The constriction and scission machineries involved in mitochondrial fission
Open accessAbstract
A key event in the evolution of eukaryotic cells was the engulfment of an aerobic bacterium by a larger anaerobic archaebacterium, leading to a close relationship between the host and the newly formed endosymbiont. Mitochondria, originating from this event, have evolved to be the main place of cellular ATP production. Maintaining elements of their independence, mitochondria undergo growth and division in the cell, thereby ensuring that new daughter cells inherit a mitochondrial complement. Mitochondrial division is also important for other processes, including quality control, mitochondrial (mt)DNA inheritance, transport and cell death. However, unlike bacterial fission, which uses a dynamin-related protein to constrict the membrane at its inner face, mitochondria use dynamin and dynamin-related proteins to constrict the outer membrane from the cytosolic face. In this Review, we summarize the role of proteins from the dynamin superfamily in mitochondrial division. This includes recent findings highlighting that dynamin-2 (Dnm2) is involved in mitochondrial scission, which led to the reappraisal of the role of dynamin-related protein 1 (Drp1; also known as Dnm1l) and its outer membrane adaptors as components of the mitochondrial constriction machinery along with ER components and actin.
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DRP1 is recruited to marked division sites to bind to its OMM receptors/adaptors, facilitating DRP1 oligomerization into a ring-like structure that narrows the membranes.
“Subsequently, DRP1 is recruited to the marked division sites to bind to its OMM receptors/adaptors. This binding facilitates DRP1 oligomerization, forming a ring-like structure that favors an additional narrowing of the membranes [83].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [83]
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Ghasemizadeh, A., Christin, E., Guiraud, A., Couturier, N., Abitbol, M., Risson, V., Girard, E., Jagla, C., Soler, C., Laddada, L., et al. (2021) · eLife · doi:10.7554/elife.70490 · Cited by 33 · see citing works
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- Authors
- Kraus, F., & Ryan, M. T.
- Affiliations
- Monash University (AU)
- Corresponding author
- Kraus, Felix
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2017-09-15
- Volume
- 130
- Issue
- 18
- Pages
- 2953-2960
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2747200758
- Cited by
- 244
- References
- 95
- Citations by year
- 2026: 13 · 2025: 14 · 2024: 25 · 2023: 26 · 2022: 32 · 2021: 40 · 2020: 41 · 2019: 33 · 2018: 19 · 2017: 1
- FWCI
- 2.41
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Cell Science (publishedVersion)
- Monash University Research Portal (Monash University) (publishedVersion, other-oa)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- Australian Research Council (DP160102176)
- National Health and Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- mitochondrial fission, mitochondrial division, dynamin superfamily, dynamin 2, Drp1, mitochondrial outer membrane, mitochondrial inheritance, endosymbiotic origin of mitochondria, actin, endoplasmic reticulum, mitochondrial quality control
- MeSH terms
- Actins, Animals, Endoplasmic Reticulum, Humans, Lipids, Models, Biological, Mitochondrial Proteins, Mitochondrial Dynamics
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