Cited by 623Mitochondrial Function and PathologyAutophagy in Disease and TherapyATP Synthase and ATPases Research

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Mitofusins and OPA1 Mediate Sequential Steps in Mitochondrial Membrane Fusion

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Song, Zhiyin, Ghochani, Mariam, McCaffery, J. Michael, Frey, Terrence G., Chan, David C.·2009·Molecular Biology of the Cell

DOI 10.1091/mbc.e09-03-0252PMC PMC2719570

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Abstract

Mitochondrial fusion requires the coordinated fusion of the outer and inner membranes. Three large GTPases--OPA1 and the mitofusins Mfn1 and Mfn2--are essential for the fusion of mammalian mitochondria. OPA1 is mutated in dominant optic atrophy, a neurodegenerative disease of the optic nerve. In yeast, the OPA1 ortholog Mgm1 is required for inner membrane fusion in vitro; nevertheless, yeast lacking Mgm1 show neither outer nor inner membrane fusion in vivo, because of the tight coupling between these two processes. We find that outer membrane fusion can be readily visualized in OPA1-null mouse cells in vivo, but these events do not progress to inner membrane fusion. Similar defects are found in cells lacking prohibitins, which are required for proper OPA1 processing. In contrast, double Mfn-null cells show neither outer nor inner membrane fusion. Mitochondria in OPA1-null cells often contain multiple matrix compartments bounded together by a single outer membrane, consistent with uncoupling of outer versus inner membrane fusion. In addition, unlike mitofusins and yeast Mgm1, OPA1 is not required on adjacent mitochondria to mediate membrane fusion. These results indicate that mammalian mitofusins and OPA1 mediate distinct sequential fusion steps that are readily uncoupled, in contrast to the situation in yeast.

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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
Self-citation
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
A Photoactivatable GFP for Selective Photolabeling of Proteins and Cells
Patterson, G. H., & Lippincott‐Schwartz, J. (2002) · Science · doi:10.1126/science.1074952 · Cited by 1,612
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
Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy
Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446
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
Functions and dysfunctions of mitochondrial dynamics
Detmer, S. A., & Chan, D. C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2275 · Cited by 1,369
Self-citation
OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28
Alexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330
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
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270

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Authors: Song, Z., Ghochani, M., McCaffery, J. M., Frey, T. G., & Chan, D. C.
Affiliations: California Institute of Technology (US)
Departments of ‡Physics and
Johns Hopkins University (US)
San Diego State University (US)
ORCID: Song, Zhiyin
McCaffery, J. Michael
Chan, David C.
Venue: Molecular Biology of the Cell
Publisher: American Society for Cell Biology (ASCB)
Published: 2009-08
Volume: 20
Issue: 15
Pages: 3525-3532
ISSN: 1059-1524 (ISSN-L)
1939-4586
DOI: 10.1091/mbc.e09-03-0252
PMC: PMC2719570
OpenAlex: W2164886443
Cited by: 623
References: 38
Citations by year: 2026: 32 · 2025: 45 · 2024: 46 · 2023: 39 · 2022: 62 · 2021: 41 · 2020: 41 · 2019: 35 · 2018: 36 · 2017: 36 · 2016: 31 · 2015: 33 · 2014: 33 · 2013: 38 · 2012: 31
FWCI: 9.79
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Molecular Biology of the Cell (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion, cc-by-nc-sa)
Funders: California Institute of Technology
National Institutes of Health
National Institute of General Medical Sciences (R01GM062967, GM062967)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords: mitochondrial fusion, mitofusins, Mfn1, mitofusin 2, OPA1, prohibitin, autosomal dominant optic atrophy, GTPase
MeSH terms: Animals, Cell Fusion, Cells, Cultured, Fibroblasts, Hybrid Cells, Membrane Fusion, Membrane Proteins, Microscopy, Electron, Polyethylene Glycols, Mice, Knockout, Microscopy, Confocal, GTP Phosphohydrolases, Mitochondrial Proteins, Adaptor Proteins, Signal Transducing, Green Fluorescent Proteins, Mitochondrial Membranes, Mice

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Mitofusins and OPA1 Mediate Sequential Steps in Mitochondrial Membrane Fusion

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