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OPA1 requires mitofusin 1 to promote mitochondrial fusion
Open accessAbstract
The regulated equilibrium between mitochondrial fusion and fission is essential to maintain integrity of the organelle. Mechanisms of mitochondrial fusion are largely uncharacterized in mammalian cells. It is unclear whether OPA1, a dynamin-related protein of the inner membrane mutated in autosomal dominant optic atrophy, participates in fusion or fission. OPA1 promoted the formation of a branched network of elongated mitochondria, requiring the integrity of both its GTPase and C-terminal coiled-coil domain. Stable reduction of OPA1 levels by RNA interference resulted in small, fragmented, and scattered mitochondria. Levels of OPA1 did not affect mitochondrial docking, but they correlated with the extent of fusion as measured by polyethylene glycol mitochondrial fusion assays. A genetic analysis proved that OPA1 was unable to tubulate and fuse mitochondria lacking the outer membrane mitofusin 1 but not mitofusin 2. Our data show that OPA1 functionally requires mitofusin 1 to regulate mitochondrial fusion and reveal a specific functional difference between mitofusin 1 and 2.
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In the citing paper
“OPA1-dependent mitochondrial fusion needs Mfn1 [73] as well as balanced OPA1S and OPA1L forms.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [73]
In the citing paper
“OPA1 deletion leads to mitochondrial fragmentation, whereas OPA1 overexpression induces mitochondrial elongation [73].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [73]
In the citing paper
“Opa1 participates in inner mitochondrial membrane fusion and cristae morphogenesis.”
From Mitochondrial DNA and TLR9 drive muscle inflammation upon Opa1 deficiency (2018) · cites this paper as Cipolat et al, 2004
In the citing paper
“which consists in the fusion of the outer and inner mitochondrial membranes orchestrated by mitofusin-1 and mitofusin-2 and optic atrophy protein 1, respectively (Figure 3; Cipolat et al., 2004).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Cipolat et al., 2004
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Metadata
- Authors
- Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L.
- Affiliations
- Veneto Institute of Molecular Medicine (IT)
- Dulbecco–Telethon Institute, Venetian Institute of Molecular Medicine, Via Orus 2, I-35129 Padua, Italy
- ORCID
- Scorrano, Luca
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2004-10-27
- Volume
- 101
- Issue
- 45
- Pages
- 15927-15932
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC528769
- OpenAlex
- W1989540421
- Cited by
- 1,300
- References
- 45
- Citations by year
- 2026: 46 · 2025: 76 · 2024: 64 · 2023: 74 · 2022: 75 · 2021: 88 · 2020: 90 · 2019: 82 · 2018: 73 · 2017: 59 · 2016: 66 · 2015: 50 · 2014: 58 · 2013: 53 · 2012: 63
- FWCI
- 10.44
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- 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 › ATP Synthase and ATPases Research
- Keywords
- OPA1, mitofusin 1, mitofusin 2, mitochondrial fusion, mitochondrial fission, dynamin-related proteins, GTPase, coiled-coil domain, mitochondrial outer membrane, mitochondrial tubulation, autosomal dominant optic atrophy, mitochondrial morphology
- MeSH terms
- Animals, Cells, Cultured, Membrane Fusion, Mitochondria, Mice, Knockout, Gene Targeting, GTP Phosphohydrolases, RNA Interference, Mice, In Vitro Techniques
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