MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion

Cao, Yu-Lu; Meng, Shuxia; Chen, Yang; Feng, Jian-Xiong; Gu, Dong-Dong; Yu, Bing; Li, Yu-Jie; Yang, Jin-Yu; Liao, Shuang; Chan, David C.; Gao, Song

doi:10.1038/nature21077

Cited by 326Mitochondrial Function and PathologyAutophagy in Disease and TherapyProtein Structure and Dynamics

MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion

Open access

Cao, Yu-Lu, Meng, Shuxia, Chen, Yang, Feng, Jian-Xiong, Gu, Dong-Dong, Yu, Bing, Li, Yu-Jie, Yang, Jin-Yu +3 more·2017·Nature

DOI 10.1038/nature21077PMC PMC5319402

Open this paper in CoChat — free account

Abstract

Mitochondria are double-membraned organelles with variable shapes influenced by metabolic conditions, developmental stage, and environmental stimuli. Their dynamic morphology is a result of regulated and balanced fusion and fission processes. Fusion is crucial for the health and physiological functions of mitochondria, including complementation of damaged mitochondrial DNAs and the maintenance of membrane potential. Mitofusins are dynamin-related GTPases that are essential for mitochondrial fusion. They are embedded in the mitochondrial outer membrane and thought to fuse adjacent mitochondria via combined oligomerization and GTP hydrolysis. However, the molecular mechanisms of this process remain unknown. Here we present crystal structures of engineered human MFN1 containing the GTPase domain and a helical domain during different stages of GTP hydrolysis. The helical domain is composed of elements from widely dispersed sequence regions of MFN1 and resembles the 'neck' of the bacterial dynamin-like protein. The structures reveal unique features of its catalytic machinery and explain how GTP binding induces conformational changes to promote GTPase domain dimerization in the transition state. Disruption of GTPase domain dimerization abolishes the fusogenic activity of MFN1. Moreover, a conserved aspartate residue trigger was found to affect mitochondrial elongation in MFN1, probably through a GTP-loading-dependent domain rearrangement. Thus, we propose a mechanistic model for MFN1-mediated mitochondrial tethering, and our results shed light on the molecular basis of mitochondrial fusion and mitofusin-related human neuromuscular disorders.

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

Crossref · 10.1038/nature21077

Cites

53 of 53 references verified0 citation errors · 0 not checkable

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?

GTP hydrolysis of MFN1 causes a conformational change that allows the OMMs of opposing mitochondria to contact and fuse.
“GTP hydrolysis of MFN1 causes a conformational change that allows the OMMs of opposing mitochondria to contact and fuse [61, 62].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [62]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

A short history of SHELX
Sheldrick, G. M. (2007) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767307043930 · Cited by 87,861 · see citing works
CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617 · see citing works
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571 · see citing works
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581 · see citing works
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612 · see citing works
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147 · see citing works
XDS
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463 · see citing works
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,671 · see citing works
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115 · see citing works
Inference of macromolecular assemblies from crystalline state.
Krissinel, E., & Henrick, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.022 · Cited by 10,189 · see citing works
The Phyre2 web portal for protein modeling, prediction and analysis
Kelley, L. A., Mezulis, S., Yates, C. M., Wass, M. N., & Sternberg, M. J. E. (2015) · Nature Protocols · doi:10.1038/nprot.2015.053 · Cited by 9,652 · see citing works
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · see citing works
MOLREP : an Automated Program for Molecular Replacement
Vagin, A. A., & Teplyakov, A. (1997) · Journal of Applied Crystallography · doi:10.1107/s0021889897006766 · Cited by 4,791 · see citing works
Mitochondrial Fission, Fusion, and Stress
Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · see citing works
Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
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
Self-citation
Mitochondrial form and function
Friedman, J. R., & Nunnari, J. (2014) · Nature · doi:10.1038/nature12985 · Cited by 1,803 · see citing works
The dynamin superfamily: universal membrane tubulation and fission molecules?
Praefcke, G. J. K., & McMahon, H. T. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1313 · Cited by 1,380 · see citing works
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196 · see citing works
Self-citation
Metabolic regulation of mitochondrial dynamics
Mishra, P., & Chan, D. C. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201511036 · Cited by 1,096 · see citing works
Self-citation
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
Mitochondrial fragmentation in neurodegeneration.
Knott, A. B., Perkins, G., Schwarzenbacher, R., & Bossy-Wetzel, E. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2417 · Cited by 1,002 · see citing works
Structural Basis of Mitochondrial Tethering by Mitofusin Complexes
Koshiba, T., Detmer, S. A., Kaiser, J. T., Chen, H., McCaffery, J. M., & Chan, D. C. (2004) · Science · doi:10.1126/science.1099793 · Cited by 910 · see citing works
Self-citation
Dynamics of mitochondrial morphology in healthy cells and during apoptosis
Karbowski, M., & Youle, R. J. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401260 · Cited by 759 · see citing works
HKL2MAP: a graphical user interface for macromolecular phasing withSHELXprograms
Pape, T., & Schneider, T. R. (2004) · Journal of Applied Crystallography · doi:10.1107/s0021889804018047 · Cited by 743 · see citing works
Mitofusin 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
Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
Rojo, M., Legros, F., Chateau, D., & Lombès, A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.8.1663 · Cited by 555 · see citing works
Membrane bending by protein–protein crowding
Stachowiak, J. C., Schmid, E. M., Ryan, C. J., Ann, H. S., Sasaki, D. Y., Sherman, M. B., Geissler, P. L., Fletcher, D. A., & Hayden, C. C. (2012) · Nature Cell Biology · doi:10.1038/ncb2561 · Cited by 539 · see citing works
The Machinery of Mitochondrial Inheritance and Behavior
Yaffe, M. P. (1999) · Science · doi:10.1126/science.283.5407.1493 · Cited by 496 · see citing works
Inter-mitochondrial complementation: Mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA
Nakada, K., Inoue, K., Ono, T., Isobe, K., Ogura, A., Goto, Y., Nonaka, I., & Hayashi, J. (2001) · Nature Medicine · doi:10.1038/90976 · Cited by 430 · see citing works
Mitochondrial dynamics and division in budding yeast
Shaw, J. M., & Nunnari, J. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02246-2 · Cited by 375 · see citing works
Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins
Prakash, B., Praefcke, G. J. K., Renault, L., Wittinghofer, A., & Herrmann, C. (2000) · Nature · doi:10.1038/35000617 · Cited by 325 · see citing works
Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling
Daumke, O., Lundmark, R., Vallis, Y., Martens, S., Butler, P. J. G., & McMahon, H. T. (2007) · Nature · doi:10.1038/nature06173 · Cited by 317 · see citing works
Crystal structure of nucleotide-free dynamin
Faelber, K., Posor, Y., Gao, S., Held, M., Roske, Y., Schulze, D., Haucke, V., Noé, F., & Daumke, O. (2011) · Nature · doi:10.1038/nature10369 · Cited by 301 · see citing works
Self-citation
G domain dimerization controls dynamin's assembly-stimulated GTPase activity
Chappie, J. S., Acharya, S., Leonard, M., Schmid, S. L., & Dyda, F. (2010) · Nature · doi:10.1038/nature09032 · Cited by 294 · see citing works
Structural insights into oligomerization and mitochondrial remodelling of dynamin 1‐like protein
Fröhlich, C., Grabiger, S., Schwefel, D., Faelber, K., Rosenbaum, E., Mears, J. A., Rocks, O., & Daumke, O. (2013) · EMBO Journal · doi:10.1038/emboj.2013.74 · Cited by 290 · see citing works
The crystal structure of dynamin
Ford, M., Jenni, S., & Nunnari, J. (2011) · Nature · doi:10.1038/nature10441 · Cited by 282 · see citing works
Structural basis of oligomerization in the stalk region of dynamin-like MxA
Gao, S., von der Malsburg, A., Paeschke, S., Behlke, J., Haller, O., Kochs, G., & Daumke, O. (2010) · Nature · doi:10.1038/nature08972 · Cited by 254 · see citing works
Self-citation
Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes
Bian, X., Klemm, R. W., Liu, T. Y., Zhang, M., Sun, S., Sui, X., Liu, X., Rapoport, T. A., & Hu, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101643108 · Cited by 243 · see citing works
Correcting mitochondrial fusion by manipulating mitofusin conformations
Franco, A., Kitsis, R. N., Fleischer, J. A., Gavathiotis, E., Kornfeld, O. S., Gong, G., Biris, N., Benz, A. M., Qvit, N., Donnelly, S. K., et al. (2016) · Nature · doi:10.1038/nature20156 · Cited by 241 · see citing works
Self-citation
Mechanisms shaping cell membranes
Kozlov, M., Campelo, F., Liska, N., Chernomordik, L., Marrink, S., & McMahon, H. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.03.006 · Cited by 233 · see citing works
Structure of Myxovirus Resistance Protein A Reveals Intra- and Intermolecular Domain Interactions Required for the Antiviral Function
Gao, S., von der Malsburg, A., Dick, A., Faelber, K., Schroeder, G. F., Haller, O., Kochs, G., & Daumke, O. (2011) · Immunity · doi:10.1016/j.immuni.2011.07.012 · Cited by 223 · see citing works
Self-citation
A bacterial dynamin-like protein
Low, H. H., & Löwe, J. (2006) · Nature · doi:10.1038/nature05312 · Cited by 223 · see citing works
Membrane Curvature in Synaptic Vesicle Fusion and Beyond
McMahon, H. T., Kozlov, M. M., & Martens, S. (2010) · Cell · doi:10.1016/j.cell.2010.02.017 · Cited by 207 · see citing works
Structure of a Bacterial Dynamin-like Protein Lipid Tube Provides a Mechanism For Assembly and Membrane Curving
Low, H. H., Sachse, C., Amos, L., & Löwe, J. (2009) · Cell · doi:10.1016/j.cell.2009.11.003 · Cited by 176 · see citing works
Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A
Byrnes, L. J., & Sondermann, H. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012792108 · Cited by 176 · see citing works
The molecular mechanism of mitochondrial fusion
Hoppins, S. C., & Nunnari, J. M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.07.005 · Cited by 141 · see citing works
A mitofusin-dependent docking ring complex triggers mitochondrial fusion in vitro
Brandt, T., Cavellini, L., Kühlbrandt, W., & Cohen, M. M. (2016) · eLife · doi:10.7554/elife.14618 · Cited by 127 · see citing works
Mitochondrial Fusion Proteins and Human Diseases
Ranieri, M., Brajkovic, S., Riboldi, G. M., Ronchi, D., Rizzo, F., Bresolin, N., Corti, S. P., & Comi, G. P. (2013) · Neurology Research International · doi:10.1155/2013/293893 · Cited by 110 · see citing works
Structural basis for conformational switching and GTP loading of the large G protein atlastin
Byrnes, L. J., Singh, A. K., Szeto, K., Benvin, N. M., O'Donnell, J. P., Zipfel, W. R., & Sondermann, H. (2013) · The EMBO Journal · doi:10.1038/emboj.2012.353 · Cited by 95 · see citing works
Cis and trans interactions between atlastin molecules during membrane fusion
Liu, T. Y., Bian, X., Romano, F. B., Shemesh, T., Rapoport, T. A., & Hu, J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504368112 · Cited by 67 · see citing works
Transient Dimerization of Human MxA Promotes GTP Hydrolysis, Resulting in a Mechanical Power Stroke
Rennie, M. L., McKelvie, S. A., Bulloch, E. M. M., & Kingston, R. L. (2014) · Structure · doi:10.1016/j.str.2014.08.015 · Cited by 44 · see citing works
Intracellular curvature-generating proteins in cell-to-cell fusion
Richard, J., Leikina, E., Langen, R., Henne, W. M., Popova, M., Balla, T., McMahon, H. T., Kozlov, M. M., & Chernomordik, L. (2011) · Biochemical Journal · doi:10.1042/bj20111243 · Cited by 41 · see citing works

Flagged first, then by citations

Sorted by citations

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 · see citing works
Self-citation
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 · see citing works
Mitochondria in oxidative stress, inflammation and aging: from mechanisms to therapeutic advances
Xu, X., Pang, Y., & Fan, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02253-4 · Cited by 939 · see citing works
Mitochondrial fusion and fission: The fine‐tune balance for cellular homeostasis
Adebayo, M., Singh, S., Singh, A. P., & Dasgupta, S. (2021) · The FASEB Journal · doi:10.1096/fj.202100067r · Cited by 733 · see citing works
Reactive Oxygen Species and Mitochondrial Dynamics: The Yin and Yang of Mitochondrial Dysfunction and Cancer Progression
Ježek, J., Cooper, K. F., & Strich, R. (2018) · Antioxidants · doi:10.3390/antiox7010013 · Cited by 515 · see citing works
Molecular mechanisms of mitochondrial dynamics
Tábara, L. C., Segawa, M., & Prudent, J. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00785-1 · Cited by 431 · see citing works
Mitochondrial Fusion: The Machineries In and Out
Gao, S., & Hu, J. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.09.008 · Cited by 396 · see citing works
Self-citation
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
Determinants and outcomes of mitochondrial dynamics
Quintana–Cabrera, R., & Scorrano, L. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.012 · Cited by 345 · see citing works
Mitochondrial fission and fusion: A dynamic role in aging and potential target for age-related disease
Liu, Y. J., McIntyre, R. L., Janssens, G. E., & Houtkooper, R. H. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111212 · Cited by 334 · see citing works
Mitochondrial 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 312 · see citing works
Fission and fusion machineries converge at ER contact sites to regulate mitochondrial morphology
Abrisch, R. G., Gumbin, S. C., Wisniewski, B. T., Lackner, L. L., & Voeltz, G. K. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201911122 · Cited by 273 · see citing works
Phosphatidic Acid and Cardiolipin Coordinate Mitochondrial Dynamics
Kameoka, S., Adachi, Y., Okamoto, K., Iijima, M., & Sesaki, H. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.08.011 · Cited by 265 · see citing works
Structure, function, and regulation of mitofusin‐2 in health and disease
Chandhok, G., Lazarou, M., & Neumann, B. (2017) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12378 · Cited by 251 · see citing works
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 223 · see citing works
The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
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 191 · see citing works
Challenges of fluoride pollution in environment: Mechanisms and pathological significance of toxicity – A review
Wu, S., Wang, Y., Iqbal, M., Mehmood, K., Li, Y., Tang, Z., & Zhang, H. (2022) · Environmental Pollution · doi:10.1016/j.envpol.2022.119241 · Cited by 190 · see citing works
Self-citation
Evolving Concepts of Mitochondrial Dynamics
Dorn, G. W. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114358 · Cited by 187 · see citing works
Mitochondrial quality control in human health and disease
Liu, B., Xu, C.-Z., Liu, Y., Lu, Z., Fu, T.-L., Li, G., Deng, Y., Luo, G., Ding, S. Z., Li, N., et al. (2024) · Military Medical Research · doi:10.1186/s40779-024-00536-5 · Cited by 189 · see citing works
Regulation of Mammalian Mitochondrial Dynamics: Opportunities and Challenges
Yu, R., Lendahl, U., Nistér, M., & Zhao, J. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00374 · Cited by 173 · see citing works
Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset
Li, Y.-J., Cao, Y.-L., Feng, J.-X., Qi, Y., Meng, S., Yang, J., Zhong, Y.-T., Kang, S., Chen, X., Lan, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12912-0 · Cited by 167 · see citing works
Self-citation
A new mitofusin topology places the redox-regulated C terminus in the mitochondrial intermembrane space
Mattie, S., Riemer, J., Wideman, J. G., & McBride, H. M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201611194 · Cited by 158 · see citing works
Splice 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
Glucose limitation activates AMPK coupled SENP1-Sirt3 signalling in mitochondria for T cell memory development
He, J., Shangguan, X., Zhou, W., Cao, Y., Zheng, Q., Tu, J., Hu, G., Liang, Z., Jiang, C., Deng, L., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24619-2 · Cited by 153 · see citing works
Self-citation
The Role of Mitochondrial Dynamics and Mitophagy in Carcinogenesis, Metastasis and Therapy
Wang, Y., Liu, H., Cao, Y., Zhang, L., Huang, F., & Yi, C. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00413 · Cited by 149 · see citing works
Self-citation
Deorphanizing Caspase-3 and Caspase-9 Substrates In and Out of Apoptosis with Deep Substrate Profiling
Araya, L. E., Soni, I. V., Hardy, J. A., & Julien, O. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00456 · Cited by 146 · see citing works
Structural mechanism of mitochondrial membrane remodelling by human OPA1
von der Malsburg, A., Sapp, G., Zuccaro, K. E., von Appen, A., Moss, F. R., Kalia, R., Bennett, J. A., Abriata, L. A., Peraro, M. D., van der Laan, M., et al. (2023) · Nature · doi:10.1038/s41586-023-06441-6 · Cited by 144 · see citing works
The relationship between phospholipids and insulin resistance: From clinical to experimental studies
Chang, W., Hatch, G. M., Wang, Y., Yu, F., & Wang, M. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13984 · Cited by 142 · see citing works
Structural Insights into the Mechanism of Dynamin Superfamily Proteins
Jimah, J. R., & Hinshaw, J. E. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.11.003 · Cited by 134 · see citing works
Dynamics and number of trans-SNARE complexes determine nascent fusion pore properties
Bao, H., Das, D., Courtney, N. A., Jiang, Y., Briguglio, J. S., Lou, X., Roston, D., Cui, Q., Chanda, B., & Chapman, E. R. (2018) · Nature · doi:10.1038/nature25481 · Cited by 131 · see citing works
Evolutionary shift toward protein-based architecture in trypanosomal mitochondrial ribosomes
Ramrath, D. J. F., Niemann, M., Leibundgut, M., Bieri, P., Prange, C. J., Horn, E. K., Leitner, A., Boehringer, D., Schneider, A., & Ban, N. (2018) · Science · doi:10.1126/science.aau7735 · Cited by 130 · see citing works
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 · see citing works
Mitochondrial Dynamics in Neurodegenerative Diseases: Unraveling the Role of Fusion and Fission Processes
Grel, H., Woźnica, D., Ratajczak, K., Kalwarczyk, E., Anchimowicz, J., Świtlik, W. Z., Olejnik, P., Zielonka, P., Stobiecka, M., & Jakieła, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713033 · Cited by 129 · see citing works
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 128 · see citing works
Modulating mitofusins to control mitochondrial function and signaling
Zacharioudakis, E., Agianian, B., Vasantha Kumar, M. V., Biris, N., Garner, T. P., Rabinovich-Nikitin, I., Ouchida, A. T., Margulets, V., Nordstrøm, L. U., Riley, J. S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31324-1 · Cited by 127 · see citing works
Self-citation
The Balance of MFN2 and OPA1 in Mitochondrial Dynamics, Cellular Homeostasis, and Disease
Zanfardino, P., Amati, A., Perrone, M., & Petruzzella, V. (2025) · Biomolecules · doi:10.3390/biom15030433 · Cited by 125 · see citing works
Structure of Schlafen13 reveals a new class of tRNA/rRNA- targeting RNase engaged in translational control
Yang, J.-Y., Deng, X.-Y., Li, Y.-S., Ma, X.-C., Feng, J.-X., Yu, B., Chen, Y., Luo, Y.-L., Wang, X., Chen, M.-L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03544-x · Cited by 124 · see citing works
Self-citation
ER as master regulator of membrane trafficking and organelle function
Wenzel, E. M., Elfmark, L. A., Stenmark, H., & Raiborg, C. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202205135 · Cited by 116 · see citing works
Posttranslational modifications of mitochondrial fission and fusion proteins in cardiac physiology and pathophysiology
Adaniya, S. M., O‐Uchi, J., Cypress, M. W., Kusakari, Y., & Jhun, B. S. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00523.2018 · Cited by 115 · see citing works
Mitochondrial dynamics proteins as emerging drug targets
Zacharioudakis, E., & Gavathiotis, E. (2022) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.11.004 · Cited by 115 · see citing works
Mitochondrial Dysfunction in Oxidative Stress‐Mediated Intervertebral Disc Degeneration
Wang, D., Zheng, H., Zhou, W., Duan, Z., Jiang, S., Li, B., Zheng, X., & Jiang, L. (2022) · Orthopaedic Surgery · doi:10.1111/os.13302 · Cited by 112 · see citing works
Selenium Alleviates Cerebral Ischemia/Reperfusion Injury by Regulating Oxidative Stress, Mitochondrial Fusion and Ferroptosis
Shi, Y., Han, L., Zhang, X., Xie, L., Pan, P., & Chen, F. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03643-8 · Cited by 112 · see citing works
Mitochondrial Dynamic Dysfunction as a Main Triggering Factor for Inflammation Associated Chronic Non-Communicable Diseases
Geto, Z., Molla, M. D., Challa, F., Belay, Y., & Getahun, T. (2020) · Journal of Inflammation Research · doi:10.2147/jir.s232009 · Cited by 110 · see citing works
Intercellular transfer of activated STING triggered by RAB22A-mediated non-canonical autophagy promotes antitumor immunity
Gao, Y., Zheng, X., Chang, B., Lin, Y., Huang, X., Wang, W., Ding, S., Zhan, W., Wang, S., Xiao, B.-B., et al. (2022) · Cell Research · doi:10.1038/s41422-022-00731-w · Cited by 107 · see citing works
Self-citation
The role of mitochondrial dynamics in oocyte and early embryo development
Yildirim, R. M., & Seli, E. U. (2024) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2024.01.007 · Cited by 106 · see citing works
Structural basis for GTP hydrolysis and conformational change of MFN1 in mediating membrane fusion
Yan, L., Qi, Y., Huang, X., Yu, C., Lan, L., Guo, X., Rao, Z., Hu, J., & Lou, Z. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0034-8 · Cited by 100 · see citing works
High‐Fidelity Trapping of Spatial–Temporal Mitochondria with Rational Design of Aggregation‐Induced Emission Probes
Zhang, J., Wang, Q., Guo, Z., Zhang, S., Yan, C., Tian, H., & Zhu, W. (2019) · Advanced Functional Materials · doi:10.1002/adfm.201808153 · Cited by 100 · see citing works
Mitofusin 2 Participates in Mitophagy and Mitochondrial Fusion Against Angiotensin II-Induced Cardiomyocyte Injury
Xiong, W., Ma, Z., An, D., Liu, Z., Cai, W., Bai, Y., Zhan, Q., Lai, W., Zeng, Q., Ren, H., et al. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00411 · Cited by 100 · see citing works
Restoring mitofusin balance prevents axonal degeneration in a Charcot-Marie-Tooth type 2A model
Zhou, Y., Carmona, S., Muhammad, A. K. M. G., Bell, S., Landeros, J., Vazquez, M., Ho, R., Franco, A., Lü, B., Dorn, G. W., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci124194 · Cited by 99 · see citing works
Highlighting the endoplasmic reticulum-mitochondria connection: Focus on Mitofusin 2
Filadi, R., Greotti, E., & Pizzo, P. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.01.003 · Cited by 97 · see citing works
Mitochondria-ER contact mediated by MFN2-SERCA2 interaction supports CD8 + T cell metabolic fitness and function in tumors
Yang, J., Xing, X., Luo, L., Zhou, X., Feng, J.-X., Huang, K., Liu, H., Jin, S., Liu, Y.-N., Zhang, S.-H., et al. (2023) · Science Immunology · doi:10.1126/sciimmunol.abq2424 · Cited by 96 · see citing works
Self-citation
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 94 · see citing works
Mitochondria: Potential Targets for Osteoarthritis
Mao, X.-J., Fu, P., Wang, L.-L., & Xiang, C. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.581402 · Cited by 89 · see citing works
Mitofusin gain and loss of function drive pathogenesis in Drosophila models of CMT2A neuropathy
Fissi, N. E., Rojo, M., Aouane, A., Karataş, E., Poliacikova, G., David, C., Royet, J., & Rival, T. (2018) · EMBO Reports · doi:10.15252/embr.201745241 · Cited by 90 · see citing works
Functional Interplay between Cristae Biogenesis, Mitochondrial Dynamics and Mitochondrial DNA Integrity
Kondadi, A. K., Anand, R., & Reichert, A. S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174311 · Cited by 90 · see citing works
Lentinan-functionalized Selenium Nanoparticles target Tumor Cell Mitochondria via TLR4/TRAF3/MFN1 pathway
Liu, H., Qin, Y., Zhao, Z., Zhang, Y., Yang, J., Zhai, D., Cui, F., Luo, C., Lu, M.-X., Liu, P.-P., et al. (2020) · Theranostics · doi:10.7150/thno.46467 · Cited by 88 · see citing works
Self-citation
Connecting mitochondrial dynamics and life-or-death events via Bcl-2 family proteins
Aouacheria, A., Baghdiguian, S., Lamb, H. M., Huska, J. D., Pineda, F. J., & Hardwick, J. M. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.04.009 · Cited by 81 · see citing works
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 81 · see citing works
Small molecule agonist of mitochondrial fusion repairs mitochondrial dysfunction
Guo, Y., Zhang, H., Chen, Y., Shen, B., Zhang, Y., Guo, X., Sun, S., Fan, Y., Yan, J., Liu, R., et al. (2023) · Nature Chemical Biology · doi:10.1038/s41589-022-01224-y · Cited by 81 · see citing works
Self-citation
Mitochondrial Dysfunction in Neurodegenerative Diseases: Mechanisms and Corresponding Therapeutic Strategies
Meng, K., Jia, H., Hou, X., Zhu, Z., Lu, Y., Feng, Y., Feng, J., Xia, Y., Tan, R., Cui, F., et al. (2025) · Biomedicines · doi:10.3390/biomedicines13020327 · Cited by 80 · see citing works
Self-citation
The advantage of channeling nucleotides for very processive functions
Zala, D., Schlattner, U., Desvignes, T., Bobe, J., Roux, A., Chavrier, P., & Boissan, M. (2017) · F1000Research · doi:10.12688/f1000research.11561.2 · Cited by 79 · see citing works
Redox regulation of UPR signalling and mitochondrial ER contact sites
Casas-Martinez, J. C., Afshin Samali, A., & McDonagh, B. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05286-0 · Cited by 79 · see citing works
Mitochondrial dynamics: The dynamin superfamily and execution by collusion
Ramachandran, R. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.07.039 · Cited by 77 · see citing works
FUNDC2 promotes liver tumorigenesis by inhibiting MFN1-mediated mitochondrial fusion
Li, S., Han, S., Zhang, Q., Zhu, Y., Zhang, H., Wang, J., Zhao, Y., Zhao, J., Su, L., Li, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31187-6 · Cited by 77 · see citing works
Mitochondria: Insights into Crucial Features to Overcome Cancer Chemoresistance
Genovese, I., Carinci, M., Modesti, L., Aguiari, G., Pinton, P., & Giorgi, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094770 · Cited by 76 · see citing works
Insulin and Its Key Role for Mitochondrial Function/Dysfunction and Quality Control: A Shared Link between Dysmetabolism and Neurodegeneration
Galizzi, G., & Carlo, M. D. (2022) · Biology · doi:10.3390/biology11060943 · Cited by 76 · see citing works
Dynamic death decisions: How mitochondrial dynamics shape cellular commitment to apoptosis and ferroptosis
Khatun, J., Gelles, J. D., & Chipuk, J. E. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.09.004 · Cited by 75 · see citing works
Research progress on the pharmacological effects of berberine targeting mitochondria
Fang, X., Wu, H., Wei, J., Miao, R., Zhang, Y., & Tian, J. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.982145 · Cited by 72 · see citing works
Mitochondrial Membrane Dynamics—Functional Positioning of OPA1
Lee, H., & Yoon, Y. (2018) · Antioxidants · doi:10.3390/antiox7120186 · Cited by 70 · see citing works
Mitochondrial dynamics and mitochondrial autophagy: Molecular structure, orchestrating mechanism and related disorders
Wang, H., Luo, W., Chen, H., Cai, Z., & Xu, G. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101847 · Cited by 69 · see citing works
Cryo-EM structures of S-OPA1 reveal its interactions with membrane and changes upon nucleotide binding
Zhang, D., Zhang, Y., Ma, J., Zhu, C., Niu, T., Chen, W., Pang, X., Zhai, Y., & Sun, F. (2020) · eLife · doi:10.7554/elife.50294 · Cited by 68 · see citing works
Metabolic features and regulation of the healing cycle—A new model for chronic disease pathogenesis and treatment
Naviaux, R. K. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.08.001 · Cited by 68 · see citing works
Mitofusins as mitochondrial anchors and tethers
Dorn, G. W. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.04.016 · Cited by 68 · see citing works
Chemotherapy Resistance: Role of Mitochondrial and Autophagic Components
Bahar, E., Han, S., Kim, J., & Yoon, H. (2022) · Cancers · doi:10.3390/cancers14061462 · Cited by 66 · see citing works
Zika Virus-Induced Neuronal Apoptosis via Increased Mitochondrial Fragmentation
Yang, S., Gorshkov, K., Lee, E. M., Xu, M., Cheng, Y., Sun, N., Soheilian, F., de Val, N., Ming, G., Song, H., et al. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.598203 · Cited by 65 · see citing works
Myoferlin controls mitochondrial structure and activity in pancreatic ductal adenocarcinoma, and affects tumor aggressiveness
Rademaker, G., Hennequière, V., Brohée, L., Nokin, M., Lovinfosse, P., Durieux, F., Gofflot, S., Bellier, J., Costanza, B., Herfs, M. F., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0287-z · Cited by 64 · see citing works
Relationship between OPA1 and cardiolipin in mitochondrial inner-membrane fusion
Ban, T., Kohno, H., Ishihara, T., & Ishihara, N. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.05.016 · Cited by 63 · see citing works
An ER phospholipid hydrolase drives ER-associated mitochondrial constriction for fission and fusion
Nguyen, T. T., & Voeltz, G. K. (2022) · eLife · doi:10.7554/elife.84279 · Cited by 62 · see citing works
The lifecycle of skeletal muscle mitochondria in obesity
Pileggi, C. A., Parmar, G., & Harper, M. (2021) · Obesity Reviews · doi:10.1111/obr.13164 · Cited by 61 · see citing works
Photoactivatable Biomedical Materials Based on Luminogens with Aggregation‐Induced Emission (AIE) Characteristics
Sun, J., Li, H., Gu, X., & Tang, B. Z. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202101177 · Cited by 59 · see citing works
Molecular mechanisms of mitophagy and its roles in neurodegenerative diseases
Li, X., Huang, L., Lan, J., Feng, X., Li, P., Wu, L., & Peng, Y. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2020.105240 · Cited by 57 · see citing works
The MFN1 and MFN2 mitofusins promote clustering between mitochondria and peroxisomes
Huo, Y., Sun, W., Shi, T., Gao, S., & Zhuang, M. (2022) · Communications Biology · doi:10.1038/s42003-022-03377-x · Cited by 56 · see citing works
Self-citation
Lipid and Lipidation in Membrane Fusion
Sardar, A., Dewangan, N., Panda, B., Bhowmick, D., & Tarafdar, P. K. (2022) · The Journal of Membrane Biology · doi:10.1007/s00232-022-00267-5 · Cited by 56 · see citing works
Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1
Yan, L., Qi, Y., Ricketson, D., Li, L., Subramanian, K., Zhao, J., Yu, C., Wu, L., Sarsam, R. D., Wong, M., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1919116117 · Cited by 56 · see citing works
Targeting mitochondrial shape: at the heart of cardioprotection
Hernández‐Reséndiz, S., Prakash, A., Loo, S. J., Semenzato, M., Chinda, K., Crespo-Avilan, G. E., Dam, L. C., Lu, S., Scorrano, L., & Hausenloy, D. J. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-01019-9 · Cited by 55 · see citing works
Mitochondrial quality control in diabetes mellitus and complications: molecular mechanisms and therapeutic strategies
Chen, Y., Liu, X., Liu, Y., Li, Y., Li, D., Mei, Z., & Deng, Y. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07936-y · Cited by 54 · see citing works
Self-citation
The heptad repeat domain 1 of Mitofusin has membrane destabilization function in mitochondrial fusion
Daste, F., Sauvanet, C., Bavdek, A., Baye, J., Pierre, F., Borgne, R. L., David, C., Rojo, M., Fuchs, P., & Tareste, D. C. (2018) · EMBO Reports · doi:10.15252/embr.201643637 · Cited by 54 · see citing works
The emerging role of skeletal muscle mitochondrial dynamics in exercise and ageing
Casuso, R. A., & Huertas, J. R. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101025 · Cited by 54 · see citing works
Mitofusins: from mitochondria to fertility
Zhao, S., Heng, N., Wang, H., Wang, H., Zhang, H., Gong, J., Hu, Z., & Zhu, H. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04386-z · Cited by 53 · see citing works
Vitamin D 3 attenuates cisplatin-induced intestinal injury by inhibiting ferroptosis, oxidative stress, and ROS-mediated excessive mitochondrial fission
Liu, X., Wang, S., Jin, S., Huang, S., & Liu, Y. (2022) · Food & Function · doi:10.1039/d2fo01028c · Cited by 51 · see citing works
From dysfunction to healing: advances in mitochondrial therapy for Osteoarthritis
Zhang, M., Wu, J., Cai, K., Liu, Y., Lu, B., Zhang, J., Xu, J., Gu, C., & Chen, T. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05799-z · Cited by 51 · see citing works
The Calcilytic Drug Calhex-231 Ameliorates Vascular Hyporesponsiveness in Traumatic Hemorrhagic Shock by Inhibiting Oxidative Stress and miR-208a-Mediated Mitochondrial Fission
Yan, L., Peng, X., Hu, Y., Xue, M., Li, T., Liu, L., & Yang, G. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/4132785 · Cited by 49 · see citing works
Structural insights into G domain dimerization and pathogenic mutation of OPA1
Yu, C., Zhao, J., Yan, L., Qi, Y., Guo, X., Lou, Z., Hu, J., & Rao, Z. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201907098 · Cited by 49 · see citing works
Role of Mitofusins and Mitophagy in Life or Death Decisions
Joaquim, M., & Escobar‐Henriques, M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.572182 · Cited by 49 · see citing works
Mitochondrial Dynamics: Molecular Mechanisms, Related Primary Mitochondrial Disorders and Therapeutic Approaches
Nottia, M. D., Verrigni, D., Torraco, A., Rizza, T., Bertini, E., & Carrozzo, R. (2021) · Genes · doi:10.3390/genes12020247 · Cited by 48 · see citing works
Ceramides and mitochondrial homeostasis
Ding, S. Z., Li, G., Fu, T., Zhang, T., Lu, X., Li, N., & Geng, Q. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111099 · Cited by 48 · see citing works
Sequences flanking the transmembrane segments facilitate mitochondrial localization and membrane fusion by mitofusin
Huang, X., Zhou, X., Hu, X., Joshi, A. S., Guo, X., Zhu, Y., Chen, Q., Prinz, W. A., & Hu, J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708782114 · Cited by 48 · see citing works
Viral Infection Modulates Mitochondrial Function
Li, X., Wu, K., Zeng, S., Zhao, F., Fan, J., Li, Z., Yi, L., Ding, H., Zhao, M., Fan, S., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084260 · Cited by 48 · see citing works
The structural biology of the dynamin‐related proteins: New insights into a diverse, multitalented family
Ford, M. G. J., & Chappie, J. S. (2019) · Traffic · doi:10.1111/tra.12676 · Cited by 47 · see citing works

Structural basis for GTP hydrolysis and conformational change of MFN1 in mediating membrane fusion
Yan, L., Qi, Y., Huang, X., Yu, C., Lan, L., Guo, X., Rao, Z., Hu, J., & Lou, Z. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0034-8 · Cited by 100 · see citing works
Structures of human mitofusin 1 provide insight into mitochondrial tethering
Qi, Y., Yan, L., Yu, C., Guo, X., Zhou, X., Hu, X., Huang, X., Rao, Z., Lou, Z., & Hu, J. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201609019 · Cited by 180 · see citing works
Structural and mechanistic investigation on mitochondrial fusion
Ozeir, M., Cavellini, L., Henri, J., & Cohen, M. M. (2022) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2022.148800
Time-resolved tmFRET reveals GTP-coupled conformational changes in Mfn1
Hurwitz, S. M., Zagotta, W. N., Gordon, S. E., & Hoppins, S. C. (2026) · The Journal of Cell Biology · doi:10.1083/jcb.202511077 · Cited by 2 · see citing works
Structure-Function analysis of the yeast mitofusin Fzo1
Cavellini, L., Ozeir, M., Morcillo-Parra, M. Á., Tang, Y., Vandjour, É., Chenuel, T., Henri, J., Meyer, P., & Cohen, M. M. (2023) · HAL

Authors: Cao, Y.-L., Meng, S., Chen, Y., Feng, J.-X., Gu, D.-D., Yu, B., Li, Y.-J., Yang, J.-Y., Liao, S., Chan, D. C., & Gao, S.
Affiliations: Sun Yat-sen University (CN)
California Institute of Technology (US)
Corresponding author: Gao, Song
ORCID: Cao, Yu-Lu
Chen, Yang
Yu, Bing
Liao, Shuang
Chan, David C.
Gao, Song
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2017-01-23
Volume: 542
Issue: 7641
Pages: 372-376
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature21077
PMC: PMC5319402
OpenAlex: W2581248702
Cited by: 326
References: 53
Citations by year: 2026: 28 · 2025: 37 · 2024: 22 · 2023: 40 · 2022: 44 · 2021: 35 · 2020: 35 · 2019: 34 · 2018: 35 · 2017: 16
FWCI: 13.41
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: National Institute of General Medical Sciences (R01GM119388, R01GM083121, R01GM110039)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: mitofusin 1, mitochondrial fusion, GTP hydrolysis, conformational change, dynamin-related GTPase, mitochondrial outer membrane, helical domain, mitochondrial elongation, mitochondrial tethering, neuromuscular disorders, crystal structure
MeSH terms: Protein Domains, Amino Acid Sequence, Guanosine Triphosphate, Humans, Hydrolysis, Membrane Fusion, Membrane Potentials, Mitochondria, Models, Molecular, Tryptophan, Crystallography, X-Ray, GTP Phosphohydrolases, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Biocatalysis, Protein Multimerization, Mitochondrial Dynamics

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

MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks