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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]
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“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]
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“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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Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy
Yamano, K., Fogel, A. I., Wang, C., van der Bliek, A. M., & Youle, R. J. (2014) · eLife · doi:10.7554/elife.01612 · Cited by 307
“In agreement with previous work (Otera et al., 2010), mitochondrial morphology, as well as peroxisomal morphology in FIS1−/− cells, was similar to that of WT cells (Figure 1B).”
BackgroundResultInfluentialSelf-citationCerS6-Derived Sphingolipids Interact with Mff and Promote Mitochondrial Fragmentation in Obesity
Hammerschmidt, P., Ostkotte, D., Nolte, H., Gerl, M. J., Jaïs, A., Brunner, H. L., Sprenger, H., Awazawa, M., Nicholls, H. T., Turpin-Nolan, S. M., et al. (2019) · Cell · doi:10.1016/j.cell.2019.05.008 · Cited by 314
Palmer, C. S., Elgass, K. D., Parton, R. G., Osellame, L. D., Stojanovski, D., & Ryan, M. T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.479873 · Cited by 301
“The authors found some increase in mitochondrial elongation in contrast to a Fis1 knock-out human cell line (22, 23).”
BackgroundResultMitochondrial dynamics in health and disease
Yapa, N. M. B., Lisnyak, V., Reljić, B., & Ryan, M. T. (2021) · FEBS Letters · doi:10.1002/1873-3468.14077 · Cited by 323
Regulation of Mitochondrial ATP Production: Ca2+ Signaling and Quality Control
Boyman, L., Karbowski, M., & Lederer, W. J. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.10.007 · Cited by 310
How mitochondrial dynamism orchestrates mitophagy
Shirihai, O. S., Song, M., & Dorn, G. W. (2015) · Circulation Research · doi:10.1161/circresaha.116.306374 · Cited by 311
“However, mitochondrial fission factor (Mff) colocalizes with Drp1 on mammalian mitochondria, and RNAi-mediated Mff knockdown both reduces Drp1 association and induces mitochondrial elongation; Mff overexpression promotes mitochondrial fragmentation.(29) Other proteins that may help recruit Drp1 to OMM are mitochondria…”
Zhou, H., Hu, S., Jin, Q., Chen, S., Zhang, Y., Zhu, P., Ma, Q., Tian, F., & Chen, Y. (2017) · Journal of the American Heart Association · doi:10.1161/jaha.116.005328 · Cited by 306
“These receptors tightly couple cytoplasmic Drp1 to the mitochondria.9 Otera et al10,11 provided experimental evidence that Mff and not mitochondrial fission 1 preferentially captures Drp1, suggesting that Mff is required for successive fission.”
BackgroundThe role of mitochondrial fission in cardiovascular health and disease
Quiles, J. M., & Gustafsson, Å. B. (2022) · Nature Reviews Cardiology · doi:10.1038/s41569-022-00703-y · Cited by 315
Hu, C., Huang, Y., & Li, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010144 · Cited by 302
“Mff knockdown has been shown to induce mitochondrial elongation in mammalian cells, whereas overexpression of Mff recruits Drp1 for mitochondrial fragmentation [17].”
BackgroundKim, S., Syed, G. H., Khan, M. A., Chiu, W.-W., Sohail, M. A., Gish, R. G., & Siddiqui, A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321114111 · Cited by 293
Mitochondria–Lysosome Crosstalk: From Physiology to Neurodegeneration
Deus, C. M., Yambire, K. F., Oliveira, P. J., & Raimundo, N. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.10.009 · Cited by 299
Structural insights into oligomerization and mitochondrial remodelling of dynamin 1‐like protein
Fröhlich, C., Grabiger, S., Schwefel, D., Faelber, K., Rosenbaum, E., Mears, J. A., Rocks, O., & Daumke, O. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.74 · Cited by 292
“…the endoplasmic reticulum (Friedman et al , 2011) and is thought to be mediated via adaptor proteins, such as mitochondrial fission factor (Mff) (Otera et al , 2010), mitochondrial elongation factor 1/mitochondrial dynamics proteins of 49 and 51 kDa (MIEF1/MiD49/51) (Palmer et al , 2011; Zhao…”
Hall, A. R., Burke, N., Dongworth, R. K., & Hausenloy, D. J. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12516 · Cited by 294
“, 2011), while MFF is reported to be a key protein in the recruitment of other proteins (potentially more Drp or other, as yet unidentified proteins) (Gandre-Babbe and van der Bliek, 2008) or a bone fide Drp1 receptor (Otera et al., 2010).”
InfluentialMitochondrial Dynamics: Coupling Mitochondrial Fitness with Healthy Aging
Sebastián, D., Palacı́n, M., & Antonio Zorzano, A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.01.003 · Cited by 292
“However, there continues to be controversy regarding the exact role of FIS1 in mitochondrial division, probably due to differences in the cellular context [117].”
BackgroundDengue Virus Perturbs Mitochondrial Morphodynamics to Dampen Innate Immune Responses
Chatel‐Chaix, L., Cortese, M., Romero‐Brey, I., Bender, S., Neufeldt, C. J., Fischl, W., Scaturro, P., Schieber, N. L., Schwab, Y., Fischer, B., et al. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.07.008 · Cited by 290
“, DRP1 and mitochondrial fission factor [MFF]) (Smirnova et al., 2001; Smirnova et al., 1998; Otera et al., 2010; Chen et al., 2003; Olichon et al., 2003).”
The peroxisome: an update on mysteries
Islinger, M., Grille, S., Fahimi, H. D., & Schrader, M. (2012) · Histochemistry and Cell Biology · doi:10.1007/s00418-012-0941-4 · Cited by 283
“Instead, the novel tail-anchored receptor Mff, which contains a cytosolic coiled-coil domain, is supposed to be the major membrane receptor for DLP (Gandre-Babbe and van der Bliek 2008; Otera et al. 2010).”
BackgroundThe regulation of mitochondrial morphology: Intricate mechanisms and dynamic machinery
Palmer, C. S., Osellame, L. D., Stojanovski, D., & Ryan, M. T. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.05.021 · Cited by 300
Molecular mechanisms for mitochondrial adaptation to exercise training in skeletal muscle
Drake, J. C., Wilson, R. J., & Yan, Z. (2016) · The FASEB Journal · doi:10.1096/fj.15-276337 · Cited by 263
“More recent evidence suggests that FIS1 is dispensable for mitochondrial fission, and instead mitochondrial fission factor (MFF)-1, a novel tail-anchored membrane protein, is essential for the recruitment of DRP1 to the damaged mitochondria (79).”
BackgroundPrieto, J., León, M., Ponsoda, X., Sendra, R., Bort, R., Ferrer‐Lorente, R., Raya, Á., López‐García, C., & Torres, J. (2016) · Nature Communications · doi:10.1038/ncomms11124 · Cited by 286
Lewis, T. L., Kwon, S.-K., Lee, A., Shaw, R., & Polleux, F. (2018) · Nature Communications · doi:10.1038/s41467-018-07416-2 · Cited by 260
Mitochondria as a therapeutic target for ischemic stroke
He, Z., Ning, N., Zhou, Q., Khoshnam, S. E., & Farzaneh, M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.11.005 · Cited by 272
Saben, J. L., Boudoures, A. L., Shyr, Z. A., Thompson, A. S., Drury, A. M., Zhang, W., Chi, M. M.-Y., Cusumano, A., Scheaffer, S. M., & Moley, K. H. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.065 · Cited by 266
“Consistent with this idea, cells lacking both OPA1 and Drp1 have large mitochondria with disrupted cristae structures or onion-like inner membrane structures (Otera et al., 2010).”
TGR5 signalling promotes mitochondrial fission and beige remodelling of white adipose tissue
Velazquez-Villegas, L. A., Perino, A., Lemos, V., Zietak, M., Nomura, M., Pols, T. W. H., & Schoonjans, K. (2018) · Nature Communications · doi:10.1038/s41467-017-02068-0 · Cited by 268
Recent advances into the understanding of mitochondrial fission
Elgass, K., Pakay, J. L., Ryan, M. T., & Palmer, C. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.002 · Cited by 274
Pleiotropic Mitochondria: The Influence of Mitochondria on Neuronal Development and Disease
Rangaraju, V., Lewis, T. L., Hirabayashi, Y., Bergami, M., Motori, E., Cartoni, R., Kwon, S., & Courchet, J. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1157-19.2019 · Cited by 271
“In mammalian cells, mitochondrial fission occurs when the GTPase Drp1 is recruited from the cytosol to the outer mitochondrial membrane via one of the four known “receptors”: MFF, FIS1, MIEF1, and MIEF2 (Gandre-Babbe and van der Bliek, 2008; Otera et al., 2010; Losón et al., 2013; Osellame et al., 2016).”
BackgroundBaek, S. H., Park, S. J., Jeong, J. I., Kim, S. H., Han, J., Kyung, J. W., Baik, S.-H., Choi, Y., Choi, B. Y., Park, J. S., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.2385-16.2017 · Cited by 258
“…of mitochondrial fission, Drp1 is translocated from the cytosol to the mitochondrial outer membrane and interacts with its receptors, such as mitochondrial fission 1 (Fis1) and mitochondrial fission factor (MFF) to promote the mitochondrial fission process (Lee et al., 2004; Otera et al., 2010).”
BackgroundMitochondrial division ensures the survival of postmitotic neurons by suppressing oxidative damage
Kageyama, Y., Zhang, Z., Roda, R. H., Fukaya, M., Wakabayashi, J., Wakabayashi, N., Kensler, T. W., Reddy, P. H., Iijima, M., & Sesaki, H. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201110034 · Cited by 256
“Drp1 is recruited to the mitochondrial surface by other outer membrane proteins (James et al., 2003; Yoon et al., 2003; Gandre-Babbe and van der Bliek, 2008; Otera et al., 2010; Palmer et al., 2011), where it assembles into spiral structures around mitochondria to induce fission of the mitochondrial membrane (Yoon et…”
ACBD5 and VAPB mediate membrane associations between peroxisomes and the ER
Costello, J. L., Castro, I. G., Hacker, C., Schrader, T. A., Metz, J., Zeuschner, D., Azadi, A. S., Godinho, L. F., Costina, V., Findeisen, P., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201607055 · Cited by 251
“DRP1 is recruited to POs by the membrane adaptors Mff and Fis1 (Koch et al., 2005; Gandre-Babbe and van der Bliek, 2008; Otera et al., 2010).”
Molecular mechanisms and physiologic functions of mitochondrial dynamics
Otera, H., & Mihara, K. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr002 · Cited by 265
“In contrast, Mff overexpression induced mitochondrial fragmentation, concomitant with increased Drp1 recruitment to the mitochondria (61).”
BackgroundInfluentialSelf-citationAMPK signaling and its targeting in cancer progression and treatment
Hsu, C.-C., Peng, D., Cai, Z., & Lin, H. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.04.006 · Cited by 265
AMPK: Regulation of Metabolic Dynamics in the Context of Autophagy
Tamargo‐Gómez, I., & Mariño, G. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123812 · Cited by 258
“MFF is a mitochondrial outer-membrane protein, which recruits cytoplasmic DRP1 (dynamin 1 like protein) to the mitochondrial outer membrane [105].”
BackgroundProgramming axonal mitochondrial maintenance and bioenergetics in neurodegeneration and regeneration
Cheng, X., Huang, N., & Sheng, Z. (2022) · Neuron · doi:10.1016/j.neuron.2022.03.015 · Cited by 257
Mitochondrial morphology in mitophagy and macroautophagy
Gomes, L. C., & Scorrano, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.012 · Cited by 259
“The core mitochondrial fission machinery in mammals is constituted by the cytoplasmic dynamin-related protein 1, DRP1 [86] and the outer mitochondrial membrane (OMM) proteins, FIS1 [87] and MFF [88].”
Background
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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