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Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Open accessAbstract
Changes in mitochondrial morphology that occur during cell cycle, differentiation, and death are tightly regulated by the balance between fusion and fission processes. Excessive fragmentation can be caused by inhibition of the fusion machinery and is a common consequence of dysfunction of the organelle. Here, we show a role for calcineurin-dependent translocation of the profission dynamin related protein 1 (Drp1) to mitochondria in dysfunction-induced fragmentation. When mitochondrial depolarization is associated with sustained cytosolic Ca 2+ rise, it activates the cytosolic phosphatase calcineurin that normally interacts with Drp1. Calcineurin-dependent dephosphorylation of Drp1, and in particular of its conserved serine 637, regulates its translocation to mitochondria as substantiated by site directed mutagenesis. Thus, fragmentation of depolarized mitochondria depends on a loop involving sustained Ca 2+ rise, activation of calcineurin, and dephosphorylation of Drp1 and its translocation to the organelle.
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“Interestingly, the downstream ROCK target calcineurin can dephosphorylate Drp1 and cause mitochondrial fission [135,136].”
From RhoA Signaling in Neurodegenerative Diseases (2022) · cites this paper as [135]
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“The activation of cAMP/PKA upon nutrient starvation leads to phosphorylation of Drp1, preventing its stable docking on the mitochondrial surface and therefore mitochondrial fission (Cereghetti et al, 2008) (Fig 2A).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Cereghetti et al, 2008
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Mitochondria: More Than Just a Powerhouse
McBride, H. M., Neuspiel, M., & Wasiak, S. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.054 · Cited by 1,985
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
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-citationMitochondrial Transport of Cations: Channels, Exchangers, and Permeability Transition
Bernardi, P. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1127 · Cited by 1,546
Self-citationBAX 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-citationMitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission.
Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., & Mihara, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607279200 · Cited by 1,226
Organelle isolation: functional mitochondria from mouse liver, muscle and cultured filroblasts
Frezza, C., Cipolat, S., & Scorrano, L. (2007) · Nature Protocols · doi:10.1038/nprot.2006.478 · Cited by 1,188
Self-citationCribbs, J. T., & Strack, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401062 · Cited by 1,061
Chang, C., & Blackstone, C. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700083200 · Cited by 824
Self-citationCipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K., Metzger, K., Frezza, C., Annaert, W. G., D'adamio, L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.021 · Cited by 756
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Rahman, A., Li, Y., Ismail, N. I., Chan, T.-K., Li, Y., Xu, D., Zhou, H., & Ong, S. (2022) · International Journal of Stem Cells · doi:10.15283/ijsc22141 · Cited by 3
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Lomash, R. M., Petralia, R. S., Holtzclaw, L. A., Tsuda, M. C., Wang, Y., Badger, J. D., Cameron, H. A., Youle, R. J., & Roche, K. W. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007245 · Cited by 3
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Wilkins, H. M., Weidling, I., Koppel, S., Wang, X., von Schulze, A., & Swerdlow, R. H. (2018) · The Molecular and Cellular Basis of Neurodegenerative Diseases · doi:10.1016/b978-0-12-811304-2.00013-4 · Cited by 2
Heard, T. C., Abaasah, I. E., Botts, E., Christy, B. A., Mdaki, M. K. S., Ross, E., Meledeo, M. A., & Herzig, M. C. S. (2025) · Cytotherapy · doi:10.1016/j.jcyt.2025.04.066 · Cited by 2
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Baik, H., & Cho, J. (2022) · Animal Bioscience · doi:10.5713/ab.22.0059 · Cited by 1
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Zhang, Q., Hu, C., Huang, J., Liu, W., Lai, W., Leng, F., Tang, Q., Liu, Y., Wang, Q., Zhou, M., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/366401 · Cited by 1
Barbosa, S. (2012) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) · Cited by 1
Zhuang, J., Chen, L., Li, G., Xia, L., Wu, S., Leng, J., Tao, X., Jiang, H., Wu, Y. P., Wang, S., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1826347/v1 · Cited by 1
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Aung, K., Kaur, N., & Hu, J. (2014) · Springer eBooks · doi:10.1007/978-3-7091-1788-0_20
Campos, J. C. (2012) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.39.2012.tde-13082012-163112
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Liu, T. (2014) · Figshare
Does animal origin and hide status affect microbial contamination in pig carcasses?
Trevisani, M., Marzadori, F., Rosmini, R., & Rustichelli, R. (2003) · International Conference on the Epidemiology and Control of Biological, Chemical and Physical Hazards in Pigs and Pork · doi:10.31274/safepork-180809-493
Drp1 ablation in the adult mouse forebrain
Oettinghaus, B. (2014) · edoc (University of Basel) · doi:10.5451/unibas-006288258
Drp1 ablation in the adult mouse forebrain
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Mihara, K., & Otera, H. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.20024-2
Iworima, D. G. (2013) · Summit (Simon Fraser University)
Metadata
- Authors
- Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L.
- Affiliations
- Veneto Institute of Molecular Medicine (IT)
- *Dulbecco-Telethon Institute;
- National Institutes of Health (US)
- University of Padua (IT)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2008-10-14
- Volume
- 105
- Issue
- 41
- Pages
- 15803-15808
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2572940
- OpenAlex
- W2023283007
- Cited by
- 1,129
- References
- 35
- Citations by year
- 2026: 40 · 2025: 51 · 2024: 54 · 2023: 79 · 2022: 67 · 2021: 79 · 2020: 92 · 2019: 60 · 2018: 86 · 2017: 78 · 2016: 80 · 2015: 59 · 2014: 68 · 2013: 58 · 2012: 54
- FWCI
- 16.44
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (acceptedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Padua Research Archive (University of Padova) (submittedVersion, other-oa)
- 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 › Cell death mechanisms and regulation
- Keywords
- calcineurin, Drp1, mitochondrial fission, mitochondrial depolarization, mitochondrial fragmentation, intracellular calcium, mitochondrial morphology, mitochondrial fusion
- MeSH terms
- Calcium, HeLa Cells, Humans, Microtubule-Associated Proteins, Mitochondria, Phosphorylation, Serine, Mutagenesis, Site-Directed, Calcineurin, GTP Phosphohydrolases, Protein Transport, Mitochondrial Proteins, Dynamins, Membrane Potential, Mitochondrial
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