The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
Open accessAbstract
The cytoplasmic dynamin-related guanosine triphosphatase Drp1 is recruited to mitochondria and mediates mitochondrial fission. Although the mitochondrial outer membrane (MOM) protein Fis1 is thought to be a Drp1 receptor, this has not been confirmed. To analyze the mechanism of Drp1 recruitment, we manipulated the expression of mitochondrial fission and fusion proteins and demonstrated that (a) mitochondrial fission factor (Mff) knockdown released the Drp1 foci from the MOM accompanied by network extension, whereas Mff overexpression stimulated mitochondrial recruitment of Drp1 accompanied by mitochondrial fission; (b) Mff-dependent mitochondrial fission proceeded independent of Fis1; (c) a Mff mutant with the plasma membrane–targeted CAAX motif directed Drp1 to the target membrane; (d) Mff and Drp1 physically interacted in vitro and in vivo; (e) exogenous stimuli–induced mitochondrial fission and apoptosis were compromised by knockdown of Drp1 and Mff but not Fis1; and (f) conditional knockout of Fis1 in colon carcinoma cells revealed that it is dispensable for mitochondrial fission. Thus, Mff functions as an essential factor in mitochondrial recruitment of Drp1.
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“MFF overexpression results in increased mitochondrial fission [90, 93].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [90]
In the citing paper
“In mammals, there are no orthologues for MDV1 and Cav 4, and recent evidence suggests that Fis1 is not required for fission [89, 90].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [90]
In the citing paper
“Instead, it has been reported that other components of the mammalian fission bind to DRP1 and arrange the assembly of DRP1 oligomers at constriction sites: mitochondrial fission factor (MFF), mitochondrial elongation factor 2/mitochondrial dynamics protein 49 (MIEF2/MiD49), and MIEF1/MiD51 [90–93].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [90]
In the citing paper
“On the contrary, silencing MFF generates elongated mitochondria and DRP1 cytosolic distribution [90, 93].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [90]
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Cites
Mitochondria: More Than Just a Powerhouse
McBride, H. M., Neuspiel, M., & Wasiak, S. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.054 · Cited by 1,985
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
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OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion
Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673
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Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270
Self-citationOlichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., & Lenaers, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200677200 · Cited by 1,168
A Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis
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Self-citationRoles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
Lee, Y.-J., Jeong, S.-Y., Karbowski, M., Smith, C. L., & Youle, R. J. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-04-0294 · Cited by 1,042
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Metadata
- Authors
- Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K.
- Affiliations
- Kyushu University (JP)
- National Institutes of Health (US)
- Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892 2
- Nagasaki International University (JP)
- Corresponding author
- Mihara, Katsuyoshi
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2010-12-13
- Volume
- 191
- Issue
- 6
- Pages
- 1141-1158
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC3002033
- OpenAlex
- W2149108521
- Cited by
- 1,110
- References
- 62
- Citations by year
- 2026: 42 · 2025: 67 · 2024: 74 · 2023: 72 · 2022: 88 · 2021: 91 · 2020: 80 · 2019: 69 · 2018: 70 · 2017: 70 · 2016: 77 · 2015: 71 · 2014: 78 · 2013: 60 · 2012: 67
- FWCI
- 20.43
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- 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 › Cell death mechanisms and regulation
- Keywords
- Mff, Drp1, mitochondrial fission, mitochondrial recruitment, Fis1, mitochondrial outer membrane, dynamin-related GTPase, mitochondrial fusion, CAAX motif, apoptosis, colon cancer cells, conditional knockout
- MeSH terms
- Animals, Cells, Cultured, Cytoplasm, Cytoskeletal Proteins, HeLa Cells, Humans, Membrane Proteins, Mitochondria, Down-Regulation, GTP Phosphohydrolases, Mitochondrial Proteins, RNA, Small Interfering
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