The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
Open accessAbstract
Juxtaposition between endoplasmic reticulum (ER) and mitochondria is a common structural feature, providing the physical basis for intercommunication during Ca(2+) signalling; yet, the molecular mechanisms controlling this interaction are unknown. Here we show that mitofusin 2, a mitochondrial dynamin-related protein mutated in the inherited motor neuropathy Charcot-Marie-Tooth type IIa, is enriched at the ER-mitochondria interface. Ablation or silencing of mitofusin 2 in mouse embryonic fibroblasts and HeLa cells disrupts ER morphology and loosens ER-mitochondria interactions, thereby reducing the efficiency of mitochondrial Ca(2+) uptake in response to stimuli that generate inositol-1,4,5-trisphosphate. An in vitro assay as well as genetic and biochemical evidences support a model in which mitofusin 2 on the ER bridges the two organelles by engaging in homotypic and heterotypic complexes with mitofusin 1 or 2 on the surface of mitochondria. Thus, mitofusin 2 tethers ER to mitochondria, a juxtaposition required for efficient mitochondrial Ca(2+) uptake.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Other important MAM tethering proteins are B-cell receptor–associated protein 31, mitochondrial fission 1 protein [96], and mitofusin [97].”
From Neuronal Apolipoprotein E4 Expression Results in Proteome-Wide Alterations and Compromises Bioenergetic Capacity by Disrupting Mitochondrial Function (2019) · cites this paper as [97]
In the citing paper
“Marf/Mfn is a mitochondrial fusion protein with pleiotropic functions [39,40] that is also a target of Parkin-dependent ubiquitination upon stress-induced mitophagy.”
From USP8 Down-Regulation Promotes Parkin-Independent Mitophagy in the Drosophila Brain and in Human Neurons (2023) · cites this paper as [39]
In the citing paper
“MFN2, and not MFN1, is expressed on the mitochondria-associated endoplasmic reticulum membranes (MAM) and, to a lesser extent, to the endoplasmic/sarcoplasmic reticulum (ER/SR) [63, 64].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [63]
In the citing paper
“Indeed, MFN2 bridges mitochondria to ER/SR, facilitating critical processes linked to ER–mitochondria interactions like calcium homeostasis and the modulation of the UPR during ER stress via PERK [63, 65–68].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [63]
In the citing paper
“ER stress is induced by the decrease of the ER–mitochondria tethering protein Mfn2 and the down- and upregulation of the ER chaperones calnexin and Bip/Grp78, respectively [63, 65, 66, 213].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [63]
In the citing paper
“Despite some redundancies in their function, the two proteins possess several distinct properties, suggesting that they fulfill different roles in fusion (de Brito and Scorrano, 2008; Eura et al., 2003; Ishihara et al., 2004).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as de Brito and Scorrano, 2008
Citations
Cites
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
Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257
Measurement of co‐localization of objects in dual‐colour confocal images
Manders, E. M. M., Verbeek, F. J., & Aten, J. A. (1993) · Journal of Microscopy · doi:10.1111/j.1365-2818.1993.tb03313.x · Cited by 2,132
OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion
Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673
Self-citationMutations 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
Organelle-specific initiation of cell death pathways
Ferri, K. F., & Kroemer, G. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-e255 · Cited by 1,455
BAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis
Scorrano, L., Oakes, S. A., Opferman, J. T., Cheng, E. H. Y., Sorcinelli, M. D., Pozzan, T., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1081208 · Cited by 1,387
Self-citationCsordás, G., Renken, C. W., Várnai, P., Walter, L., Weaver, D., BUTTLE, K. F., Balla, T., Mannella, C. A., & Hajnóczky, G. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604016 · Cited by 1,377
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
OPA1 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
Self-citation
Cited by
Sorted by citations
Items 701–800 of 1,010
Crosstalk between mitochondria–ER contact sites and the apoptotic machinery as a novel health meter
Larrañaga-SanMiguel, A., Bengoa‐Vergniory, N., & Flores‐Romero, H. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.08.007 · Cited by 94
Intracellular trafficking of ceramide by ceramide transfer protein
Hanada, K. (2010) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.86.426 · Cited by 94
COG complexes form spatial landmarks for distinct SNARE complexes
Willett, R. A., Kudlyk, T. A., Pokrovskaya, I. D., Schönherr, R., Ungár, D., Duden, R., & Lupashin, V. V. (2013) · Nature Communications · doi:10.1038/ncomms2535 · Cited by 94
Pla‐Martín, D., Rueda, C. B., Estela, A., Sánchez‐Piris, M., González‐Sánchez, P., Traba, J., de la Fuente, S., Scorrano, L., Renau‐Piqueras, J., Álvarez, J., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.03.010 · Cited by 94
Self-citationSchlattner, U., Tokarska-Schlattner, M., Rousseau, D. L., Boissan, M., Mannella, C. A., Epand, R. M., & Lacombe, M. (2014) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2013.12.008 · Cited by 93
Rocha, S., Freitas, A., Guimarães, S., Vitorino, R. M. P., Aroso, M., & Gómez-Lázaro, M. (2017) · Antioxidants · doi:10.3390/antiox7010001 · Cited by 93
Zhang, Y., Wu, Y. F., Zhang, M., Li, Z., Liu, B., Liu, H.-F., Hao, J., & Li, X. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01353-w · Cited by 95
Mitochondrial Dysfunction in Neurodegenerative Diseases
Yang, H. (2025) · Cells · doi:10.3390/cells14040276 · Cited by 95
Lipids at membrane contact sites: cell signaling and ion transport
Muallem, S., Chung, W. Y., Jha, A., & Ahuja, M. (2017) · EMBO Reports · doi:10.15252/embr.201744331 · Cited by 93
Zampieri, S., Mammucari, C., Romanello, V., Barberi, L., Pietrangelo, L., Fusella, A., Mosole, S., Gherardi, G., Höfer, C., Löfler, S., et al. (2016) · Physiological Reports · doi:10.14814/phy2.13005 · Cited by 92
Mechanisms of mitochondrial cell death
Dadsena, S., Zollo, C., & García-Sáez, A. J. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200522 · Cited by 92
Intertwined and Finely Balanced: Endoplasmic Reticulum Morphology, Dynamics, Function, and Diseases
Perkins, H. T., & Allan, V. (2021) · Cells · doi:10.3390/cells10092341 · Cited by 93
Role of Mitochondrial Dynamics in Heart Diseases
Tokuyama, T., & Yanagi, S. (2023) · Genes · doi:10.3390/genes14101876 · Cited by 92
Mitochondria-Associated Membranes (MAMs) as Hotspot Ca2+ Signaling Units
Bononi, A., Missiroli, S., Poletti, F., Suski, J. M., Agnoletto, C., Bonora, M., Marchi, E. D., Giorgi, C., Marchi, S., Patergnani, S., et al. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2888-2_17 · Cited by 92
Bock, M. D., Decrock, E., Wang, N., Bol, M., Vinken, M., Bultynck, G., & Leybaert, L. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.04.016 · Cited by 92
Perturbed mitochondrial Ca2+signals as causes or consequences of mitophagy induction
Rimessi, A., Bonora, M., Marchi, S., Patergnani, S., Marobbio, C. M. T., Lasorsa, F. M., & Pinton, P. (2013) · Autophagy · doi:10.4161/auto.24795 · Cited by 92
Barneo‐Muñoz, M., Juárez, P., Civera-Tregón, A., Yndriago, L., Pla‐Martín, D., Zenker, J., Cuevas-Martín, C., Estela, A., Sánchez‐Aragó, M., Forteza‐Vila, J., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005115 · Cited by 92
Wolfram syndrome: MAMs’ connection?
Delprat, B., Maurice, T., & Delettre, C. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0406-3 · Cited by 91
PACS-2: A key regulator of mitochondria-associated membranes (MAMs)
Li, C., Li, L., Yang, M., Zeng, L., & Sun, L. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105080 · Cited by 91
Mitochondrial localization unveils a novel role for GRK2 in organelle biogenesis
Fusco, A., Santulli, G., Sorriento, D., Cipolletta, E., Garbi, C., Dorn, G. W., Trimarco, B., Feliciello, A., & Iaccarino, G. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.09.026 · Cited by 91
New concepts of endoplasmic reticulum function in the heart: Programmed to conserve
Doroudgar, S., & Glembotski, C. C. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.10.006 · Cited by 90
Mitochondrial lipids in neurodegeneration
Aufschnaiter, A., Kohler, V., Diessl, J., Peselj, C., Carmona‐Gutiérrez, D., Keller, W., & Büttner, S. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2463-1 · Cited by 91
Thoudam, T., Jeon, J., Ha, C., & Lee, I. (2016) · Mediators of Inflammation · doi:10.1155/2016/1851420 · Cited by 91
Simmen, T., & Herrera-Cruz, M. S. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.04.014 · Cited by 90
Han, S. H., Zhao, F., Hsia, J., Ma, X., Liu, Y., Torres, S. L., Fujioka, H., & Zhu, X. (2021) · Journal of Cell Science · doi:10.1242/jcs.253443 · Cited by 90
Transient Ca2+ depletion of the sarcoplasmic reticulum at the onset of reperfusion
Valverde, C. A., Kornyeyev, D., Ferreiro, M., Petrosky, A. D., MATTIAZZI, A. R., & Escobar, A. L. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp371 · Cited by 90
Wakai, T., Harada, Y., Miyado, K., & Kono, T. (2014) · Molecular Human Reproduction · doi:10.1093/molehr/gau064 · Cited by 90
Cheng, H., Gang, X., He, G., Liu, Y., Wang, Y., Zhao, X. Y., & Wang, G. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.592129 · Cited by 89
BOK controls apoptosis by Ca2+ transfer through ER-mitochondrial contact sites
Carpio, M. A., Means, R. E., Brill, A. L., Sainz, A. G., Ehrlich, B. E., & Katz, S. G. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108827 · Cited by 89
Cellular senescence links mitochondria-ER contacts and aging
Ziegler, D. V., Martin, N., & Bernard, D. (2021) · Communications Biology · doi:10.1038/s42003-021-02840-5 · Cited by 91
Chhimpa, N., Singh, N., Puri, N., & Kayath, H. P. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-220514 · Cited by 89
Aravamudan, B., Thompson, M. A., Pabelick, C. M., & Prakash, Y. S. (2013) · Expert Review of Respiratory Medicine · doi:10.1586/17476348.2013.834252 · Cited by 89
A novel fission-independent role of dynamin-related protein 1 in cardiac mitochondrial respiration
Zhang, H., Wang, P., Bisetto, S., Yoon, Y., Chen, Q., Sheu, S., & Wang, W. (2016) · Cardiovascular Research · doi:10.1093/cvr/cvw212 · Cited by 88
Bernard‐Marissal, N., Chrast, R., & Schneider, B. L. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0125-1 · Cited by 88
DJ-1 in neurodegenerative diseases: Pathogenesis and clinical application
Huang, M., & Chen, S. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102114 · Cited by 88
Mitophagy Promotes Resistance to BH3 Mimetics in Acute Myeloid Leukemia
Glytsou, C., Chen, X., Zacharioudakis, E., Al-Santli, W., Zhou, H., Nadorp, B., Lee, S., Lasry, A., Sun, Z., Papaioannou, D., et al. (2023) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0601 · Cited by 91
Mitochondrial dynamics altered by oxidative stress in cancer
Kim, B., & Song, Y. S. (2016) · Free Radical Research · doi:10.1080/10715762.2016.1210141 · Cited by 88
Endoplasmic Reticulum–Mitochondria Contact Sites and Neurodegeneration
Xu, L., Wang, X., & Tong, C. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00428 · Cited by 87
Zeviani, M., & Carelli, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010210 · Cited by 87
Liu, Y., Liu, S., Huang, J., Liu, Y., Wang, Q., Chen, J., Sun, L., & Tu, W. (2023) · Environment International · doi:10.1016/j.envint.2023.107977 · Cited by 87
Shiiba, I., Ito, N., Oshio, H., Ishikawa, Y., Nagao, T., Shimura, H., Oh, K.-W., Takasaki, E., Yamaguchi, F., Konagaya, R., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56666-4 · Cited by 87
Attenuation of endoplasmic reticulum stress by caffeine ameliorates hyperoxia-induced lung injury
Teng, R., Jing, X., Michalkiewicz, T., Afolayan, A. J., Wu, T.-J., & Konduri, G. G. (2017) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00405.2016 · Cited by 87
Tying trafficking to fusion and fission at the mighty mitochondria
Farmer, T., Naslavsky, N., & Caplan, S. (2018) · Traffic · doi:10.1111/tra.12573 · Cited by 87
Renault, T. T., & Chipuk, J. E. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.10.009 · Cited by 86
Cofilin1-dependent actin dynamics control DRP1-mediated mitochondrial fission
Rehklau, K., Hoffmann, L., Gurniak, C. B., Ott, M., Witke, W., Scorrano, L., Culmsee, C., & Rust, M. B. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.448 · Cited by 86
Self-citationReview: The role of mitochondria in the pathogenesis of amyotrophic lateral sclerosis
Duffy, L. M., Chapman, A. L., Shaw, P. J., & Grierson, A. J. (2011) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2011.01166.x · Cited by 86
Mitochondrial dynamics and their impact on T cell function
Quintana, A., & Hoth, M. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.02.005 · Cited by 86
The ERMES complex and ER–mitochondria connections
Michel, A. H., & Kornmann, B. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110758 · Cited by 86
Mechanical ventilation triggers abnormal mitochondrial dynamics and morphology in the diaphragm
Picard, M. A., Azuelos, I., Jung, B., Giordano, C., Matecki, S., Hussain, S. N. A., White, K., Li, T., Liang, F., Benedetti, A., et al. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00873.2014 · Cited by 86
Parkin functionally interacts with PGC-1α to preserve mitochondria and protect dopaminergic neurons
Zheng, L., Bernard‐Marissal, N., Moullan, N., D'Amico, D. F., Auwerx, J. H., Moore, D. J., Knott, G. W., Aebischer, P., & Schneider, B. L. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw418 · Cited by 86
Mitofusins: Disease Gatekeepers and Hubs in Mitochondrial Quality Control by E3 Ligases
Escobar‐Henriques, M., & Joaquim, M. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00517 · Cited by 85
Chang, J., Liu, K., Li, Y., Kou, S.-J., Wei, Y., Chuang, C., Hsieh, M., & Liu, C. (2012) · Neurosignals · doi:10.1159/000341981 · Cited by 85
Regulation of autophagy by mitochondrial phospholipids in health and diseases
Hsu, P., & Shi, Y. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.003 · Cited by 86
Kulkarni, S. S., Joffraud, M., Boutant, M., Ratajczak, J., Gao, A. W., Maclachlan, C., Hernández‐Álvarez, M. I., Raymond, F., Métairon, S., Descombes, P., et al. (2016) · Diabetes · doi:10.2337/db15-1725 · Cited by 85
The mystery of mitochondria-ER contact sites in physiology and pathology: A cancer perspective
Simões, I. C. M., Morciano, G., Lebiedzińska, M., Aguiari, G., Pinton, P., Potes, Y., & Wieckowski, M. R. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165834 · Cited by 84
Enhanced mitochondrial fission suppresses signaling and metastasis in triple-negative breast cancer
Humphries, B. A., Cutter, A. C., Buschhaus, J. M., Chen, Y., Qyli, T., Palagama, D. S. W., Eckley, S. S., Robison, T. H., Bevoor, A. S., Chiang, B., et al. (2020) · Breast Cancer Research · doi:10.1186/s13058-020-01301-x · Cited by 84
Multitasking guardian of mitochondrial quality: Parkin function and Parkinson’s disease
Kamienieva, I., Duszyński, J., & Szczepanowska, J. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-020-00229-8 · Cited by 84
Multifaceted roles of mitochondria in wound healing and chronic wound pathogenesis
Hunt, M., Torres, M. S., Bachar-Wikström, E., & Wikström, J. D. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1252318 · Cited by 84
Functional implications of mitofusin 2-mediated mitochondrial-SR tethering
Dorn, G. W., Song, M., & Walsh, K. X. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.09.015 · Cited by 84
Endosome–mitochondria juxtaposition during apoptosis induced by H. pylori VacA
Calore, F., Genisset, C., Casellato, A., Rossato, M., Codolo, G., Esposti, M. D., Scorrano, L., & de Bernard, M. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.42 · Cited by 84
Self-citationPodocyte Injury in Diabetic Kidney Disease: A Focus on Mitochondrial Dysfunction
Liu, S., Yuan, Y., Yi, X., Xing, C., & Zhang, B. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.832887 · Cited by 82
Neurotoxic β-amyloid oligomers cause mitochondrial dysfunction—the trigger for PANoptosis in neurons
Meng, X., Song, Q., Liu, Z., Liu, X., Wang, Y., & Liu, J. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1400544 · Cited by 84
Mitofusin 2 as a Driver That Controls Energy Metabolism and Insulin Signaling
Antonio Zorzano, A., Hernández‐Álvarez, M. I., Sebastián, D., & Muñoz, J. P. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6208 · Cited by 83
Molecular mechanisms of asbestos-induced lung epithelial cell apoptosis
Liu, G., Beri, R., Mueller, A., & Kamp, D. W. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.03.047 · Cited by 83
MLN64 induces mitochondrial dysfunction associated with increased mitochondrial cholesterol content
Balboa, E., Castro, J., Pinochet, M.-J., Cancino, G. I., Matías, N., Sáez, P. J., Martinez, A. N., Alvarez, A. R., García‐Ruiz, C., Fernández-Checa, J. C., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.02.024 · Cited by 83
Khalil, S., Holy, M., Grado, S., Fleming, R. E., Kurita, R., Nakamura, Y., & Goldfarb, A. N. (2017) · Blood Advances · doi:10.1182/bloodadvances.2016003772 · Cited by 85
Redox signals at the ER–mitochondria interface control melanoma progression
Zhang, X., Gibhardt, C. S., Will, T., Stanisz, H., Körbel, C., Mitkovski, M., Stejerean‐Todoran, I., Cappello, S., Pacheu‐Grau, D., Dudek, J., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2018100871 · Cited by 83
Dorn, G. W., & Scorrano, L. (2010) · Circulation Research · doi:10.1161/circresaha.110.225714 · Cited by 82
Self-citationThe biology of lipid droplet-bound mitochondria
Veliova, M., Petcherski, A., Liesa, M., & Shirihai, O. S. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.04.013 · Cited by 82
Implications of mitochondrial dynamics on neurodegeneration and on hypothalamic dysfunction
Antonio Zorzano, A., & Claret, M. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00101 · Cited by 83
Melatonin prevents adverse myocardial infarction remodeling via Notch1/Mfn2 pathway
Pei, H., Du, J., Song, X., He, L., Zhang, Y., Li, X., Qiu, C., Zhang, Y., Hou, J., Feng, J., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.06.015 · Cited by 82
Mitochondria-Associated Membranes (MAMs): Overview and Its Role in Parkinson’s Disease
Rodríguez‐Arribas, M., Yakhine-Diop, S. M. S., Pedro, J. M. B., Gómez‐Suaga, P., Gómez‐Sánchez, R., Martínez-Chacón, G., Fuentes, J. M., González‐Polo, R. A., & Niso‐Santano, M. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0140-8 · Cited by 82
Mitochondria in Structural and Functional Cardiac Remodeling
Torrealba, N., Aránguiz, P., Alonso, C., Rothermel, B. A., & Lavandero, S. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_15 · Cited by 82
Peroxisome Interactions and Cross-Talk with Other Subcellular Compartments in Animal Cells
Schrader, M., Grille, S., Fahimi, H. D., & Islinger, M. (2013) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-6889-5_1 · Cited by 82
Dysregulation of Mfn2 and Drp-1 proteins in heart failure
Givvimani, S., Pushpakumar, S. B., Veeranki, S., & Tyagi, S. C. (2014) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2014-0060 · Cited by 83
Cardiolipin remodeling by ALCAT1 links mitochondrial dysfunction to Parkinson’s diseases
Song, C., Zhang, J., Qi, S., Liu, Z., Zhang, X., Zheng, Y., Andersen, J.-P., Zhang, W., Strong, R., Martinez, P. A., et al. (2019) · Aging Cell · doi:10.1111/acel.12941 · Cited by 81
Zhong, S., Li, L., Liang, N., Zhang, L., Xu, X., Chen, S., & Yin, H. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101919 · Cited by 81
Pereira, A. C., Pascale, J. D., Resende, R., Cardoso, S., Ferreira, I., Neves, B. M., Carrascal, M. A., Zuzarte, M., Madeira, N. G. G. F., Morais, S., et al. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04211-7 · Cited by 81
Redox regulation of UPR signalling and mitochondrial ER contact sites
Casas-Martinez, J. C., Samali, A., & McDonagh, B. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05286-0 · Cited by 85
Ligand-dependent localization and function of ORP–VAP complexes at membrane contact sites
Weber‐Boyvat, M., Kentala, H., Peränen, J., & Olkkonen, V. M. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1786-x · Cited by 81
Oxysterol-binding proteins: Functions in cell regulation beyond lipid metabolism
Weber‐Boyvat, M., Zhong, W., Yan, D., & Olkkonen, V. M. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.02.016 · Cited by 81
Optic Atrophy 1-Dependent Mitochondrial Remodeling Controls Steroidogenesis in Trophoblasts
Wasilewski, M., Semenzato, M., Rafelski, S. M., Robbins, J. R., Bakardjiev, A. I., & Scorrano, L. (2012) · Current Biology · doi:10.1016/j.cub.2012.04.054 · Cited by 81
Self-citationATP increases within the lumen of the endoplasmic reticulum upon intracellular Ca2+release
Vishnu, N., Khan, M. J., Karsten, F., Groschner, L. N., Waldeck‐Weiermair, M., Rost, R., Hallström, S., Imamura, H., Graier, W. F., & Malli, R. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-07-0433 · Cited by 81
MIRO GTPases in Mitochondrial Transport, Homeostasis and Pathology
Tang, B. L. (2015) · Cells · doi:10.3390/cells5010001 · Cited by 81
Oettinghaus, B., D’Alonzo, D., Barbieri, E., Restelli, L. M., Savoia, C., Licci, M., Tolnay, M., Frank, S., & Scorrano, L. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.016 · Cited by 81
Self-citationDysregulation of organelle membrane contact sites in neurological diseases
Kim, S., Coukos, R., Gao, F., & Krainc, D. (2022) · Neuron · doi:10.1016/j.neuron.2022.04.020 · Cited by 82
Wang, X., Qian, J., Yang, Z., Song, Y., Pan, W., Ye, Y., Qin, X., Yan, X., Huang, X., Wang, X., et al. (2023) · Advanced Materials · doi:10.1002/adma.202310964 · Cited by 80
CRAC channels and Ca2+ signaling in mast cells
Capite, J. L. D., & Parekh, A. B. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2009.00808.x · Cited by 80
Functional multi-organelle units control inflammatory lipid metabolism of macrophages
Zimmermann, J. A., Lucht, K., Stecher, M., Badhan, C., Glaser, K. M., Epple, M. W., Koch, L. R., Deboutte, W., Manke, T., Ebnet, K., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01457-0 · Cited by 79
Organelle crosstalk in the kidney
Inoue, T., Maekawa, H., & Inagi, R. (2019) · Kidney International · doi:10.1016/j.kint.2018.11.035 · Cited by 79
Endoplasmic reticulum & mitochondrial calcium homeostasis: The interplay with viruses
Panda, S., Behera, S., Alam, M. F., & Syed, G. H. (2021) · Mitochondrion · doi:10.1016/j.mito.2021.03.008 · Cited by 79
Jiang, R.-Q., Li, Q., & Sheng, R. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.106761 · Cited by 79
Shioda, N., Ishikawa, K., Tagashira, H., Ishizuka, T., Yawo, H., & Fukunaga, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.349142 · Cited by 79
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 79
Corazao-Rozas, P., Guerreschi, P., André, F., Gabert, P.-E., Lancel, S., Dekiouk, S., Fontaine, D., Tardivel, M., Savina, A., Quesnel, B., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7790 · Cited by 79
A time to reap, a time to sow: Mitophagy and biogenesis in cardiac pathophysiology
Andres, A. M., Stotland, A., Queliconi, B. B., & Gottlieb, R. A. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.10.003 · Cited by 78
From Mitochondria to Atherosclerosis: The Inflammation Path
Suarez-Rivero, J. M., Pastor‐Maldonado, C. J., Povea-Cabello, S., Álvarez-Córdoba, M., Villalón-García, I., Talaverón-Rey, M., Suárez-Carrillo, A., Munuera-Cabeza, M., & Sánchez-Alcázar, J. A. (2021) · Biomedicines · doi:10.3390/biomedicines9030258 · Cited by 78
Resende, R., Fernandes, T., Pereira, A. C., Marques, A. P., & Pereira, C. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8231 · Cited by 78
snoRNA U17 Regulates Cellular Cholesterol Trafficking
Jinn, S., Brandis, K. A., Ren, A. A., Chacko, A., Dudley-Rucker, N., Gale, S. E., Sidhu, R., Fujiwara, H., Jiang, H., Olsen, B. N., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.04.010 · Cited by 78
Distelmaier, F., Valsecchi, F., Forkink, M., Vries, S. E. V. E., Swarts, H. G. P., Rodenburg, R. J., Verwiel, E. T. P., Smeitink, J. A. M., Willems, P. H. G. M., & Koopman, W. J. H. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4294 · Cited by 79
Metadata
- Authors
- de Brito, O. M., & Scorrano, L.
- Affiliations
- University of Geneva (CH)
- Corresponding author
- Scorrano, Luca
- ORCID
- Scorrano, Luca
- Venue
- Nature
- Published
- 2008-12-01
- Volume
- 456
- Issue
- 7222
- Pages
- 605-610
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2166432730
- Cited by
- 2,442
- References
- 35
- Citations by year
- 2026: 105 · 2025: 142 · 2024: 136 · 2023: 142 · 2022: 139 · 2021: 188 · 2020: 186 · 2019: 148 · 2018: 132 · 2017: 175 · 2016: 129 · 2015: 119 · 2014: 132 · 2013: 133 · 2012: 145
- FWCI
- 39.45
- Type
- journal article
- Language
- en
- Update notices
- correction (2014-09-10)
- Open access
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitofusin 2, mitochondrial calcium uptake, inositol 1,4,5-trisphosphate, calcium signaling, dynamin-related proteins, ER morphology, calcium homeostasis
- MeSH terms
- Animals, Calcium, Charcot-Marie-Tooth Disease, Endoplasmic Reticulum, Fibroblasts, HeLa Cells, Humans, Membrane Proteins, Mitochondria, Inositol 1,4,5-Trisphosphate, Calcium Signaling, GTP Phosphohydrolases, Mitochondrial Proteins, Mice, Organelle Shape
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
