SIRT3 Deacetylates and Activates OPA1 To Regulate Mitochondrial Dynamics during Stress
Open accessAbstract
Mitochondrial morphology is regulated by the balance between two counteracting mitochondrial processes of fusion and fission. There is significant evidence suggesting a stringent association between morphology and bioenergetics of mitochondria. Morphological alterations in mitochondria are linked to several pathological disorders, including cardiovascular diseases. The consequences of stress-induced acetylation of mitochondrial proteins on the organelle morphology remain largely unexplored. Here we report that OPA1, a mitochondrial fusion protein, was hyperacetylated in hearts under pathological stress and this posttranslational modification reduced the GTPase activity of the protein. The mitochondrial deacetylase SIRT3 was capable of deacetylating OPA1 and elevating its GTPase activity. Mass spectrometry and mutagenesis analyses indicated that in SIRT3-deficient cells OPA1 was acetylated at lysine 926 and 931 residues. Overexpression of a deacetylation-mimetic version of OPA1 recovered the mitochondrial functions of OPA1-null cells, thus demonstrating the functional significance of K926/931 acetylation in regulating OPA1 activity. Moreover, SIRT3-dependent activation of OPA1 contributed to the preservation of mitochondrial networking and protection of cardiomyocytes from doxorubicin-mediated cell death. In summary, these data indicated that SIRT3 promotes mitochondrial function not only by regulating activity of metabolic enzymes, as previously reported, but also by regulating mitochondrial dynamics by targeting OPA1.
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Under stress conditions, hyperacetylation of OPA1 reduces its GTPase activity, while SIRT3-dependent deacetylation increases OPA1 GTPase activity.
“Under stress conditions, hyperacetylation of OPA1 reduces its GTPase activity while SIRT3-dependent deacetylation increases OPA1 GTPase activity [79].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [79]
SIRT3 deacetylates OPA1, elevating its GTPase activity and increasing fusion processes.
“SIRT3 also emerges as an important factor in the control of mitochondrial dynamics during ageing since it deacetylates OPA1 elevating its GTPase activity and then, increasing fusion processes (Samant et al., 2014).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Samant et al., 2014
SIRT3 deacetylates and elevates the GTPase activity of the inner membrane fusion protein OPA1, thereby favoring mitochondrial elongation.
“Interestingly, SIRT3 also deacetylates and elevates the GTPase activity of the inner membrane fusion protein OPA1, thereby favoring mitochondrial elongation (Samant et al, 2014).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Samant et al, 2014
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- Authors
- Samant, S. A., Zhang, H. J., Hong, Z., Pillai, V. B., Sundaresan, N. R., Wolfgeher, D., Archer, S. L., Chan, D. C., & Gupta, M. P.
- Affiliations
- University of Chicago (US)
- Queen's University (CA)
- California Institute of Technology (US)
- ORCID
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2014-03-01
- Volume
- 34
- Issue
- 5
- Pages
- 807-819
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC4023816
- OpenAlex
- W2163051782
- Cited by
- 446
- References
- 79
- Citations by year
- 2026: 22 · 2025: 34 · 2024: 43 · 2023: 45 · 2022: 50 · 2021: 58 · 2020: 33 · 2019: 24 · 2018: 33 · 2017: 33 · 2016: 37 · 2015: 18 · 2014: 13
- FWCI
- 10.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health
- National Heart, Lung, and Blood Institute (R01HL111455, R01 HL83423, R01HL071115, R01HL117041, R01HL113003, R01HL083423)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- SIRT3, OPA1, protein acetylation, mitochondrial fusion, mitochondrial dynamics, mitochondrial fission, GTPase activity, lysine acetylation, cardiomyocytes, mitochondrial morphology, post-translational modification
- MeSH terms
- Acetylation, Animals, Cells, Cultured, Fibroblasts, Heart, HeLa Cells, Humans, Mice, Transgenic, Mitochondria, Protein Processing, Post-Translational, Cell Death, GTP Phosphohydrolases, Mitochondrial Proteins, Myocytes, Cardiac, Cell Line, Tumor, Mice, Sirtuin 3, Mitochondrial Dynamics
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