 95, 9134-9139.  [PDF]

Chan, D. C., Fass, D., Berger, J. M., and Kim, P. S. (1997). Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263-273. [PDF]