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Disturbed mitochondrial and peroxisomal dynamics due to loss of MFF causes Leigh-like encephalopathy, optic atrophy and peripheral neuropathy
Abstract
Background: Mitochondria are dynamic organelles which undergo continuous fission and fusion to maintain their diverse cellular functions. Components of the fission machinery are partly shared between mitochondria and peroxisomes, and inherited defects in two such components (dynamin-related protein (DRP1) and ganglioside-induced differentiation-associated protein 1 (GDAP1)) have been associated with human disease. Deficiency of a third component (mitochondrial fission factor, MFF) was recently reported in one index patient, rendering MFF another candidate disease gene within the expanding field of mitochondrial and peroxisomal dynamics. Here we investigated three new patients from two families with pathogenic mutations in MFF . Methods: The patients underwent clinical examination, brain MRI, and biochemical, cytological and molecular analyses, including exome sequencing. Results: The patients became symptomatic within the first year of life, exhibiting seizures, developmental delay and acquired microcephaly. Dysphagia, spasticity and optic and peripheral neuropathy developed subsequently. Brain MRI showed Leigh-like patterns with bilateral changes of the basal ganglia and subthalamic nucleus, suggestive of impaired mitochondrial energy metabolism. However, activities of mitochondrial respiratory chain complexes were found to be normal in skeletal muscle. Exome sequencing revealed three different biallelic loss-of-function variants in MFF in both index cases. Western blot studies of patient-derived fibroblasts indicated normal content of mitochondria and peroxisomes, whereas immunofluorescence staining revealed elongated mitochondria and peroxisomes. Furthermore, increased mitochondrial branching and an abnormal distribution of fission-mediating DRP1 were observed. Conclusions: Our findings establish MFF loss of function as a cause of disturbed mitochondrial and peroxisomal dynamics associated with early-onset Leigh-like basal ganglia disease. We suggest that, even if laboratory findings are not indicative of mitochondrial or peroxisomal dysfunction, the co-occurrence of optic and/or peripheral neuropathy with seizures warrants genetic testing for MFF mutations.
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Patients with mutations in the DRP1 receptor MFF suffer from developmental delay and acquired microcephaly, seizures, spasticity, and optic atrophy.
“Patients with mutations in the DRP1 receptor MFF, suffer from developmental delay and acquired microcephaly, seizures, spasticity, and optic atrophy [204, 205].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [205]
Citations
Cites
Fiji: an open-source platform for biological-image analysis
Schindelin, J., Arganda-Carreras, I., Frise, E., Kaynig, V., Longair, M., Pietzsch, T., Preibisch, S., Rueden, C., Saalfeld, S., Schmid, B., et al. (2012) · Nature Methods · doi:10.1038/nmeth.2019 · Cited by 66,890
Biochemical and molecular investigations in respiratory chain deficiencies
Rustin, P., Chrétien, D., Bourgeron, T., Gérard, B., Rötig, A., Saudubray, J., & Münnich, A. (1994) · Clinica Chimica Acta · doi:10.1016/0009-8981(94)90055-8 · Cited by 1,265
Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission
Losón, O. C., Song, Z., Chen, H., & Chan, D. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0721 · Cited by 1,235
Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007152 · Cited by 1,110
Ishihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S. O., Masuda, K., Otera, H., Nakanishi, Y., Nonaka, I., Goto, Y.-I., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1907 · Cited by 1,066
Gandre-Babbe, S., & van der Bliek, A. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1287 · Cited by 769
A Lethal Defect of Mitochondrial and Peroxisomal Fission
Waterham, H. R., Koster, J., van Roermund, C. W. T., Mooyer, P. A. W., Wanders, R. J. A., & Leonard, J. V. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa064436 · Cited by 749
Song, M., Mihara, K., Chen, Y., Scorrano, L., & Dorn, G. W. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.011 · Cited by 482
Haack, T. B., Hogarth, P., Kruer, M. C., Gregory, A., Wieland, T., Schwarzmayr, T., Graf, E., Sanford, L., Meyer, E., Kara, E., et al. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2012.10.019 · Cited by 360
Self-citationPeroxisome‐mitochondria interplay and disease
Schrader, M., Costello, J. L., Godinho, L. F., & Islinger, M. (2015) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-015-9819-7 · Cited by 231
Mutations in SLC25A46, encoding a UGO1-like protein, cause an optic atrophy spectrum disorder
Abrams, A. J., Hufnagel, R. B., Rebelo, A. P., Zanna, C., Patel, N., Gonzalez, M., Campeanu, I. J., Griffin, L. B., Groenewald, S., Strickland, A. V., et al. (2015) · Nature Genetics · doi:10.1038/ng.3354 · Cited by 215
Shamseldin, H. E., Alshammari, M., Al-Sheddi, T., Salih, M. A., Alkhalidi, H., Kentab, A., Repetto, G. M., Hashem, M., & Alkuraya, F. S. (2012) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2012-100836 · Cited by 182
Mitochondrial Phosphate–Carrier Deficiency: A Novel Disorder of Oxidative Phosphorylation
Mayr, J. A., Merkel, O., Kohlwein, S. D., Gebhardt, B. R., Böhles, H., Fötschl, U., Koch, J., Jaksch, M., Lochmüller, H., Horváth, R., et al. (2007) · The American Journal of Human Genetics · doi:10.1086/511788 · Cited by 167
Self-citationDecrease of mitochondrial DNA content and energy metabolism in renal cell carcinoma
Meierhofer, D. (2004) · Carcinogenesis · doi:10.1093/carcin/bgh104 · Cited by 164
HOLTZMAN, E., TEICHBERG, S., ABRAHAMS, S. J., CITKOWITZ, E., CRAIN, S. M., KAWAI, N., & PETERSON, E. R. (1973) · Journal of Histochemistry & Cytochemistry · doi:10.1177/21.4.349 · Cited by 146
Mitochondrial dynamics and inherited peripheral nerve diseases
Pareyson, D., Saveri, P., Sagnelli, A., & Piscosquito, G. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.04.001 · Cited by 128
A Bcl-xL–Drp1 complex regulates synaptic vesicle membrane dynamics during endocytosis
Li, H., Alavian, K. N., Lazrove, E., Mehta, N., Jones, A., Zhang, P., Licznerski, P., Graham, M. M., Uo, T., Guo, J., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2791 · Cited by 123
Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission
Richter, V., Palmer, C. S., Osellame, L. D., Singh, A. P., Elgass, K., Stroud, D. A., Sesaki, H., Kvansakul, M., & Ryan, M. T. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201311014 · Cited by 106
miR-761 regulates the mitochondrial network by targeting mitochondrial fission factor
Long, B., Wang, K., Li, N., Murtaza, I., Xiao, J. Y., Fan, Y. Y., Liu, C.-Y., Li, W. H., Cheng, Z., & Li, P. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.009 · Cited by 95
PEX11 proteins attract Mff and hFis1 to coordinate peroxisomal fission
Koch, J., & Brocard, C. (2012) · Journal of Cell Science · doi:10.1242/jcs.102178 · Cited by 86
Self-citationSevere depletion of mitochondrial DNA in spinal muscular atrophy
Berger, A., Mayr, J. A., Meierhofer, D., Fötschl, U., Bittner, R. E., Budka, H., Grethen, C., Huemer, M., Kofler, B., & Sperl, W. (2003) · Acta Neuropathologica · doi:10.1007/s00401-002-0638-1 · Cited by 82
Self-citationAlterations of oxidative phosphorylation complexes in astrocytomas
Feichtinger, R. G., Weis, S., Mayr, J. A., Zimmermann, F., Geilberger, R., Sperl, W., & Kofler, B. (2014) · Glia · doi:10.1002/glia.22621 · Cited by 76
Self-citationDerouiche, A., Haseleu, J., & Korf, H. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1563-8 · Cited by 75
Myelin peroxisomes–Essential organelles for the maintenance of white matter in the nervous system
Kassmann, C. M. (2014) · Biochimie · doi:10.1016/j.biochi.2013.09.020 · Cited by 72
A role for myelin-associated peroxisomes in maintaining paranodal loops and axonal integrity
Kassmann, C. M., Quintes, S., Rietdorf, J., Möbius, W., Sereda, M. W., Nientiedt, T., Saher, G., Baes, M., & Nave, K.-A. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.032 · Cited by 52
Bonekamp, N. A., Sampaio, P., de Abreu, F. V., Lüers, G. H., & Schrader, M. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01356.x · Cited by 38
Organelle Dynamics: ER Embraces Mitochondria for Fission
Westermann, B. (2011) · Current Biology · doi:10.1016/j.cub.2011.10.010 · Cited by 28
Neuroradiological findings expand the phenotype of OPA1-related mitochondrial dysfunction
Roubertie, A., Leboucq, N., Picot, M., Nogué, E., Brunel, H., Bars, E. L., Manès, G., Angebault, C., Blanchet, C., Mondain, M., et al. (2015) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2015.01.008 · Cited by 24
Respiratory chain deficiencies
de Lonlay, P., Rötig, A., & Sarnat, H. B. (2013) · Handbook of clinical neurology · doi:10.1016/b978-0-444-59565-2.00033-2 · Cited by 21
Rocca, M. A., Bianchi‐Marzoli, S., Messina, R., Cascavilla, M. L., Zeviani, M., Lamperti, C., Milesi, J., Carta, A., Cammarata, G., Leocani, L., et al. (2015) · Journal of Neurology · doi:10.1007/s00415-015-7696-5 · Cited by 7
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Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550
Mitochondrial Dynamics and Its Involvement in Disease
Chan, D. C. (2020) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012419-032711 · Cited by 1,416
Mitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397
Mitochondrial dynamics in adaptive and maladaptive cellular stress responses
Eisner, V., Picard, M., & Hajnóczky, G. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0133-0 · Cited by 622
Quality control of the mitochondrion
Ng, M. Y. W., Wai, T., & Simonsen, A. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.02.009 · Cited by 464
Function and regulation of the divisome for mitochondrial fission
Kraus, F., Roy, K., Pucadyil, T. J., & Ryan, M. T. (2021) · Nature · doi:10.1038/s41586-021-03214-x · Cited by 445
Mitochondrial Dynamics in Regulating the Unique Phenotypes of Cancer and Stem Cells
Chen, H., & Chan, D. C. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.05.016 · Cited by 454
The Peroxisome-Mitochondria Connection: How and Why?
Fransen, M., Lismont, C., & Walton, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061126 · Cited by 351
“Loss of MFF has been linked to mitochondrial encephalomyopathy [170] and early-onset Leigh-like encephalopathy, optic atrophy, and peripheral neuropathy [171]; and mutations in GDAP1 have been shown to cause Charcot-Marie-Tooth disease, the most common inherited peripheral neuropathy [172].”
BackgroundMitochondrial dynamics in health and disease
Yapa, N. M. B., Lisnyak, V., Reljić, B., & Ryan, M. T. (2021) · FEBS Letters · doi:10.1002/1873-3468.14077 · Cited by 323
Regulation of Mitochondrial ATP Production: Ca2+ Signaling and Quality Control
Boyman, L., Karbowski, M., & Lederer, W. J. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.10.007 · Cited by 310
Hu, C., Huang, Y., & Li, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010144 · Cited by 302
The peroxisome: an update on mysteries 2.0
Islinger, M., Völkl, A., Fahimi, H. D., & Schrader, M. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1722-5 · Cited by 296
ACBD5 and VAPB mediate membrane associations between peroxisomes and the ER
Costello, J. L., Castro, I. G., Hacker, C., Schrader, T. A., Metz, J., Zeuschner, D., Azadi, A. S., Godinho, L. F., Costina, V., Findeisen, P., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201607055 · Cited by 251
The physiological functions of human peroxisomes
Wanders, R. J. A., Baes, M., Ribeiro, D., Ferdinandusse, S., & Waterham, H. R. (2023) · Physiological Reviews · doi:10.1152/physrev.00051.2021 · Cited by 228
Mitochondrial dynamics and their potential as a therapeutic target
Whitley, B. N., Engelhart, E. A., & Hoppins, S. C. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.06.002 · Cited by 227
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197
Mitochondrial function in development and disease
Rossmann, M. P., Dubois, S. M., Agarwal, S., & Zon, L. I. (2021) · Disease Models & Mechanisms · doi:10.1242/dmm.048912 · Cited by 197
Zerihun, M., Sukumaran, S., & Qvit, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065785 · Cited by 195
Mitochondrial dysfunction in the regulation of aging and aging-related diseases
Zhang, X., Gao, Y., Zhang, S., Wang, Y., Pei, X., Chen, Y., Zhang, J., Zhang, Y., Du, Y., Hao, S., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02308-7 · Cited by 183
Organelle interplay-peroxisome interactions in health and disease.
Schrader, M., Kamoshita, M., & Islinger, M. (2020) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12083 · Cited by 149
Mechanisms and roles of mitochondrial localisation and dynamics in neuronal function
Seager, R., Lee, L. J., Henley, J. M., & Wilkinson, K. A. (2020) · Neuronal Signaling · doi:10.1042/ns20200008 · Cited by 150
Mitochondrial dynamics: Biological roles, molecular machinery, and related diseases
El‐Hattab, A. W., Suleiman, J., Almannai, M., & Scaglia, F. (2018) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2018.10.003 · Cited by 138
Mitochondrial Fission and Fusion: Molecular Mechanisms, Biological Functions, and Related Disorders
Ojaimi, M. A., Salah, A., & El‐Hattab, A. W. (2022) · Membranes · doi:10.3390/membranes12090893 · Cited by 130
Mitochondrial Morphofunction in Mammalian Cells
Bulthuis, E. P., Adjobo-Hermans, M. J. W., Willems, P. H. G. M., & Koopman, W. J. H. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7534 · Cited by 133
Long-Term Potentiation Requires a Rapid Burst of Dendritic Mitochondrial Fission during Induction
Divakaruni, S. S., Dyke, A. M. V., Chandra, R., LeGates, T. A., Contreras, M., Dharmasri, P. A., Higgs, H. N., Lobo, M. K., Thompson, S. M., & Blanpied, T. A. (2018) · Neuron · doi:10.1016/j.neuron.2018.09.025 · Cited by 130
Atkins, K., Dasgupta, A., Chen, K., Mewburn, J., & Archer, S. L. (2016) · Clinical Science · doi:10.1042/cs20160030 · Cited by 129
Kang, T. (2020) · Antioxidants · doi:10.3390/antiox9070617 · Cited by 120
Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells
Costello, J. L., Castro, I. G., Camões, F., Schrader, T. A., McNeall, D., Yang, J., Giannopoulou, E., Gomes, S. R. A. M., Pogenberg, V., Bonekamp, N. A., et al. (2017) · Journal of Cell Science · doi:10.1242/jcs.200204 · Cited by 115
The Maintenance of Mitochondrial DNA Integrity and Dynamics by Mitochondrial Membranes
Chapman, J., Ng, Y. S., & Nicholls, T. J. J. (2020) · Life · doi:10.3390/life10090164 · Cited by 100
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Castro, I. G., Richards, D. M., Metz, J., Costello, J. L., Passmore, J. B., Schrader, T. A., Gouveia, A., Ribeiro, D., & Schrader, M. (2018) · Traffic · doi:10.1111/tra.12549 · Cited by 84
Maintaining social contacts: The physiological relevance of organelle interactions
Silva, B. S. C., DiGiovanni, L. F., Kumar, R., Carmichael, R. E., Kim, P. K., & Schrader, M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118800 · Cited by 84
Biallelic Mutations in DNM1L are Associated with a Slowly Progressive Infantile Encephalopathy
Nasca, A., Legati, A., Baruffini, E., Nolli, C., Moroni, I., Ardissone, A., Goffrini, P., & Ghezzi, D. (2016) · Human Mutation · doi:10.1002/humu.23033 · Cited by 77
Peripheral neuropathy in complex inherited diseases: an approach to diagnosis
Rossor, A. M., Carr, A. S., Devine, H. E., Hoskote, C., Pelayo‐Negro, A. L., Pareyson, D., Shy, M. E., Scherer, S. S., & Reilly, M. M. (2017) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2016-313960 · Cited by 77
Mitochondrial division, fusion and degradation
Murata, D., Arai, K., Iijima, M., & Sesaki, H. (2019) · The Journal of Biochemistry · doi:10.1093/jb/mvz106 · Cited by 73
A novel mechanism causing imbalance of mitochondrial fusion and fission in human myopathies
Bartsakoulia, M., Pyle, A., Troncoso-Chandía, D., Vial-Brizzi, J., Paz-Fiblas, M. V., Duff, J., Griffin, H., Boczonadi, V., Lochmüller, H., Kleinle, S., et al. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy033 · Cited by 68
MAVS is energized by Mff which senses mitochondrial metabolism via AMPK for acute antiviral immunity
Hanada, Y., Ishihara, N., Wang, L., Otera, H., Ishihara, T., Koshiba, T., Mihara, K., Ogawa, Y., & Nomura, M. (2020) · Nature Communications · doi:10.1038/s41467-020-19287-7 · Cited by 68
Rahman, S. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-12-821751-1.00015-4 · Cited by 62
High‐throughput screening identifies suppressors of mitochondrial fragmentation in OPA1 fibroblasts
Cretin, E., Lopes, P. T., Vimont, E., Tatsuta, T., Langer, T., Gazi, A. D., Sachse, M., Yu‐Wai‐Man, P., Reynier, P., & Wai, T. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202013579 · Cited by 63
Measuring Mitochondrial Shape with ImageJ
Merrill, R. A., Flippo, K. H., & Strack, S. (2017) · Neuromethods · doi:10.1007/978-1-4939-6890-9_2 · Cited by 58
Regulating peroxisome–ER contacts via the ACBD5-VAPB tether by FFAT motif phosphorylation and GSK3β
Kors, S., Hacker, C., Bolton, C., Maier, R., Reimann, L., Kitchener, E. J. A., Warscheid, B., Costello, J. L., & Schrader, M. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202003143 · Cited by 58
Verrigni, D., Nottia, M. D., Ardissone, A., Baruffini, E., Nasca, A., Legati, A., Bellacchio, E., Fagiolari, G., Martinelli, D., Fusco, L., et al. (2019) · Human Mutation · doi:10.1002/humu.23729 · Cited by 53
The role of mitochondrial dynamics in mtDNA maintenance
Sabouny, R., & Shutt, T. E. (2021) · Journal of Cell Science · doi:10.1242/jcs.258944 · Cited by 51
Nottia, M. D., Verrigni, D., Torraco, A., Rizza, T., Bertini, E., & Carrozzo, R. (2021) · Genes · doi:10.3390/genes12020247 · Cited by 50
Is mitochondrial morphology important for cellular physiology?
Wai, T. (2024) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2024.05.005 · Cited by 50
Mitochondrial protein dysfunction in pathogenesis of neurological diseases
Wang, L., Yang, Z., He, X., Pu, S., Yang, C., Wu, Q., Zhou, Z., Cen, X., & Zhao, H. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.974480 · Cited by 47
The R941L mutation in MYH14 disrupts mitochondrial fission and associates with peripheral neuropathy
Almutawa, W., Smith, C., Sabouny, R., Smit, R. B., Zhao, T., Wong, R., Lee-Glover, L. P., Desrochers-Goyette, J., Ilamathi, H. S., Suchowersky, O., et al. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.06.018 · Cited by 45
The relevance of mitochondrial morphology for human disease
Navaratnarajah, T., Anand, R., Reichert, A. S., & Distelmaier, F. (2021) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2021.105951 · Cited by 49
Staying in Healthy Contact: How Peroxisomes Interact with Other Cell Organelles
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Clinical and Biochemical Features in a Patient With Mitochondrial Fission Factor Gene Alteration
Nasca, A., Nardecchia, F., Commone, A., Semeraro, M., Legati, A., Garavaglia, B., Ghezzi, D., & Leuzzi, V. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00625 · Cited by 42
Liu, A., Kage, F., & Higgs, H. N. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-04-0224 · Cited by 42
PEX11β and FIS1 cooperate in peroxisome division independently of mitochondrial fission factor
Schrader, T. A., Carmichael, R. E., Islinger, M., Costello, J. L., Hacker, C., Bonekamp, N. A., Weishaupt, J. H., Andersen, P. M., & Schrader, M. (2022) · Journal of Cell Science · doi:10.1242/jcs.259924 · Cited by 39
Multi-localized Proteins: The Peroxisome-Mitochondria Connection
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Passmore, J. B., Carmichael, R. E., Schrader, T. A., Godinho, L. F., Ferdinandusse, S., Lismont, C., Wang, Y.-H., Hacker, C., Islinger, M., Fransen, M., et al. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118709 · Cited by 38
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Magro, G., Laterza, V., & Tosto, F. (2025) · Biomedicines · doi:10.3390/biomedicines13030733 · Cited by 37
Oikawa, Y., Izumi, R., Koide, M., Hagiwara, Y., Kanzaki, M., Suzuki, N., Kikuchi, K., Matsuhashi, T., Akiyama, Y., Ichijo, M., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0231064 · Cited by 36
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Kyriakoudi, S., Drousiotou, A., & Petrou, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094617 · Cited by 33
Linker, S. B., Mendes, A. P. D., & Marchetto, M. C. (2020) · Molecular Autism · doi:10.1186/s13229-020-00359-w · Cited by 31
Mitochondrial quality control in the brain: The physiological and pathological roles
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Imoto, Y., Itoh, K., & Fujiki, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155452 · Cited by 27
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Iwama, K., Takaori, T., Fukushima, A., Tohyama, J., Ishiyama, A., Ohba, C., Mitsuhashi, S., Miyatake, S., Takata, A., Miyake, N., et al. (2018) · Journal of Human Genetics · doi:10.1038/s10038-017-0405-8 · Cited by 26
Chiaratti, M. R. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00891-w · Cited by 25
Μitochondrial Membrane Dynamics and Inherited Optic Neuropathies
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Metadata
- Authors
- Koch, J., Feichtinger, R. G., Freisinger, P., Pies, M., Schrödl, F., Iuso, A., Sperl, W., Mayr, J. A., Prokisch, H., & Haack, T. B.
- Affiliations
- Paracelsus Medical University (AT)
- Kreiskliniken Reutlingen (DE)
- Klinikum Frankfurt Höchst (DE)
- Department of Ophthalmology and Optometry, Department of Anatomy, Department of Laboratory Medicine (HW), and First Department of Internal Medicine, Paracelsus Medical University, Salzburg, Austria
- TUM Klinikum (DE)
- Corresponding author
- Koch, Johannes
- ORCID
- Venue
- Journal of Medical Genetics
- Publisher
- BMJ
- Published
- 2016-01-18
- Volume
- 53
- Issue
- 4
- Pages
- 270-278
- ISSN
- 0022-2593 (ISSN-L)
- 1468-6244
- OpenAlex
- W2298458814
- Cited by
- 127
- References
- 30
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 6 · 2023: 8 · 2022: 20 · 2021: 25 · 2020: 20 · 2019: 10 · 2018: 15 · 2017: 11 · 2016: 4
- FWCI
- 6.93
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Medical Genetics (publishedVersion)
- PubMed (publishedVersion)
- mediaTUM (Technical University of Munich) (submittedVersion)
- HighWire Press Open Archive (submittedVersion)
- Site cant be reached (submittedVersion)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion)
- Funders
- E-Rare
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
- Keywords
- mitochondrial fission factor, mitochondrial dynamics, optic atrophy, peripheral neuropathy, Drp1, GDAP1, mitochondrial fission, seizures, developmental delay, microcephaly, mitochondrial bioenergetics, inherited mitochondrial disease
- MeSH terms
- Basal Ganglia Diseases, Brain Diseases, Child, Preschool, Humans, Infant, Magnetic Resonance Imaging, Male, Membrane Proteins, Mitochondria, Nerve Tissue Proteins, Optic Atrophy, Peripheral Nervous System Diseases, Peroxisomes, Mitochondrial Proteins, High-Throughput Nucleotide Sequencing, Exome
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