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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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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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