Dynamic recruitment of dynamin for final mitochondrial severance in a primitive red alga
Open accessAbstract
Dynamins are a eukaryote-specific family of GTPases. Some family members are involved in diverse and varied cellular activities. Here, we report that the primitive red alga Cyanidioschyzon merolae retains only one dynamin homolog, CmDnm1, belonging to the mitochondrial division subfamily. Previously, the bacterial cell division protein, FtsZ, was shown to localize at the mitochondrial division site in the alga. We showed that FtsZ and dynamin coexist as mitochondrial division-associated proteins that act during different phases of division. CmDnm1 was recruited from 10–20 cytoplasmic patches (dynamin patches) to the midpoint of the constricted mitochondrion-dividing ring (MD ring), which was observed as an electron-dense structure on the cytoplasmic side. CmDnm1 is probably not required for early constriction; it forms a ring or spiral when the outer mitochondrial membrane is finally severed, whereas the FtsZ and MD rings are formed before constriction. It is thought that the FtsZ, MD, and dynamin rings are involved in scaffolding, constriction, and final separation, respectively. In eukaryotes, mitochondrial severance is probably the most conserved role for the dynamin family.
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In prokaryotic cells and certain primitive eukaryotic species, FtsZ is a self-assembly GTPase that forms a calcium-mediated constricting ring on the IMM matrix side, suggesting that specific mechanisms for IMM constriction must exist.
“In prokaryotic cells and certain primitive eukaryotic species, FtsZ is a self-assembly GTPase that forms a calcium-mediated constricting ring on IMM's matrix side, suggesting that specific mechanisms for IMM constriction must exist [98].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [98]
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- Authors
- Nishida, K., Takahara, M., Miyagishima, S.-Y., Kuroiwa, H., Matsuzaki, M., & Kuroiwa, T.
- Affiliations
- Ministry of Agriculture, Forestry and Fisheries (JP)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2003-02-03
- Volume
- 100
- Issue
- 4
- Pages
- 2146-2151
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC149973
- OpenAlex
- W1982745631
- Cited by
- 154
- References
- 30
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 1 · 2023: 3 · 2022: 1 · 2021: 6 · 2020: 7 · 2019: 5 · 2018: 5 · 2017: 21 · 2016: 2 · 2015: 3 · 2014: 3 · 2013: 3 · 2012: 3
- FWCI
- 5.75
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- 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
- dynamin, mitochondrial division, FtsZ, mitochondrial outer membrane, Cyanidioschyzon merolae, red algae, GTPase, protein recruitment
- MeSH terms
- Rhodophyta, Microscopy, Electron, Microscopy, Fluorescence, Mitochondria, Molecular Sequence Data, Blotting, Western, Dynamins
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