Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice
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Mitochondria are dynamic subcellular organelles that convert nutrient intermediates into readily available energy equivalents. Optimal mitochondrial function is ensured by a highly evolved quality control system, coordinated by protein machinery that regulates a process of continual fusion and fission. In this work, we provide in vivo evidence that the ATP-independent metalloprotease OMA1 plays an essential role in the proteolytic inactivation of the dynamin-related GTPase OPA1 (optic atrophy 1). We also show that OMA1 deficiency causes a profound perturbation of the mitochondrial fusion-fission equilibrium that has important implications for metabolic homeostasis. Thus, ablation of OMA1 in mice results in marked transcriptional changes in genes of lipid and glucose metabolic pathways and substantial alterations in circulating blood parameters. Additionally, Oma1-mutant mice exhibit an increase in body weight due to increased adipose mass, hepatic steatosis, decreased energy expenditure and impaired thermogenenesis. These alterations are especially significant under metabolic stress conditions, indicating that an intact OMA1-OPA1 system is essential for developing the appropriate adaptive response to different metabolic stressors such as a high-fat diet or cold-shock. This study provides the first description of an unexpected role in energy metabolism for the metalloprotease OMA1 and reinforces the importance of mitochondrial quality control for normal metabolic function.
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Germline deletion of OMA1 does not impair embryogenesis, indicating that OMA1-induced OPA1 processing is dispensable for embryonic and adult mouse development.
“In contrast to Yme1L1, the germline deletion of OMA1 does not impair embryogenesis, which indicates that OMA1-induced OPA1 processing is dispensable for embryonic and adult mouse development [166, 167].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [167]
OMA1 deficiency causes lack of processing of OPA1L, resulting in a shift of mitochondrial dynamics towards fusion.
“OMA1 deficiency causes the lack of processing of OPA1L, which results in the shift of mitochondrial dynamics towards fusion.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [167]
OMA1-deficient mice display a diet-induced obesity phenotype, increased hepatic steatosis, altered glucose metabolism, and defective thermogenesis, suggesting a role for OMA1 in energy metabolism.
“OMA1-deficient mice display a diet-induced obesity phenotype, with increased hepatic steatosis and alteration of glucose metabolism, in addition to defective thermogenesis, suggesting a role for OMA1 in energy metabolism [167].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [167]
Dysregulation of mitochondrial dynamics with a shift towards fission promotes metabolic dysfunction, as shown by the onset of obesity and insulin resistance following ablation of fusion protein in mice.
“In support of this paradigm, dysregulation of mitochondria dynamic with a shift towards fission promotes metabolic dysfunction as demonstrated by the onset of obesity and insulin resistance following the ablation of fusion protein in mice (Quiros et al., 2012; Sebastian et al., 2012).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Quiros et al., 2012
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Loss of OMA1 delays neurodegeneration by preventing stress-induced OPA1 processing in mitochondria
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Mitochondrial Morphofunction in Mammalian Cells
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Self-citationThe dynamin GTPase OPA1: More than mitochondria?
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Loss of mitochondrial protease ClpP protects mice from diet‐induced obesity and insulin resistance
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Proteolytic control of mitochondrial function and morphogenesis
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Self-citationReturning to the Fold for Lessons in Mitochondrial Crista Diversity and Evolution
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YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stress
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Mitofusin 2 as a Driver That Controls Energy Metabolism and Insulin Signaling
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Self-citationSirtuin 5 protects mitochondria from fragmentation and degradation during starvation
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Regulation of Mother-to-Offspring Transmission of mtDNA Heteroplasmy
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OPA1 deletion in brown adipose tissue improves thermoregulation and systemic metabolism via FGF21
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Self-citationPISD is a mitochondrial disease gene causing skeletal dysplasia, cataracts, and white matter changes
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Melatonin, mitochondria and hypertension
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Prohibitin levels regulate OMA1 activity and turnover in neurons
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Dual regulation of mitochondrial fusion by Parkin–PINK1 and OMA1
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Self-citationGenome-wide identification of loci associated with growth in rainbow trout
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The short variant of optic atrophy 1 (OPA1) improves cell survival under oxidative stress
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Loss of the mitochondrial i‐AAA protease YME1L leads to ocular dysfunction and spinal axonopathy
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Changing appetites: the adaptive advantages of fuel choice
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- Authors
- Quirós, P. M., Ramsay, A. J., Sala, D., Fernández‐Vizarra, E., Rodríguez, F., Peinado, J. R., Fernández‐García, M. S., Vega, J. A., Enríquez, J. A., Zorzano, A., & López‐Otín, C.
- Affiliations
- Universidad de Oviedo (ES)
- Instituto de Salud Carlos III (ES)
- Universidad de Zaragoza (ES)
- Venue
- The EMBO Journal
- Published
- 2012-03-20
- Volume
- 31
- Issue
- 9
- Pages
- 2117-2133
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3343468
- OpenAlex
- W2119434925
- Cited by
- 269
- References
- 56
- Citations by year
- 2026: 14 · 2025: 11 · 2024: 16 · 2023: 18 · 2022: 20 · 2021: 17 · 2020: 26 · 2019: 25 · 2018: 28 · 2017: 15 · 2016: 18 · 2015: 16 · 2014: 20 · 2013: 17 · 2012: 8
- FWCI
- 7.85
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Zaguan (University of Zaragoza Repository) (publishedVersion)
- Consultation of the Doctoral Thesis Database (TESEO) (Ministerio de Educación, Cultura y Deporte) (submittedVersion, cc-by-nc-nd)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (submittedVersion, cc-by-nc-nd)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- European Commission
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- OMA1, OPA1, mitochondrial fission, mitochondrial fusion, mitochondrial quality control, metalloproteinases, thermogenesis, obesity, energy expenditure, hepatic steatosis, lipid metabolism, glucose metabolism, metabolic stress, cold exposure, high-fat diet, mitochondrial dynamics
- MeSH terms
- Animals, Blood Glucose, Embryo, Mammalian, Fibroblasts, Metalloendopeptidases, Mice, Inbred C57BL, Mitochondria, Obesity, Mice, Knockout, GTP Phosphohydrolases, Thermogenesis, Mitochondrial Proteins, Metalloproteases, Lipid Metabolism, Mice, Adipocytes, Brown, Diet, High-Fat
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