Reduction of endoplasmic reticulum stress attenuates the defects caused by Drosophila mitofusin depletion
Open accessAbstract
Ablation of the mitochondrial fusion and endoplasmic reticulum (ER)–tethering protein Mfn2 causes ER stress, but whether this is just an epiphenomenon of mitochondrial dysfunction or a contributor to the phenotypes in mitofusin (Mfn)-depleted Drosophila melanogaster is unclear. In this paper, we show that reduction of ER dysfunction ameliorates the functional and developmental defects of flies lacking the single Mfn mitochondrial assembly regulatory factor (Marf). Ubiquitous or neuron- and muscle-specific Marf ablation was lethal, altering mitochondrial and ER morphology and triggering ER stress that was conversely absent in flies lacking the fusion protein optic atrophy 1. Expression of Mfn2 and ER stress reduction in flies lacking Marf corrected ER shape, attenuating the developmental and motor defects. Thus, ER stress is a targetable pathogenetic component of the phenotypes caused by Drosophila Mfn ablation.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Decreased mitofusin2 and calnexin expression explain why ER stress and UPR are induced by DRP1 inhibition.
“Both the decreased mitofusin2 and calnexin expression explain why ER stress and UPR are induced by DRP1 inhibition36,37.”
From DRP1-mediated mitochondrial shape controls calcium homeostasis and muscle mass (2019) · cites this paper as [37]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
Brand, A. H., & Perrimon, N. (1993) · Development · doi:10.1242/dev.118.2.401 · Cited by 9,510 · see citing works
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442 · see citing works
Self-citationÖzcan, U., Yilmaz, E., Özcan, L., Furuhashi, M., Vaillancourt, E., Smith, R. O., Görgün, C. Z., & Hotamisligil, G. S. (2006) · Science · doi:10.1126/science.1128294 · Cited by 2,413 · see citing works
ER Tubules Mark Sites of Mitochondrial Division
Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072 · see citing works
Autophagosomes form at ER–mitochondria contact sites
Hamasaki, M., Furuta, N., Matsuda, A., Nezu, A., Yamamoto, A., Fujita, N., Oomori, H., Noda, T., Haraguchi, T., Hiraoka, Y., et al. (2013) · Nature · doi:10.1038/nature11910 · Cited by 1,747 · see citing works
Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572 · see citing works
A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
Stefani, D. D., Raffaello, A., Teardo, E., Szabò, I., & Rizzuto, R. (2011) · Nature · doi:10.1038/nature10230 · Cited by 1,431 · see citing works
Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376 · cited 1× · see citing works
“Mfn1/ and Mfn2/ MEFs were obtained from D. Chan (California Institute of Technology, Pasadena, CA) and cultured as previously described (Chen et al., 2003, 2005).”
MethodOPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300 · see citing works
Self-citationAn ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275 · see citing works
Control of mitochondrial morphology by a human mitofusin
Santel, A., & Fuller, M. T. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.867 · Cited by 1,012 · see citing works
A conditional tissue-specific transgene expression system using inducible GAL4
Osterwalder, T., Yoon, K. S., White, B. H., & Keshishian, H. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221303298 · Cited by 770 · see citing works
SLP‐2 is required for stress‐induced mitochondrial hyperfusion
Tondera, D., Grandemange, S., Jourdain, A. A., Karbowski, M., Mattenberger, Y., Herzig, S., Cruz, S. D., Clerc, P., Lauria, I., Merkwirth, C., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.89 · Cited by 767 · see citing works
<i>Drosophila</i> Parkin requires PINK1 for mitochondrial translocation and ubiquitinates Mitofusin
Ziviani, E., Tao, R. N., & Whitworth, A. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913485107 · Cited by 735 · see citing works
Self-citationMitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
Ishihara, N., Eura, Y., & Mihara, K. (2004) · Journal of Cell Science · doi:10.1242/jcs.01565 · Cited by 731 · see citing works
Deng, H., Dodson, M. W., Huang, H., & Guo, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803998105 · Cited by 683 · see citing works
Sebastián, D., Hernández-Alvarez, M. I., Segalés, J., Sorianello, E., Muñoz, J. P., Sala, D., Waget, A., Liesa, M., Paz, J. C., Gopalacharyulu, P., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108220109 · Cited by 673 · see citing works
Upregulated function of mitochondria‐associated ER membranes in Alzheimer disease
Area‐Gomez, E., del Carmen Lara Castillo, M., Tambini, M. D., Guardia‐Laguarta, C., de Groof, A. J. C., Madra, M., Ikenouchi, J., Umeda, M., Bird, T. D., Sturley, S. L., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.202 · Cited by 638 · see citing works
Developmentally Regulated Mitochondrial Fusion Mediated by a Conserved, Novel, Predicted GTPase
Hales, K. G., & Fuller, M. T. (1997) · Cell · doi:10.1016/s0092-8674(00)80319-0 · Cited by 611 · see citing works
Mitofusin 2 in POMC neurons connects ER stress with leptin resistance and energy imbalance
Schneeberger, M., Dietrich, M. O., Sebastián, D., Imbernón, M., Castaño, C., Garcia, A., Esteban, Y., Gonzalez-Franquesa, A., Rodríguez, I. C., Bortolozzi, A., et al. (2013) · Cell · doi:10.1016/j.cell.2013.09.003 · Cited by 519 · see citing works
Mitochondrial dysfunction and apoptosis in myopathic mice with collagen VI deficiency
Irwin, W., Bergamin, N., Sabatelli, P., Reggiani, C., Megighian, A., Merlini, L., Braghetta, P., Columbaro, M., Volpin, D., Bressan, G. M., et al. (2003) · Nature Genetics · doi:10.1038/ng1270 · Cited by 509 · see citing works
Homotypic fusion of ER membranes requires the dynamin-like GTPase Atlastin
Orso, G., Pendin, D., Liu, S., Tosetto, J., Moss, T. J., Faust, J. E., Micaroni, M., Egorova, A., Martinuzzi, A., McNew, J. A., et al. (2009) · Nature · doi:10.1038/nature08280 · Cited by 473 · see citing works
Self-citationMitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells
Santel, A., Frank, S., Gaume, B. R., Herrler, M., Youle, R. J., & Fuller, M. T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00479 · Cited by 445 · see citing works
Olichon, A., Emorine, L. J., Descoins, E., Pelloquin, L., Brichese, L., Gas, N., Guillou, E., Delettre, C., Valette, A., Hamel, C., et al. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02985-x · Cited by 430 · see citing works
Papanicolaou, K. N., Khairallah, R. J., Ngoh, G. A., Chikando, A. C., Luptak, I., O’Shea, K. M., Riley, D. D., Lugus, J. J., Colucci, W. S., Lederer, W. J., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.00911-10 · Cited by 358 · see citing works
Mitochondrial Fusion Directs Cardiomyocyte Differentiation via Calcineurin and Notch Signaling
Kasahara, A., Cipolat, S., Chen, Y., Dorn, G. W., & Scorrano, L. (2013) · Science · doi:10.1126/science.1241359 · Cited by 354 · see citing works
Self-citationChen, Y., Csordás, G., Jowdy, C. C., Schneider, T. G., Csordás, N., Wang, W., Liu, Y., Kohlhaas, M., Meiser, M., Bergem, S., et al. (2012) · Circulation Research · doi:10.1161/circresaha.112.266585 · Cited by 348 · see citing works
Detmer, S. A., & Chan, D. C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611080 · Cited by 343 · see citing works
An intimate liaison: spatial organization of the endoplasmic reticulum–mitochondria relationship
de Brito, O. M., & Scorrano, L. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.177 · Cited by 297 · see citing works
Self-citationUnfolded protein response in a Drosophila model for retinal degeneration
Ryoo, H. D., Domingos, P. M., Kang, M., & Steller, H. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601477 · Cited by 292 · see citing works
The ER stress factor XBP1s prevents amyloid-β neurotoxicity
Casas-Tinto, S., Zhang, Y., Sanchez-Garcia, J., Gomez-Velazquez, M., Rincon-Limas, D. E., & Fernandez-Funez, P. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr100 · Cited by 275 · see citing works
Inden, M., Kitamura, Y., Takeuchi, H., Yanagida, T., Takata, K., Kobayashi, Y., Taniguchi, T., Yoshimoto, K., Kaneko, M., Okuma, Y., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04440.x · Cited by 261 · see citing works
Wingless Signaling InducesnautilusExpression in the Ventral Mesoderm of theDrosophilaEmbryo
Ranganayakulu, G., Schulz, R. A., & Olson, E. N. (1996) · Developmental Biology · doi:10.1006/dbio.1996.9987 · Cited by 210 · see citing works
Loss of Mitofusin 2 Promotes Endoplasmic Reticulum Stress
Ngoh, G. A., Papanicolaou, K. N., & Walsh, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.359174 · Cited by 183 · see citing works
Detmer, S. A., Velde, C. V., Cleveland, D. W., & Chan, D. C. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm314 · Cited by 148 · see citing works
MARF and Opa1 Control Mitochondrial and Cardiac Function in Drosophila
Dorn, G. W., Clark, C. F., Eschenbacher, W. H., Kang, M., Engelhard, J. T., Warner, S. J., Matkovich, S. J., & Jowdy, C. C. (2010) · Circulation Research · doi:10.1161/circresaha.110.236745 · Cited by 136 · see citing works
Trichoplein/mitostatin regulates endoplasmic reticulum–mitochondria juxtaposition
Cerqua, C., Anesti, V., Pyakurel, A., Liu, D., Naón, D., Wiche, G., Baffa, R., Dimmer, K. S., & Scorrano, L. (2010) · EMBO Reports · doi:10.1038/embor.2010.151 · Cited by 129 · see citing works
Self-citationThe Fusome Mediates Intercellular Endoplasmic Reticulum Connectivity inDrosophilaOvarian Cysts
Snapp, E. L., Iida, T., Frescas, D., Lippincott‐Schwartz, J., & Lilly, M. A. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-06-0475 · Cited by 125 · see citing works
Solá, S., Castro, R. E., Laires, P. A., Steer, C. J., & Rodrigues, C. M. P. (2003) · Molecular Medicine · doi:10.2119/2003-00042.rodrigues · Cited by 119 · see citing works
Expression of mitofusin 2R94Q in a transgenic mouse leads to Charcot–Marie–Tooth neuropathy type 2A
Cartoni, R., Arnaud, E., Médard, J., Poirot, O., Courvoisier, D. S., Chrast, R., & Martinou, J. (2010) · Brain · doi:10.1093/brain/awq082 · Cited by 114 · see citing works
Differential expression of the Drosophila mitofusin genes fuzzy onions (fzo) and dmfn
Hwa, J. J., Hiller, M. A., Fuller, M. T., & Santel, A. (2002) · Mechanisms of Development · doi:10.1016/s0925-4773(02)00141-7 · Cited by 89 · see citing works
Ryoo, H. D., Li, J., & Kang, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075774 · Cited by 39 · see citing works
Ishikawa, F., Akimoto, T., Yamamoto, H., Araki, Y., Yoshie, T., Mori, K., Hayashi, H., Nose, K., & Shibanuma, M. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp052 · Cited by 31 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Critical reappraisal confirms that Mitofusin 2 is an endoplasmic reticulum–mitochondria tether
Naon, D., Zaninello, M., Giacomello, M., Varanita, T., Grespi, F., Lakshminaranayan, S., Serafini, A., Semenzato, M., Herkenne, S., Hernández-Alvarez, M. I., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606786113 · Cited by 521 · see citing works
Self-citationSoluble Uric Acid Activates the NLRP3 Inflammasome
Braga, T. T., Forni, M. F., Corrêa-Costa, M., Ramos, R. N., Barbuto, J. A. M., Branco, P. C., Castoldi, Â., Hiyane, M. I., Davanso, M. R., Latz, E., et al. (2017) · Scientific Reports · doi:10.1038/srep39884 · Cited by 447 · see citing works
DRP1-mediated mitochondrial shape controls calcium homeostasis and muscle mass
Favaro, G., Romanello, V., Varanita, T., Andrea Desbats, M., Morbidoni, V., Tezze, C., Albiero, M., Canato, M., Gherardi, G., De Stefani, D., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10226-9 · Cited by 398 · see citing works
Self-citationMitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity
Bertholet, A. M., Delerue, T., Millet, A. M., Moulis, M. F., David, C., Daloyau, M., Arnauné-Pelloquin, L., Davezac, N., Mils, V., Miquel, M. C., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.011 · Cited by 363 · see citing works
Mitofusin 2: from functions to disease
Filadi, R., Pendin, D., & Pizzo, P. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0023-6 · Cited by 359 · see citing works
Self-citationRegulation of ER-mitochondria contacts by Parkin via Mfn2
Basso, V., Marchesan, E., Peggion, C., Chakraborty, J., von Stockum, S., Giacomello, M., Ottolini, D., Debattisti, V., Caicci, F., Tasca, E., et al. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.09.006 · Cited by 207 · see citing works
Self-citationCelardo, I., Costa, A. C., Lehmann, S., Jones, C., Wood, N. W., Mencacci, N. E., Mallucci, G. R., Loh, S. H. Y., & Martins, L. M. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.173 · Cited by 181 · see citing works
At the right distance: ER-mitochondria juxtaposition in cell life and death
Naon, D., & Scorrano, L. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.05.011 · Cited by 178 · see citing works
Self-citationSplice variants of mitofusin 2 shape the endoplasmic reticulum and tether it to mitochondria
Naón, D., Hernández‐Álvarez, M. I., Shinjo, S., Wieczór, M., Ivanova, S., de Brito, O. M., Quintana, A., Hidalgo, J., Palacı́n, M., Aparicio, P., et al. (2023) · Science · doi:10.1126/science.adh9351 · Cited by 158 · see citing works
Self-citationMitochondrial dynamism and heart disease: changing shape and shaping change
Dorn, G. W. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201404575 · Cited by 147 · see citing works
Sandoval, H., Yao, C., Chen, K., Jaiswal, M., Donti, T., Qi, L. Y., Bayat, V., Xiong, B., Zhang, K., David, G., et al. (2014) · eLife · doi:10.7554/elife.03558 · Cited by 138 · see citing works
Restelli, L. M., Oettinghaus, B., Halliday, M., Ağca, C., Licci, M., Sironi, L., Savoia, C., Hench, J., Tolnay, M., Neutzner, A., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.023 · Cited by 96 · see citing works
Self-citationManganelli, V., Matarrese, P., Antonioli, M., Gambardella, L., Vescovo, T., Gretzmeier, C., Longo, A., Capozzi, A., Recalchi, S., Riitano, G., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1834207 · Cited by 94 · see citing works
Trevisan, T., Pendin, D., Montagna, A., Bova, S., Ghelli, A. M., & Daga, A. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.017 · Cited by 86 · see citing works
Functional implications of mitofusin 2-mediated mitochondrial-SR tethering
Dorn, G. W., Song, M., & Walsh, K. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.09.015 · Cited by 86 · see citing works
Bioenergetic roles of mitochondrial fusion
Ramos, E. S., Larsson, N., & Mourier, A. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.04.002 · Cited by 76 · see citing works
Drosophila as a model for unfolded protein response research
Ryoo, H. D. (2015) · BMB Reports · doi:10.5483/bmbrep.2015.48.8.099 · Cited by 59 · see citing works
Tsakiri, E. N., Gumeni, S., Vougas, K. N., Pendin, D., Papassideri, I. S., Daga, A., Gorgoulis, V. G., Juhász, G., Scorrano, L., & Trougakos, I. P. (2019) · Autophagy · doi:10.1080/15548627.2019.1596477 · Cited by 52 · see citing works
Self-citationEdenharter, O., Schneuwly, S., & Navarro, J. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00038 · Cited by 44 · see citing works
Decreasing pdzd8-mediated mito–ER contacts improves organismal fitness and mitigates Aβ 42 toxicity
Hewitt, V. L., Miller‐Fleming, L., Twyning, M. J., Andreazza, S., Mattedi, F., Prudent, J., Polleux, F., Vagnoni, A., & Whitworth, A. J. (2022) · Life Science Alliance · doi:10.26508/lsa.202201531 · Cited by 44 · see citing works
Wang, Z.-H., Clark, C. P., & Geisbrecht, E. R. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw067 · Cited by 44 · see citing works
Bhandari, P., Song, M., & Dorn, G. W. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.12.018 · Cited by 34 · see citing works
Rab7a modulates ER stress and ER morphology
Mateus, D., Marini, E. S., Progida, C., & Bakke, O. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.02.011 · Cited by 35 · see citing works
Inhibition of the deubiquitinase USP8 corrects a Drosophila PINK1 model of mitochondria dysfunction
von Stockum, S., Sánchez-Martínez, Á., Corrà, S., Chakraborty, J., Marchesan, E., Locatello, L., Da‐Ré, C., Cusumano, P., Caicci, F., Ferrari, V., et al. (2019) · Life Science Alliance · doi:10.26508/lsa.201900392 · Cited by 31 · see citing works
Self-citationER responses play a key role in Swiss-Cheese/Neuropathy Target Esterase-associated neurodegeneration
Sunderhaus, E. R., Law, A. D., & Kretzschmar, D. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104520 · Cited by 32 · see citing works
Cardiac mitochondria: A surprise about size
Sun, N., & Finkel, T. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.01.009 · Cited by 29 · see citing works
Μitochondrial Membrane Dynamics and Inherited Optic Neuropathies
Bagli, E., Zikou, A. K., Agnantis, N. J., & Kitsos, G. (2017) · In Vivo · doi:10.21873/invivo.11090 · Cited by 24 · see citing works
Analysis of mitochondrial structure and function in the Drosophila larval musculature
Wang, Z.-H., Clark, C. P., & Geisbrecht, E. R. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.11.005 · Cited by 23 · see citing works
Chakrabarti, L., Chaerkady, R., Wang, J., Weng, S. H. S., Wang, C., Qian, C., Cazares, L. H., Hess, S. Y., Amaya, P., Zhu, J., et al. (2022) · mAbs · doi:10.1080/19420862.2021.2020081 · Cited by 22 · see citing works
DRP-1-mediated apoptosis induces muscle degeneration in dystrophin mutants
Scholtes, C., Bellemin, S., Martin, E., Carre-Pierrat, M., Mollereau, B., Gieseler, K., & Walter, L. (2018) · Scientific Reports · doi:10.1038/s41598-018-25727-8 · Cited by 22 · see citing works
Mitochondria in the Aging Muscles of Flies and Mice: New Perspectives for Old Characters
del Campo, A., Jaimovich, E., & Tevy, M. F. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9057593 · Cited by 22 · see citing works
Wang, Z.-H., Rabouille, C., & Geisbrecht, E. R. (2015) · Biology Open · doi:10.1242/bio.201511551 · Cited by 20 · see citing works
Molecular pathogenesis of peripheral neuropathies: insights from Drosophila models
Bussmann, J., & Storkebaum, E. (2017) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2017.01.011 · Cited by 20 · see citing works
Gumeni, S., Evangelakou, Z., Tsakiri, E. N., Scorrano, L., & Trougakos, I. P. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101219 · Cited by 20 · see citing works
Self-citationKasture, A. S., Fischer, F. P., Kunert, L., Burger, M., Burgstaller, A. C., El‐Kasaby, A., Hummel, T., & Sučić, S. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.1074427 · Cited by 19 · see citing works
Relationship between mitofusin 2 and cancer
Allegra, A., Innao, V., Allegra, A. G., & Musolino, C. (2018) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2018.11.009 · Cited by 19 · see citing works
Recent Advances in Drosophila Models of Charcot-Marie-Tooth Disease
Kitani‐Morii, F., & Noto, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197419 · Cited by 16 · see citing works
Mauri, S., Bernardo, G., Martinez, A., Favaro, M., Trevisan, M., Cobraiville, G., Fillet, M., Caicci, F., Whitworth, A. J., & Ziviani, E. (2023) · Cells · doi:10.3390/cells12081143 · Cited by 19 · see citing works
Self-citationEnhancing folic acid metabolism suppresses defects associated with loss of Drosophila mitofusin
Garrido‐Maraver, J., Celardo, I., Costa, A. C. O., Lehmann, S., Loh, S. H. Y., & Martins, L. M. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1496-2 · Cited by 14 · see citing works
Mitochondrial Dynamics: Shaping Metabolic Adaptation
Cantó, C. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.05.004 · Cited by 14 · see citing works
Mitochondria-associated endoplasmic reticulum membranes: A promising toxicity regulation target
Hu, Z., Shi, S., Ou, Y., Hu, F., & Long, D. (2023) · Acta Histochemica · doi:10.1016/j.acthis.2023.152000 · Cited by 12 · see citing works
The IRE1 pathway regulates honey bee Unfolded Protein Response gene expression
Adames, T. R., Rondeau, N. C., Kabir, M. T., Johnston, B. A., Truong, H., & Snow, J. W. (2020) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2020.103368 · Cited by 12 · see citing works
Pereira, M. T., Brock, K., & Musselman, L. P. (2020) · G3 Genes Genomes Genetics · doi:10.1534/g3.120.401688 · Cited by 11 · see citing works
Translational approaches to restoring mitochondrial function in Parkinson's disease
Mortiboys, H., Macdonald, R., Payne, T., Sassani, M., Jenkins, T. M., & Bandmann, O. (2017) · FEBS Letters · doi:10.1002/1873-3468.12920 · Cited by 11 · see citing works
Lobato, A. G., Ortiz-Vega, N., Canic, T., Tao, X., Bucan, N., Ruan, K., Rebelo, A. P., Schüle, R., Zuchner, S. L., Syed, S., et al. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167348 · Cited by 10 · see citing works
Fidelis, K. R., Nunes, R. G. D. S., da Silva, C. S., Oliveira, C. V. B., Costa, A. R., Silva, J. R. D. L., dos Santos, L. B., de Oliveira, E. E. S., Pereira, P. S., de Menezes, I. R. A., et al. (2021) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2021.109119 · Cited by 10 · see citing works
Nacα protects the larval fat body from cell death by maintaining cellular proteostasis in Drosophila
Yamada, T., Yoshinari, Y., Tobo, M., Habara, O., & Nishimura, T. (2023) · Nature Communications · doi:10.1038/s41467-023-41103-1 · Cited by 7 · see citing works
Murray-Cors, S., Owens, M., Liew, Y.-T., Day, M., Cairns, W., & Prokop, A. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1631752 · Cited by 8 · see citing works
Mitochondrial fusion protein 2 regulates endoplasmic reticulum stress in preeclampsia
Sun, D., Zhu, H., Ai, L., Wu, H., Wu, Y., & Jin, J. (2021) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2000557 · Cited by 8 · see citing works
Live applications of norbormide-based fluorescent probes in Drosophila melanogaster
Forgiarini, A., Wang, Z., D’Amore, C., Jay‐Smith, M., Li, F. F., Hopkins, B., Brimble, M. A., Pagetta, A., Bersani, S., Martin, S. D., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0211169 · Cited by 7 · see citing works
The Enigma of Norbormide, a Rattus-Selective Toxicant
Fusi, F., Saponara, S., Brimble, M. A., Rennison, D., Hopkins, B., & Bova, S. (2024) · Cells · doi:10.3390/cells13090788 · Cited by 5 · see citing works
Role of MFN2 in bovine embryonic development and the mitigation of ER stress
Shi, S., Hu, B., Chi, Z.-C., Qu, L.-Y., Liu, L., He, Y.-Y., Jia, G.-L., Li, J., Kong, I., Jin, Y.-X., et al. (2024) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2024.107664 · Cited by 4 · see citing works
Djalalvandi, A., Takeda, K., Grespi, F., Fan, H., Fonseca, T. B., Nogara, L., Sharifi, S., Barison, C., Semenzato, M., Omori, A., et al. (2025) · Cell Reports Medicine · doi:10.1016/j.xcrm.2025.102248 · Cited by 2 · see citing works
Self-citationLiu, H., Deng, Y., Peng, M., Nie, Y., & Chen, J. (2025) · The FASEB Journal · doi:10.1096/fj.202500821r · Cited by 2 · see citing works
Modulation of Cell Fate by Tauroursodeoxycholic Acid: All Paths Lead to Mitochondria
Solá, S., Ribeiro, M. F., Genebra, T., & Rodrigues, C. M. P. (2018) · Springer eBooks · doi:10.1007/978-3-319-73344-9_19 · Cited by 1 · see citing works
Li, J. (2017) · Deep Blue (University of Michigan)
VARUK, O. O., Ruiz, A., Orengo, C., Cozzolino, A., de Boissier, P., Aouane, A., & Rival, T. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.14.642792
Li, Y., Zhao, Q., Xu, W., Kong, X., Hou, C., Dong, Y., Guan, Y., Wang, R., Cai, L., & Niu, Y. (2026) · Journal of Nutrition · doi:10.1016/j.tjnut.2026.101492
Arginine ameliorates motor and survival deficits in MFN2-Deficient Drosophila models
Ando, M., Okamoto, Y., Higuchi, Y., Yuan, J., Yoshimura, A., Yano, C., Nagatomo, R., Hobara, T., Kojima, F., Hiramatsu, Y., et al. (2026) · Neurotherapeutics · doi:10.1016/j.neurot.2026.e00900
Gong, Q., Liu, T., Han, X., Zhang, R. J., Liu, X., Xiong, B., Ali, T., Huang, J., Xie, Y., Li, S., et al. (2026) · Molecular Biomedicine · doi:10.1186/s43556-026-00457-w
- Authors
- Debattisti, V., Pendin, D., Ziviani, E., Daga, A., & Scorrano, L.
- Affiliations
- Veneto Institute of Molecular Medicine (IT)
- IRCCS Eugenio Medea (IT)
- University of Geneva (CH)
- University of Padua (IT)
- Corresponding author
- Scorrano, Luca
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2014-01-27
- Volume
- 204
- Issue
- 3
- Pages
- 303-312
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC3912536
- OpenAlex
- W2077906609
- Cited by
- 63
- References
- 44
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 3 · 2023: 6 · 2022: 2 · 2021: 2 · 2020: 4 · 2019: 7 · 2018: 11 · 2017: 5 · 2016: 6 · 2015: 6 · 2014: 4
- FWCI
- 2.87
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion, cc-by-nc-sa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- endoplasmic reticulum stress, mitofusins, mitofusin 2, Marf, mitochondrial fusion, optic atrophy 1, ER morphology, motor defects, developmental defects, Drosophila melanogaster
- MeSH terms
- Animals, Drosophila melanogaster, Genetic Complementation Test, Humans, Locomotion, Membrane Proteins, Mitochondria, Phenylbutyrates, Taurochenodeoxycholic Acid, Drosophila Proteins, RNA Interference, Mice, Endoplasmic Reticulum Stress
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review