The Novel Tail-anchored Membrane Protein Mff Controls Mitochondrial and Peroxisomal Fission in Mammalian Cells
Open accessAbstract
Few components of the mitochondrial fission machinery are known, even though mitochondrial fission is a complex process of vital importance for cell growth and survival. Here, we describe a novel protein that controls mitochondrial fission. This protein was identified in a small interfering RNA (siRNA) screen using Drosophila cells. The human homologue of this protein was named Mitochondrial fission factor (Mff). Mitochondria of cells transfected with Mff siRNA form a closed network similar to the mitochondrial networks formed when cells are transfected with siRNA for two established fission proteins, Drp1 and Fis1. Like Drp1 and Fis1 siRNA, Mff siRNA also inhibits fission induced by loss of mitochondrial membrane potential, it delays cytochrome c release from mitochondria and further progression of apoptosis, and it inhibits peroxisomal fission. Mff and Fis1 are both tail anchored in the mitochondrial outer membrane, but other parts of these proteins are very different and they exist in separate 200-kDa complexes, suggesting that they play different roles in the fission process. We conclude that Mff is a novel component of a conserved membrane fission pathway used for constitutive and induced fission of mitochondria and peroxisomes.
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Silencing MFF generates elongated mitochondria and DRP1 cytosolic distribution.
“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 [93]
MFF, MIEF2/MiD49, and MIEF1/MiD51 bind to DRP1 and arrange assembly of DRP1 oligomers at constriction sites.
“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 [93]
MFF overexpression results in increased mitochondrial fission.
“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 [93]
DLP-1 has a shared function in peroxisomal and mitochondrial fission and is recruited to peroxisomes by MFF and FIS1 following PEX11β-mediated elongation.
“DLP-1 has a shared function in peroxisomal and mitochondrial fission, and is recruited to peroxisomes by two mitochondrial-associated fission factors, mitochondrial fission factor (MFF) (Gandre-Babbe and van der Bliek, 2008), and mitochondrial fission 1 (FIS1), following PEX11β-mediated elongation (Koch et al., 2005; Itoyama et al., 2013).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Gandre-Babbe and van der Bliek, 2008
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References 67 · Cited by 769
- Authors
- Gandre-Babbe, S., & van der Bliek, A. M.
- Affiliations
- University of California, Los Angeles (US)
- Department of Biological Chemistry, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095
- Venue
- Molecular Biology of the Cell
- Published
- 2008-06
- Volume
- 19
- Issue
- 6
- Pages
- 2402-2412
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC2397315
- OpenAlex
- W2098181117
- Cited by
- 769
- References
- 67
- Citations by year
- 2026: 16 · 2025: 32 · 2024: 39 · 2023: 38 · 2022: 45 · 2021: 61 · 2020: 53 · 2019: 39 · 2018: 58 · 2017: 56 · 2016: 57 · 2015: 44 · 2014: 47 · 2013: 37 · 2012: 53
- FWCI
- 12.63
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular Biology of the Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM051866, GM-051866)
- 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
- Mff, mitochondrial fission, tail-anchored membrane proteins, mitochondrial outer membrane, Drp1, Fis1, mitochondrial membrane potential, cytochrome c release, apoptosis, siRNA screen, mitochondrial network
- MeSH terms
- Amino Acid Sequence, Animals, Carbonyl Cyanide m-Chlorophenyl Hydrazone, Drosophila, Genes, Dominant, HeLa Cells, Humans, Membrane Proteins, Mitochondria, Molecular Sequence Data, Mutation, Apoptosis, Sequence Homology, Amino Acid, GTP Phosphohydrolases, Peroxisomes, Protein Transport, Mitochondrial Proteins, Membrane Transport Proteins, Mitochondrial Membrane Transport Proteins, RNA Interference, RNA, Small Interfering, Multiprotein Complexes, Membrane Potential, Mitochondrial, Organelle Shape
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