C. elegans Dynamin-Related Protein DRP-1 Controls Severing of the Mitochondrial Outer Membrane
Open accessAbstract
Little is known about the mechanism of mitochondrial division. We show here that mitochondria are disrupted by mutations in a C. elegans dynamin-related protein (DRP-1). Mutant DRP-1 causes the mitochondrial matrix to retract into large blebs that are both surrounded and connected by tubules of outer membrane. This indicates that scission of the mitochondrial outer membrane is inhibited, while scission of the inner membrane still occurs. Overexpressed wild-type DRP-1 causes mitochondria to become excessively fragmented, consistent with an active role in mitochondrial scission. DRP-1 fused to GFP is observed in spots on mitochondria where scission eventually occurs. These data indicate that wild-type DRP-1 contributes to the final stages of mitochondrial division by controlling scission of the mitochondrial outer membrane.
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In the absence of DRP1 or OMM constriction, IMM division still occurs, indicating the presence of an inner membrane fission machinery independent of DRP1.
“In the absence of DRP1 or OMM constriction, the IMM division still occurs, indicating the presence of an inner membrane fission machinery independent of DRP1 [100, 101].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [100]
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- Authors
- Labrousse, A. M., Zappaterra, M. D., Rube, D. A., & van der Bliek, A. M.
- Affiliations
- University of California, Los Angeles (US)
- ORCID
- Labrousse, Arnaud M.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 1999-11
- Volume
- 4
- Issue
- 5
- Pages
- 815-826
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2126624770
- Cited by
- 670
- References
- 48
- Citations by year
- 2026: 9 · 2025: 21 · 2024: 33 · 2023: 19 · 2022: 20 · 2021: 27 · 2020: 28 · 2019: 24 · 2018: 30 · 2017: 34 · 2016: 19 · 2015: 27 · 2014: 34 · 2013: 25 · 2012: 32
- FWCI
- 5.74
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM051866, GM 51866)
- 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
- Drp1, dynamin-related proteins, mitochondrial division, mitochondrial fission, mitochondrial fragmentation, Caenorhabditis elegans, mitochondrial matrix
- MeSH terms
- Animals, Cell Division, Female, Genes, Lethal, Humans, Intracellular Membranes, Membrane Proteins, Mitochondria, Molecular Sequence Data, Muscles, Mutation, Neuropeptides, Oogenesis, Recombinant Fusion Proteins, RNA, Messenger, Tetradecanoylphorbol Acetate, Gene Expression, Consensus Sequence, Caenorhabditis elegans, Sequence Homology, Amino Acid, Cell Lineage, Gene Expression Profiling, Drosophila Proteins, Caenorhabditis elegans Proteins, Vesicular Transport Proteins, Dynamins
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