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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]
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]
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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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BackgroundInfluentialThe membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission
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“We also find that Mff, which recruits Drp1 to the mitochondrial membrane towards causing mitochondrial fission [46], overwhelmingly shares its cell cycle co-expression module with Drp1.”
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“The major receptors for Drp1 on the outer membrane are mitochondrial fission factor (Mff) [32] and, to a lesser extent, Fission 1 (Fis1) [51].”
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Guo, C., Wilkinson, K. A., Evans, A. J., Rubin, P. P., & Henley, J. M. (2017) · Scientific Reports · doi:10.1038/srep43811 · Cited by 77
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“Abbreviations T2DM Type 2 diabetes mellitus HF Heart failure ATP Adenosine triphosphate FDG-PET 18F-2-deoxyglucose positron emission tomography HFrEF HF with a reduced ejection fraction HFpEF HF with a preserved ejection fraction HFmrEF HF with a mid-range ejection fraction mPTP Mitochondrial permeability transition p…”
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“Mff (the OMM-anchored mitochondrial fission factor) was proposed as the bona fide receptor, essential for recruiting Drp1 to mitochondria and to promote mitochondrial fission [48].”
BackgroundDynamin-related Protein 1 (Drp1) Promotes Structural Intermediates of Membrane Division
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BackgroundThe regulation of tumor cell physiology by mitochondrial dynamics
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“Of note, a particular recent study suggests that Mff is responsible for recruiting Drp1 to the foci at the outer mitochondrial membrane.(63) Downstream of mitochondria, the expression of CASP9, which encodes for the initiator caspase-9, is regulated by miR-133a, whereas CASP3, which encodes for the executioner caspase…”
BackgroundMSTO1 is a cytoplasmic pro‐mitochondrial fusion protein
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“In both fusion and fission, the key factors are the large GTPase enzymes belonging to the large dynamin superfamily; fusion is mainly regulated by MFN1, MFN2, and OPA1 (Meeusen et al, 2006; Song et al, 2009), while fission requires mainly DRP1 (Otera et al, 2010; Loson et al, 2013).”
BackgroundWu, D., Dasgupta, A., Read, A. D., Bentley, R. E. T., Motamed, M., Chen, K., Al‐Qazazi, R., Mewburn, J. D., Dunham‐Snary, K. J., Alizadeh, E., et al. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.12.452 · Cited by 69
“and MiD51 (mitochondrial dynamics protein 51 kDa) [217-221].”
Luteinizing Hormone Regulation of Inter-Organelle Communication and Fate of the Corpus Luteum
Przygrodzka, E., Plewes, M. R., & Davis, J. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189972 · Cited by 71
“Genetic knockdown of DRP1 and MFF, but not fission protein FIS1, disrupts exogenous stimuli–induced mitochondrial fission and apoptosis in HeLa and MEF cells [89].”
BackgroundTargeting Mitochondrial Metabolism as a Strategy to Treat Senescence
Lee, Y. H., Park, J. Y., Lee, H., Song, E. S., Kuk, M. U., Joo, J., Oh, S., Kwon, H. W., Park, J. T., & Park, S. C. (2021) · Cells · doi:10.3390/cells10113003 · Cited by 66
Insights on altered mitochondrial function and dynamics in the pathogenesis of neurodegeneration
McInnes, J. (2013) · Translational Neurodegeneration · doi:10.1186/2047-9158-2-12 · Cited by 65
“solic dynamin-related Drp1 to the mitochondrial outer membrane [5].”
BackgroundMitochondrial Quality Control in Cardiac Diseases
Campos, J. C., Bozi, L. H. M., Bechara, L. R. G., Lima, V. M., & Ferreira, J. C. B. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00479 · Cited by 67
Liu, W., Tian, F., Kurata, T., Morimoto, N., & Abe, K. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.23016 · Cited by 62
“, 2003) and mitochondrial fission factor (Mff; Otera et al., 2010).”
BackgroundAung, K., & Hu, J. (2011) · The Plant Cell · doi:10.1105/tpc.111.090142 · Cited by 63
“…mammalian mitochondrial and peroxisome division factor Mff, which is a C-terminal tail-anchored (C-TA) protein with a cytosolic CC domain (Gandre-Babbe and van der Bliek, 2008; Otera et al., 2010), Arabidopsis homologous proteins PLASTID DIVISION1 (PDV1) and PDV2 also contain CC domains.”
BackgroundRelationship between OPA1 and cardiolipin in mitochondrial inner-membrane fusion
Ban, T., Kohno, H., Ishihara, T., & Ishihara, N. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.05.016 · Cited by 63
George, D., Hackelberg, S., Jayaraj, N. D., Ren, D., Edassery, S. L., Rathwell, C. A., Miller, R. E., Malfait, A., Savas, J. N., Miller, R. J., et al. (2021) · Pain · doi:10.1097/j.pain.0000000000002391 · Cited by 64
“Mff overexpression causes mitochondrial fragmentation, consistent with increased fission rates.(64,78) These data suggest a role formitochondria in the pathogenesis of axonal degeneration and mechanical allodynia in the HFD mouse model of PDN.”
BackgroundMethodKrzystek, T. J., Banerjee, R., Thurston, L., Huang, J., Swinter, K., Rahman, S. N., Falzone, T. L., & Gunawardena, S. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04046-3 · Cited by 68
“Indeed, several reports indicate that DRP1-receptor interactions are of low-affinity or transient, and can only be detected using cross-linking reagents [50, 51].”
BackgroundColpman, P., Dasgupta, A., & Archer, S. L. (2023) · Cells · doi:10.3390/cells12141897 · Cited by 66
“found that overexpression of MiD51/49 induces mitochondrial elongation, possibly by inhibiting fission [89], whereas overexpression of MFF increased mitochondrial fragmentation [86,90].”
BackgroundResultInfluentialThe lifecycle of skeletal muscle mitochondria in obesity
Pileggi, C. A., Parmar, G., & Harper, M. (2021) · Obesity Reviews · doi:10.1111/obr.13164 · Cited by 61
Mitochondria-associated membranes: A hub for neurodegenerative diseases
Liu, J., & Yang, J. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112890 · Cited by 67
Lacombe, A., & Scorrano, L. (2024) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2024.02.001 · Cited by 65
In vivo functions of Drp1: Lessons learned from yeast genetics and mouse knockouts
Sesaki, H., Adachi, Y., Kageyama, Y., Itoh, K., & Iijima, M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.11.024 · Cited by 62
“Mff is a 33-kDa protein anchored to the outer membrane via its C-terminal transmembrane domain [47,48].”
BackgroundLysine deacetylases and mitochondrial dynamics in neurodegeneration
Guedes-Dias, P., & Oliveira, J. M. A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.005 · Cited by 63
“Thus, mitochondrial fission factor (Mff) was proposed as an essential factor for Drp1 recruitment, mediating fission independently from Fis1 [104].”
BackgroundBiosynthesis and roles of phospholipids in mitochondrial fusion, division and mitophagy
Zhang, Q., Tamura, Y., Roy, M., Adachi, Y., Iijima, M., & Sesaki, H. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1648-6 · Cited by 65
“Drp1 is a cytosolic protein, which assembles onto the surface of mitochondria by associating with its receptor proteins, including the Mff, Fis1 and Mid/MIeF proteins [31–34, 120–124].”
Mitochondrial-associated metabolic disorders: foundations, pathologies and recent progress
McInnes, J. (2013) · Nutrition & Metabolism · doi:10.1186/1743-7075-10-63 · Cited by 64
“It is thought that the ER encircles mitochondria, providing an initial constriction before the Drp1 protein provides the mechanical force to carry out fission [12,13,44].”
BackgroundLi, S., Wang, J., Zhou, A., Khan, F. A., Hu, L., & Zhang, S. (2016) · Oncotarget · doi:10.18632/oncotarget.10817 · Cited by 62
“Besides, mitochondrial fission is promoted by several mitochondrial outer membrane proteins, including mitochondrial fission factor (Mff), mitochondrial fission protein 1 (Fis1), mitochondrial dynamic proteins of 49 and 51kDa (MiD49 and MiD51, respectively) [10-12].”
BackgroundMFF Regulation of Mitochondrial Cell Death Is a Therapeutic Target in Cancer
Seo, J. H., Chae, Y. C., Kossenkov, A. V., Lee, Y. G., Tang, H., Agarwal, E., Gabrilovich, D. I., Languino, L. R., Speicher, D. W., Shastrula, P. K., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1982 · Cited by 61
“In this study, we uncovered a novel, therapeutically actionable interface between a regulator of mitochondrial fission, Mitochondrial Fission Factor (MFF) (18) and VDAC1 in the regulation of organelle cell death, selectively in cancer (19).”
BackgroundProtein Kinase C-δ Mediates Kidney Tubular Injury in Cold Storage–Associated Kidney Transplantation
Zhu, J., Zhang, G., Song, Z., Xiang, X., Shu, S., Liu, Z., Yang, D., Wei, Q., & Dong, Z. (2020) · Journal of the American Society of Nephrology · doi:10.1681/asn.2019101060 · Cited by 60
Mitochondrial Damage Response and Fate of Normal Cells Exposed to FLASH Irradiation with Protons
Guo, Z., Buonanno, M., Harken, A., Zhou, G., & Hei, T. K. (2022) · Radiation Research · doi:10.1667/rade-21-00181.1 · Cited by 62
“Upon activation, Drp1 translocate to the mitochondria through binding to its mitochondrial adaptors, such as Fis1 (29), Mff (30) and MiD49/51 (31) to process fission.”
BackgroundJugé, R., Breugnot, J., Silva, C. D., Bordes, S., Closs, B., & Aouacheria, A. (2016) · Scientific Reports · doi:10.1038/srep35065 · Cited by 61
Lu, Y., Chen, L., Ye, J., Chen, C., Zhou, Y., Li, K., Zhang, Z., & Peng, M. (2020) · Aging · doi:10.18632/aging.102659 · Cited by 64
“During fission, cytosolic Drp1 is recruited to the mitochondrial outer membrane, followed by its oligomerization into a ring-like structure to sever the mitochondrial membrane by self-assembly and GTP hydrolysis [34, 35].”
BackgroundLavin, K. M., Coen, P. M., Baptista, L. C. P., Bell, M. B., Drummer, D. J., Harper, S. A., Lixandrão, M. E., McAdam, J. S., O’Bryan, S. M., Ramos, S. V., et al. (2022) · Comprehensive physiology · doi:10.1002/cphy.c200033 · Cited by 78
The Multifaceted Regulation of Mitochondrial Dynamics During Mitosis
Pangou, E., & Sumara, I. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.767221 · Cited by 66
O'Rourke, S. A., Neto, N. G. B., Devilly, E., Shanley, L. C., Fitzgerald, H. K., Monaghan, M. G., & Dunne, A. (2022) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2022.05.015 · Cited by 62
Nardin, A., Schrepfer, E., & Ziviani, E. (2016) · Current Neuropharmacology · doi:10.2174/1570159x13666151030104414 · Cited by 61
“Fis1 and MFF operate as Drp1 receptor on mitochondria outer membrane [51-53].”
Niemann, J., Johne, C., Schröder, S., Koch, F., Ibrahim, S. M., Schultz, J., Tiedge, M., & Baltrusch, S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.035 · Cited by 61
“Gene expression of MFF showed comparable increases in both strains from 3 to 9 months followed by a decrease at 12 months (Fig.”
BackgroundApoptotic foci at mitochondria: in and around Bax pores
Ugarte‐Uribe, B., & García‐Sáez, A. J. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0217 · Cited by 59
Non‐mammalian Hosts and Photobiomodulation: Do All Life‐forms Respond to Light?
Hamblin, M. R., Huang, Y., & Heiskanen, V. (2019) · Photochemistry and Photobiology · doi:10.1111/php.12951 · Cited by 58
“tion factor 1 (MEIF1), have been reported to promote mitochondrial fission by recruiting Drp1 (39,40).”
BackgroundInfluentialUSP19 promotes hypoxia-induced mitochondrial division via FUNDC1 at ER-mitochondria contact sites
Chai, P., Cheng, Y., Hou, C., Yin, L., Zhang, D., Hu, Y., Chen, Q., Zheng, P., Teng, J., & Chen, J. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202010006 · Cited by 59
Liu, T., Yu, R., Jin, S., Han, L., Lendahl, U., Zhao, J., & Nistér, M. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2013.07.010 · Cited by 58
Benigni, A., Perico, L., & Macconi, D. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6682 · Cited by 59
Mortal engines: Mitochondrial bioenergetics and dysfunction in neurodegenerative diseases
Joshi, A. U., & Mochly‐Rosen, D. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.08.010 · Cited by 57
“Moreover, Mff and Fis1 occur in separate complexes, indicating that they may have distinct roles in regulating mitochondrial fission (20, 43, 58); Mff is localized in punctate structures on mitochondria in a manner independent of Drp1 and Fis1 and in contrast to the uniform distribution of Fis1 on the mitochondrial ou…”
BackgroundInfluentialGuo, Y., Wang, S., Liu, Y., Fan, L., Booz, G. W., Roman, R. J., Chen, Z., & Fan, F. (2020) · GeroScience · doi:10.1007/s11357-020-00179-z · Cited by 54
“MFF recruits DRP1 to promote mitochondrial fission (Otera et al. 2010).”
Wu, H., Wei, H., Sehgal, S. A., Liu, L., & Chen, Q. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.03.030 · Cited by 58
Virga, D. M., Hamilton, S., Osei, B., Morgan, A., Kneis, P., Zamponi, E., Park, N. J., Hewitt, V. L., Zhang, D., Gonzalez, K. C., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46463-w · Cited by 61
Losón, O. C., Meng, S., Ngo, H., Liu, R., Kaiser, J. T., & Chan, D. C. (2015) · Protein Science · doi:10.1002/pro.2629 · Cited by 57
“Early studies suggested that Fis1 is important for fission, but more recent studies with knockout cells indicate that Fis1 has little or no role in mitochondrial fission.(19,20) In contrast, Mff is critical for the recruitment of Drp1 and regulation of mitochondrial morphology in several cell types.”
BackgroundCoughlan, M. T., Higgins, G. C., Nguyen, T.-V., Penfold, S. A., Thallas‐Bonke, V., Tan, S. M., Ramm, G., Bergen, N. J. V., Henstridge, D. C., Sourris, K. C., et al. (2016) · Diabetes · doi:10.2337/db15-0864 · Cited by 57
“5I), which facilitates the recruitment of Drp-1 to the mitochondrial surface (39), in Aifm1 mice.”
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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