An Actin-Dependent Step in Mitochondrial Fission Mediated by the ER-Associated Formin INF2
Open accessAbstract
Masterminding Mitochondrial Fission: Mitochondria are highly dynamic and undergo fusion and fission and they move in cells. Defects in mitochondrial dynamics are implicated in many neurodegenerative diseases. Recent findings have suggested that mitochondrial fission occurs preferentially at endoplasmic reticulum (ER) contact sites, with ER circumscribing mitochondria and possibly promoting the constriction of mitochondria during fission. Korobova et al. (p. 464 ) now suggest that an ER-localized formin, INF2, is required for mitochondrial fission and that INF2-mediated actin polymerization facilitates mitochondrial constriction.
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The ER protein inverted formin 2 (INF2) might facilitate initial mitochondrial constriction by inducing actin polymerization at ER-mitochondria contact sites.
“This process might be facilitated by the action of the ER protein inverted formin 2 (INF2), which induces actin polymerization at the ER–mitochondria contact sites, enabling force generation to drive initial mitochondrial constriction [82].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [82]
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References 26 · Cited by 817
Research works printed but not linked: 1
- [21]WoŸniak MJ J Cell Sci 122 1979 2009 19454478 PMC2723153
- Authors
- Korobova, F., Ramabhadran, V., & Higgs, H. N.
- Affiliations
- Dartmouth College (US)
- Tufts University (US)
- Corresponding author
- Higgs, Henry N.
- Venue
- Science
- Published
- 2013-01-25
- Volume
- 339
- Issue
- 6118
- Pages
- 464-467
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3843506
- OpenAlex
- W2054115583
- Cited by
- 817
- References
- 26
- Citations by year
- 2026: 44 · 2025: 61 · 2024: 74 · 2023: 62 · 2022: 64 · 2021: 80 · 2020: 75 · 2019: 61 · 2018: 58 · 2017: 61 · 2016: 56 · 2015: 51 · 2014: 44 · 2013: 26
- FWCI
- 26.45
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (P30CA023108)
- National Institute of General Medical Sciences (GM069818, R01GM069818)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK088826, DK88826)
- 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, actin polymerization, INF2, Drp1, endoplasmic reticulum, F-actin, Charcot-Marie-Tooth disease, mitochondrial dynamics
- MeSH terms
- Formins, Actins, Animals, Endoplasmic Reticulum, Humans, Microfilament Proteins, Actin Cytoskeleton, Microtubule-Associated Proteins, Mitochondria, Recombinant Fusion Proteins, Bridged Bicyclo Compounds, Heterocyclic, GTP Phosphohydrolases, Mitochondrial Proteins, Dynamins, RNA, Small Interfering, NIH 3T3 Cells, Cell Line, Tumor, Mice, Thiazolidines, Protein Multimerization, Mitochondrial Dynamics
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