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Loss of Prohibitin Membrane Scaffolds Impairs Mitochondrial Architecture and Leads to Tau Hyperphosphorylation and Neurodegeneration
Open accessAbstract
Fusion and fission of mitochondria maintain the functional integrity of mitochondria and protect against neurodegeneration, but how mitochondrial dysfunctions trigger neuronal loss remains ill-defined. Prohibitins form large ring complexes in the inner membrane that are composed of PHB1 and PHB2 subunits and are thought to function as membrane scaffolds. In Caenorhabditis elegans, prohibitin genes affect aging by moderating fat metabolism and energy production. Knockdown experiments in mammalian cells link the function of prohibitins to membrane fusion, as they were found to stabilize the dynamin-like GTPase OPA1 (optic atrophy 1), which mediates mitochondrial inner membrane fusion and cristae morphogenesis. Mutations in OPA1 are associated with dominant optic atrophy characterized by the progressive loss of retinal ganglion cells, highlighting the importance of OPA1 function in neurons. Here, we show that neuron-specific inactivation of Phb2 in the mouse forebrain causes extensive neurodegeneration associated with behavioral impairments and cognitive deficiencies. We observe early onset tau hyperphosphorylation and filament formation in the hippocampus, demonstrating a direct link between mitochondrial defects and tau pathology. Loss of PHB2 impairs the stability of OPA1, affects mitochondrial ultrastructure, and induces the perinuclear clustering of mitochondria in hippocampal neurons. A destabilization of the mitochondrial genome and respiratory deficiencies manifest in aged neurons only, while the appearance of mitochondrial morphology defects correlates with tau hyperphosphorylation in the absence of PHB2. These results establish an essential role of prohibitin complexes for neuronal survival in vivo and demonstrate that OPA1 stability, mitochondrial fusion, and the maintenance of the mitochondrial genome in neurons depend on these scaffolding proteins. Moreover, our findings establish prohibitin-deficient mice as a novel genetic model for tau pathologies caused by a dysfunction of mitochondria and raise the possibility that tau pathologies are associated with other neurodegenerative disorders caused by deficiencies in mitochondrial dynamics.
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“inactivation of PHB-2 in mice brain affects mitochondrial structure and activity resulting in neurodegeneration by hyperphosphorylation of Tau (Merkwirth et al., 2012)”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Merkwirth et al., 2012
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Citations
Cites
Generalized lacZ expression with the ROSA26 Cre reporter strain
Soriano, P. (1999) · Nature Genetics · doi:10.1038/5007 · Cited by 5,237
Premature ageing in mice expressing defective mitochondrial DNA polymerase
Trifunovic, A., Wredenberg, A., Falkenberg, M., Spelbrink, J. N., Rovio, A. T., Bruder, C. E., Bohlooly-Y, M., Gidlöf, S., Oldfors, A., Wibom, R., et al. (2004) · Nature · doi:10.1038/nature02517 · Cited by 2,734
Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002
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
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
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
Ishihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S. O., Masuda, K., Otera, H., Nakanishi, Y., Nonaka, I., Goto, Y.-I., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1907 · Cited by 1,066
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
Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965
Flagged first, then by citations
Research works printed but not linked: 1
- D DiBella, 2008, AFG3L2 mutations cause autosomal dominant ataxia SCA28 and reveal an essential role of the m-AAA AFG3L2 homocomplex in the cerebellum, Annual meeting of the American Society of Human Genetics
Cited by
Sorted by citations
Items 101–162 of 162
Lizama, B. N., Palubinsky, A. M., & McLaughlin, B. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.08.013 · Cited by 14
Lachén‐Montes, M., González-Morales, A., Alonso, M. P., Ausín, K., Gómez-Ochoa, M., Zelaya, M. V., Ferrer, I., Pérez‐Mediavilla, A., Fernández‐Irigoyen, J., & Santamaría, E. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00141 · Cited by 16
Kahl, A., Anderson, C. J., Qian, L., Voss, H. U., Manfredi, G., Iadecola, C., & Zhou, P. (2017) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x17720371 · Cited by 14
Chen, Y., Xu, R., Liu, Q., Zeng, Y., Chen, W., Liu, Y., Cao, Y., Liu, G., & Chen, Y. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04206-4 · Cited by 14
Xu, L., Xiang, W., Yang, J., Gao, J. X., Wang, X., Li, M., Ye, K., Zhao, X. H., Zhang, X. D., Jin, L., et al. (2024) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02937-1 · Cited by 13
Xu, Y. X. Z., Bassi, G., & Mishra, S. (2019) · Biology of Sex Differences · doi:10.1186/s13293-019-0239-5 · Cited by 13
Hou, C.-C., Wei, C., Lu, C.-P., Gao, X., Yang, W., & Zhu, J. (2017) · Oncotarget · doi:10.18632/oncotarget.21961 · Cited by 13
Wu, S., Liu, X., Yang, H., Ma, W., & Qin, Z. (2023) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2023.08.2194 · Cited by 13
Tau phosphorylation and OPA1 proteolysis are unrelated events: Implications for Alzheimer's Disease
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Jiang, T., Wang, J., Li, C., Cao, G., & Wang, X. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7494863 · Cited by 12
Guérin, A., Angebault, C., Kinet, S., Cazevieille, C., Rojo, M., Fauconnier, J., Lacampagne, A., Mourier, A., Taylor, N. N., Barbara, P. D. S., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102431 · Cited by 12
Cuadrado‐Tejedor, M., Pérez-González, M., Alfaro‐Ruiz, R., Badesso, S., Sucunza, D., Espelosin, M., Ursúa, S., Lachén‐Montes, M., Fernández‐Irigoyen, J., Santamaría, E., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111950 · Cited by 11
Psaltis, C. E., Fussner, L. A., Yaeger, M. J., Aloor, J. J., Reece, S. W., Kilburg-Basnyat, B. J., Varikuti, S., Luo, B., Inks, M., Sergin, S., et al. (2023) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2023.102540 · Cited by 12
Prohibitin Signaling at the Kidney Filtration Barrier
Ising, C., & Brinkkoetter, P. T. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_29 · Cited by 11
Shi, Y., Li, Q., Sun, F., Zhu, C., Ma, S., Qin, D., Li, Q., & Li, T. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.06.037 · Cited by 11
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Valdés‐Tovar, M., Rodríguez‐Ramírez, A. M., Rodríguez-Cárdenas, L., Sotelo-Ramírez, C. E., Camarena, B., Sanabrais‐Jiménez, M. A., Solís‐Chagoyán, H., Argueta, J., & López-Riquelme, G. O. (2022) · World Journal of Psychiatry · doi:10.5498/wjp.v12.i2.268 · Cited by 11
Prohibitins in neurodegeneration and mitochondrial homeostasis
Fernandez-Abascal, J., & Artal‐Sanz, M. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.1043300 · Cited by 10
Prohibitin: A hypothetical target for sex-based new therapeutics for metabolic and immune diseases
Mishra, S., & Nyomba, B. L. G. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219828362 · Cited by 13
Rab32/38 and the xenophagic restriction of intracellular bacteria replication
Tang, B. L. (2016) · Microbes and Infection · doi:10.1016/j.micinf.2016.05.006 · Cited by 10
Tie-song, L., Wang, Y., Gao, Y., & Li, Q. (2014) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2014.11.016 · Cited by 9
Discovery of bactericides as an acute mitochondrial membrane damage inducer
Houston, R., Sekine, Y., Larsen, M. B., Murakami, K., Mullett, S. J., Wendell, S. G., Narendra, D. P., Chen, B. B., & Sekine, S. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-04-0191 · Cited by 9
The Role of Prohibitin-2 in Diseases
Liu, F., Zhang, Y., Guo, Z., & Ren, A. (2023) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2809211 · Cited by 8
Sakai, Y., & Sokolowski, B. H. A. (2015) · Journal of Neuroscience Research · doi:10.1002/jnr.23538 · Cited by 8
Mouse models of central nervous system ageing
Heng, Y., Eggen, B. J. L., Boddeke, E., & Kooistra, S. M. (2017) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2018.10.002 · Cited by 8
Phb1:Phb2 heterodimers in the mitochondria—beyond functional interdependence
Mishra, S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.l119.010788 · Cited by 8
Role of Prohibitins as Guardians of mitochondrial homeostasis
Champsi, S., & Hood, D. A. (2025) · Mitochondrion · doi:10.1016/j.mito.2025.102075 · Cited by 7
Mitochondrial Precursor Overaccumulation Stress
Coyne, L. P., & Chen, X. J. (2026) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051424-061016 · Cited by 7
Brunette, S., Sharma, A., Bell, R. A. V., Puente, L. G., & Megeney, L. A. (2023) · Microbial Cell · doi:10.15698/mic2023.08.801 · Cited by 7
Fatemi, S. H., Folsom, T. D., Eschenlauer, A. C., & Chekouo, T. (2025) · The Cerebellum · doi:10.1007/s12311-025-01880-5 · Cited by 7
Konovalova, S. A., Torregrosa‐Muñumer, R., Manjunath, P., Liu, X., Baral, S., Fatima, K., Holopainen, M., Kvist, J., Rajendran, J., Yang, Y., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2210599120 · Cited by 6
Ye, X., Zhao, Y., Zhao, L., Sun, Y., Yang, J., & Yang, W. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109152 · Cited by 5
Bettahi, I., Krishnankutty, R., Jaganjac, M., Suleiman, N., Ramanjaneya, M., Jerobin, J., Hassoun, S., Alkasem, M., Abdelhakam, I., Iskandarani, A., et al. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.1024832 · Cited by 5
Bernstein, H., Smalla, K., Keilhoff, G., Dobrowolny, H., Kreutz, M. R., & Steiner, J. H. (2023) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2023.102321 · Cited by 4
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Sugimoto, K., Miyazawa, T., Miyazaki, K., Yanagida, H., Enya, T., Nishi, H., Wada, N., Okada, M., & Takemura, T. (2016) · Clinical and Experimental Nephrology · doi:10.1007/s10157-016-1325-1 · Cited by 4
Vila, È., Pinacho, R., Prades, R., Tarragó, T., Castro, E., Munarriz‐Cuezva, E., Meana, J. J., Eugui-Anta, A., Roldán, M., Vera-Montecinos, A., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076016 · Cited by 4
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Nezhyva, M., Shahen-Zoabi, S., Kabirova, M., Bentov‐Arava, E., Shalev, O., Andrén, P. E., Thornton, C., Yaka, R., Margulis, K., & Jansson, E. T. (2024) · PNAS Nexus · doi:10.1093/pnasnexus/pgae458 · Cited by 3
Zhong, Y., Zhou, L. F., Wang, H., Lin, S., Liu, T., Kong, X., Xiao, G., & Gao, H. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105601 · Cited by 3
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Verma, G., Dixit, A., & Nunemaker, C. S. (2020) · Journal of Diabetes Research · doi:10.1155/2020/7814628 · Cited by 2
Park, H., Kwon, H. S., Lee, K., Kim, Y. E., Son, J., Choi, N.-Y., Han, M., Park, D. W., Kim, S., & Koh, S. (2024) · Aging · doi:10.18632/aging.205489 · Cited by 3
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Tan, S., Kennedy, B. K., & Wong, E. S. P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821562-3.00037-x · Cited by 2
Lachén‐Montes, M., Mendizuri, N., Ausín, K., Echaide, M., Blanco, E., Chocarro, L., de Toro, M., Escors, D., Fernández‐Irigoyen, J., Kochan, G. T., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.866564 · Cited by 2
Lu, J., Rao, S. R., Knowles, H. J., Zhan, H., Gámez, B., Qin, M., Platt, E., Frost, L. R., Allen, T.-J., Marshall, G. B., et al. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02799-x · Cited by 2
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Cantor, R. M., & Lowe, J. K. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-817986-4.00003-1 · Cited by 1
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Chang, C., Chang, Y., Chuang, P., Nguyen, T. N. A., Chou, F.-Y., Cheng, S., Chen, H., Jin, L., Carvalho, K., Huin, V., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.25.334201
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González-Morales, A., Lachén‐Montes, M., Ausín, K., Cartas‐Cejudo, P., Mendizuri, N., Fernández‐Irigoyen, J., & Santamaría, E. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-817990-1.00011-1
Samluk, Ł., Ostapczuk, P., Malicka, D., & Dziembowska, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.21.496965
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Golubiani, G. (2023) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-10054
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Vogt, J. F., Merkwirth, C., Adams‐Quack, P., Zurkowski, E., Stylianakis, E., Uhlfelder, D. C., Michna, T., Nurbekova, A., Distler, U., Rojas-Charry, L., et al. (2026) · Communications Biology · doi:10.1038/s42003-026-10522-3
Self-citationKong, B., Han, C. Y., Kim, S. I., Patten, D. A., Han, Y., Carmona, E., Shieh, D.-B., Cheung, A. C., Mes‐Masson, A., Harper, M.-E., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20013025
Kong, B., Han, C. Y., Kim, S. I., Patten, D. A., Han, Y., Carmona, E., Shieh, D.-B., Cheung, A. C., Mes‐Masson, A., Harper, M.-E., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20013022
Xu, L., Xiang, W., Yang, J., Gao, J., Wang, X., Meng, L., Ye, K., Zhao, X. H., Zhang, X. D., Jin, L., et al. (2024) · Figshare · doi:10.6084/m9.figshare.24979491
Chang, C.-P., Chang, Y.-G., Chuang, P.-Y., Nguyen, T. N. A., Wu, K.-C., Chou, F.-Y., Cheng, S.-J., Chen, H.-M., Jin, L.-W., Carvalho, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14826218
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Olkhova, E. A., Dimitriou, A., Johnson, B. M., Hanaford, A., & Johnson, S. C. (2026) · Brain Mechanisms · doi:10.1016/j.bramec.2026.202535
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Zhou, S., Li, Y., Yang, F., Yang, J., Liu, Y., Wang, Y., Bai, D., Gao, Y., Jiao, Z., Tang, H., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-8380581/v1
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Filipović, D. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27083386
Rivera, G. O., & Theiss, A. L. (2026) · Microbial Cell · doi:10.15698/mic2026.06.878
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Metadata
- Authors
- Merkwirth, C., Martinelli, P., Korwitz, A., Morbin, M., Brönneke, H. S., Jordan, S. D., Rugarli, E. I., & Langer, T.
- Affiliations
- University of Cologne (DE)
- Fondazione IRCCS Istituto Neurologico Carlo Besta (IT)
- Corresponding author
- Langer, Thomas
- ORCID
- Venue
- PLoS Genetics
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-11-08
- Volume
- 8
- Issue
- 11
- Pages
- e1003021
- ISSN
- 1553-7390 (ISSN-L)
- 1553-7404
- PMC
- PMC3493444
- OpenAlex
- W2005255392
- Cited by
- 162
- References
- 59
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 8 · 2023: 13 · 2022: 20 · 2021: 16 · 2020: 18 · 2019: 15 · 2018: 11 · 2017: 12 · 2016: 12 · 2015: 9 · 2014: 9 · 2013: 8
- FWCI
- 3.34
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS Genetics (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Kölner Universitäts PublikationsServer (Universität zu Köln) (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- Deutsche Forschungsgemeinschaft (SFB635, C4, 233078, SFB 635)
- FP7 Ideas: European Research Council (233078)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- prohibitin, PHB2, prohibitin 1, OPA1, mitochondrial fusion, mitochondrial fission, mitochondrial dynamics, tau hyperphosphorylation, neurodegeneration, hippocampal neurons, mitochondrial ultrastructure, mitochondrial genome stability, respiratory deficiency, neuronal aging, cognitive impairment, autosomal dominant optic atrophy
- MeSH terms
- Prohibitins, Animals, Membrane Fusion, Mitochondria, Morphogenesis, Neurons, Phosphorylation, Repressor Proteins, tau Proteins, Apoptosis, Neurodegenerative Diseases, Optic Atrophy, Autosomal Dominant, Caenorhabditis elegans Proteins, Mitochondrial Membranes, Mice, Genome, Mitochondrial
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