Cited by 1,168Mitochondrial Function and PathologyCell death mechanisms and regulationAutophagy in Disease and Therapy

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Loss of OPA1 Perturbates the Mitochondrial Inner Membrane Structure and Integrity, Leading to Cytochrome c Release and Apoptosis

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Olichon, Aurélien, Baricault, Laurent, Gas, Nicole, Guillou, Emmanuelle, Valette, Annie, Belenguer, Pascale, Lenaers, Guy·2003·Journal of Biological Chemistry

DOI 10.1074/jbc.c200677200

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Abstract

OPA1 encodes a large GTPase related to dynamins, anchored to the mitochondrial cristae inner membrane, facing the intermembrane space. OPA1 haplo-insufficiency is responsible for the most common form of autosomal dominant optic atrophy (ADOA, MIM165500), a neuropathy resulting from degeneration of the retinal ganglion cells and optic nerve atrophy. Here we show that down-regulation of OPA1 in HeLa cells using specific small interfering RNA (siRNA) leads to fragmentation of the mitochondrial network concomitantly to the dissipation of the mitochondrial membrane potential and to a drastic disorganization of the cristae. These events are followed by cytochrome c release and caspase-dependent apoptotic nuclear events. Similarly, in NIH-OVCAR-3 cells, the OPA1 siRNA induces mitochondrial fragmentation and apoptosis, the latter being inhibited by Bcl2 overexpression. These results suggest that OPA1 is a major organizer of the mitochondrial inner membrane from which the maintenance of the cristae integrity depends. As loss of OPA1 commits cells to apoptosis without any other stimulus, we propose that OPA1 is involved in the cytochrome c sequestration and might be a target for mitochondrial apoptotic effectors. Our results also suggest that abnormal apoptosis is a possible pathophysiological process leading to the retinal ganglion cells degeneration in ADOA patients.

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Mitochondria as the central control point of apoptosis
Desagher, S., & Martinou, J. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01803-1 · Cited by 1,935
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755
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
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
Analysis of gene function in somatic mammalian cells using small interfering RNAs
Elbashir, S. M. (2002) · Methods · doi:10.1016/s1046-2023(02)00023-3 · Cited by 1,099
A Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis
Scorrano, L., Ashiya, M., Buttle, K., Weiler, S., Oakes, S. A., Mannella, C. A., & Korsmeyer, S. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00116-2 · Cited by 1,072
The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast
Bleazard, W., McCaffery, J. M., King, E. J., Bale, S., Mozdy, A. D., Tieu, Q., Nunnari, J. M., & Shaw, J. M. (1999) · Nature Cell Biology · doi:10.1038/13014 · Cited by 795
A Human Dynamin-related Protein Controls the Distribution of Mitochondria
Смирнова, Е. А., Shurland, D., Ryazantsev, S. N., & van der Bliek, A. M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.351 · Cited by 734
Mitochondrial Fusion in Human Cells Is Efficient, Requires the Inner Membrane Potential, and Is Mediated by Mitofusins
Legros, F., Lombès, A., Frachon, P., & Rojo, M. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-06-0330 · Cited by 676
The human dynamin‐related protein OPA1 is anchored to the mitochondrial inner membrane facing the inter‐membrane space
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
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Ishihara, N., Otera, H., Oka, T., & Mihara, K. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4830 · Cited by 77
Respiratory Chain Complexes in Dynamic Mitochondria Display a Patchy Distribution in Life Cells
Muster, B., Kohl, W., Wittig, I., Strecker, V., Joos, F., Haase, W., Bereiter‐Hahn, J., & Busch, K. B. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011910 · Cited by 74
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Corrado, M., Scorrano, L., & Campello, S. (2012) · International Journal of Cell Biology · doi:10.1155/2012/729290 · Cited by 77
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Chien, Y., Rosal, K. G., & Chung, B. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.10.030 · Cited by 75
Elevated hydrostatic pressure triggers release of OPA1 and cytochrome C, and induces apoptotic cell death in differentiated RGC-5 cells.
Ju, W., Keun-young Kim, A., Lindsey, J. D., Angert, M., Patel, A., Scott, R. T., Liu, Q., Crowston, J. G., Ellisman, M. H., Perkins, G. A., et al. (2009) · PubMed Central · Cited by 74
Real-time tracking mitochondrial dynamic remodeling with two-photon phosphorescent iridium (III) complexes
Huang, H., Yang, L., Zhang, P., Qiu, K., Huang, J., Chen, Y., Diao, J., Liu, J., Ji, L., Long, J., et al. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.01.014 · Cited by 75
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OPA1: How much do we know to approach therapy?
Dotto, V. D., Fogazza, M., Lenaers, G., Rugolo, M., Carelli, V., & Zanna, C. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.02.018 · Cited by 76
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Lin, H., Lai, R.-H., St, L., Lin, R.-C., Wang, M.-J., Lin, C.-C., Lee, H.-C., Ff, W., & Chen, J.-Y. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.106 · Cited by 74
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Sessions, D. T., & Kashatus, D. F. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03773-2 · Cited by 75
Mitostasis, Calcium and Free Radicals in Health, Aging and Neurodegeneration
Godoy, J. A., Ríos, J. A., Picón-Pagès, P., Herrera-Fernández, V., Swaby, B., Crepin, G., Vicente, R., Fernández‐Fernández, J. M., & Muñoz, F. J. (2021) · Biomolecules · doi:10.3390/biom11071012 · Cited by 73
In situ architecture of Opa1-dependent mitochondrial cristae remodeling
Fry, M. Y., Navarro, P. P., Hakim, P., Ananda, V. Y., Qin, X., Landoni, J. C., Rath, S. P., Inde, Z., Lugo, C. M., Luce, B. E., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00027-2 · Cited by 72
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Chen, L., & Knowlton, A. A. (2011) · Congestive Heart Failure · doi:10.1111/j.1751-7133.2011.00255.x · Cited by 73
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Heiduschka, P., Schnichels, S., Fuhrmann, N., Hofmeister, S., Schraermeyer, U., Wissinger, B., & Alavi, M. V. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.09-3606 · Cited by 72
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Marroquí, L., Tudurí, E., Alonso‐Magdalena, P., Quesada, I., Nadal, Á., & dos Santos, R. S. (2018) · Journal of Endocrinology · doi:10.1530/joe-18-0362 · Cited by 75
Regulating cell death at, on, and in membranes
Chi, X., Kale, J., Leber, B. F., & Andrews, D. W. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.06.002 · Cited by 75
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Chen, S., Liu, S., Wang, J., Wu, Q., Wang, A., Guan, H., Zhang, Q. Y., Zhang, D., Wang, X., Song, H., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.10.018 · Cited by 74
Impact of nitric oxide on metabolism in health and age‐related disease
Knott, A. B., & Bossy‐Wetzel, E. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01267.x · Cited by 73
Mitochondrial death pathways in yeast and mammalian cells
Cheng, W., Leach, K. M., & Hardwick, J. M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.04.012 · Cited by 73
Loss of SLC25A46 causes neurodegeneration by affecting mitochondrial dynamics and energy production in mice
Li, Z., Peng, Y., Hufnagel, R. B., Hu, Y., Zhao, C., Queme, L. F., Khuchua, Z. A., Driver, A. M., Dong, F., Lu, Q. R., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx262 · Cited by 70
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Hales, K. G. (2004) · Mitochondrion · doi:10.1016/j.mito.2004.05.007 · Cited by 70
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Dhingra, R., & Kirshenbaum, L. A. (2014) · Circulation Journal · doi:10.1253/circj.cj-14-0240 · Cited by 69
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Lee, H., & Yoon, Y. (2018) · Antioxidants · doi:10.3390/antiox7120186 · Cited by 73
The Dynamin-Related Protein Mgm1p Assembles into Oligomers and Hydrolyzes GTP To Function in Mitochondrial Membrane Fusion
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Zamberlan, M., Boeckx, A., Muller, F., Vinelli, F., Ek, O., Vianello, C., Coart, E., Shibata, K., Christian, A., Grespi, F., et al. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02304-6 · Cited by 72
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Staying in aerobic shape: how the structural integrity of mitochondria and mitochondrial DNA is maintained
Scott, S. V., Cassidy-Stone, A., Meeusen, S., & Nunnari, J. M. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00070-x · Cited by 68
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Austin, S., Mekis, R., Mohammed, S. E. M., Scalise, M., Wang, W., Galluccio, M., Pfeiffer, C., Borovec, T., Parapatics, K., Vitko, D., et al. (2022) · EMBO Reports · doi:10.15252/embr.202254978 · Cited by 72
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Plotnikov, E. Y., Vasileva, A. K., Arkhangelskaya, A. A., Pevzner, I. B., Skulachev, V. P., & Zorov, D. B. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.08.002 · Cited by 66
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Anderson, C. J., Kahl, A., Fruitman, H., Qian, L., Zhou, P., Manfredi, G., & Iadecola, C. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0469-4 · Cited by 62
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Lopez, E. G., Vue, Z., Katti, P., Neikirk, K., Biete, M., Lam, J., Beasley, H. K., Marshall, A. G., Rodman, T. A., Christensen, T. A., et al. (2021) · Cells · doi:10.3390/cells11010065 · Cited by 61
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Luce, K., Weil, A. C., & Osiewacz, H. D. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_9 · Cited by 61
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Ito, Y., Nakamura, M., Yamakoshi, T., Lin, J. J., Yatsuya, H., & Terasaki, H. (2007) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.07-0024 · Cited by 59
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Zhao, Y., Yang, M., & Liang, X. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05740-4 · Cited by 67
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Ashley, N., & Poulton, J. (2009) · Oncogene · doi:10.1038/onc.2009.242 · Cited by 57
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Shen, X. L., Zhang, Y., Xu, W., Liang, R., Zheng, J., Luo, Y., Wang, Y., & Huang, K. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.10.010 · Cited by 57
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Ju, W., Misaka, T., Kushnareva, Y., Nakagomi, S., Agarwal, N., Kubo, Y., Lipton, S. A., & Bossy‐Wetzel, E. (2005) · The Journal of Comparative Neurology · doi:10.1002/cne.20586 · Cited by 56
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Votruba, M. (2004) · Eye · doi:10.1038/sj.eye.6701570 · Cited by 56
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Caffin, F., Prola, A., Piquereau, J., Novotova, M., David, D. J., Garnier, A., Fortin, D., Alavi, M. V., Veksler, V., Ventura‐Clapier, R., et al. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.263079 · Cited by 55
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Authors: Olichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., & Lenaers, G.
Affiliations: Université Toulouse III - Paul Sabatier (FR)
Corresponding author: Belenguer, Pascale
ORCID: Olichon, Aurélien
Guillou, Emmanuelle
Belenguer, Pascale
Lenaers, Guy
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2003-03
Volume: 278
Issue: 10
Pages: 7743-7746
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.c200677200
OpenAlex: W1986996580
Cited by: 1,168
References: 27
Citations by year: 2026: 29 · 2025: 46 · 2024: 38 · 2023: 55 · 2022: 47 · 2021: 64 · 2020: 59 · 2019: 61 · 2018: 50 · 2017: 60 · 2016: 78 · 2015: 61 · 2014: 57 · 2013: 39 · 2012: 61
FWCI: 12.90
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6443 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: OPA1, mitochondrial fission, mitochondrial cristae, inner mitochondrial membrane, cytochrome c release, apoptosis, mitochondrial membrane potential, autosomal dominant optic atrophy, Bcl-2, GTPase, retinal ganglion cell death
MeSH terms: Cytochrome c Group, Humans, Intracellular Membranes, Microscopy, Electron, Mitochondria, Tumor Cells, Cultured, Apoptosis, GTP Phosphohydrolases

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Loss of OPA1 Perturbates the Mitochondrial Inner Membrane Structure and Integrity, Leading to Cytochrome c Release and Apoptosis

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