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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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“Mitochondrial fission is further enhanced by Fis1 [20,21], Mff [22,23], MiD49 and MiD51 [24–26], which contribute to fission in numerous ways, including the recruitment of Drp1 to the mitochondrial membrane.”
BackgroundInfluentialSplitting up the powerhouse: structural insights into the mechanism of mitochondrial fission
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“Although MFF is expressed as multiple splice variants across various cell types, its expression is variable in different human tissues and cell types.(46,47) The Human Protein Atlas Program reports that MFF protein is undetectable in endothelial cells in colon and cerebral cortex tissue (http://www.”
BackgroundMitochondrial fission mediated by Drp1-Fis1 pathway and neurodegenerative diseases
Shi, W., Tan, C., Liu, C., & Chen, D. (2022) · Reviews in the Neurosciences · doi:10.1515/revneuro-2022-0056 · Cited by 51
Lackner, L. L. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.02.011 · Cited by 48
Sánchez‐Alvarez, R., Francesco, E. M. D., Fiorillo, M., Sotgia, F., & Lisanti, M. P. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01776 · Cited by 50
ER–Mitochondria Contact Sites Reporters: Strengths and Weaknesses of the Available Approaches
Giamogante, F., Barazzuol, L., Brini, M., & Calí, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218157 · Cited by 51
Mitochondrial Dynamics at Different Levels: From Cristae Dynamics to Interorganellar Cross Talk
Kondadi, A. K., & Reichert, A. S. (2024) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-030822-020736 · Cited by 46
Role of Mitochondrial Dysfunctions in Neurodegenerative Disorders: Advances in Mitochondrial Biology
Kathiresan, D. S., Balasubramani, R., Marudhachalam, K., Jaiswal, P., Ramesh, N., Suruthi, G. S., Moorthi, P. V., & Vijayan, M. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04469-x · Cited by 49
“Conversely, an overexpression of MFF leads to the recruitment of Drp1 to the Mt, inducing hyper-fission in these cells [172].”
Human mitochondrial Fis1 links to cell cycle regulators at G2/M transition
Lee, S.-M., Park, Y., Kim, S., Nguyen, T. K. O., Yoo, Y., Chan, G. K. T., Sun, X., & Cho, H. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1428-8 · Cited by 46
“Yeast Fis1p (an ortholog of hFis1) and Mff promote mitochondrial fission by recruiting Drp1 (dynamin-related protein1; a dynamin-related GtPase) to mitochondria [8, 9].”
BackgroundMethodInfluentialChursa, U., Nuñez‐Durán, E., Cansby, E., Amrutkar, M., Sütt, S., Ståhlman, M., Olsson, B., Borén, J., Johansson, M. E., Bäckhed, F., et al. (2016) · Diabetologia · doi:10.1007/s00125-016-4171-5 · Cited by 46
“MFF knockdown in mammalian cells resulted in an interconnected tubular network of mitochondria, whereas MFF overexpression stimulated mitochondrial fission [31, 47].”
BackgroundWang, H.-H., Wu, Y., Tseng, Y.-M., Su, C., Hsieh, C., & Yeh, H. (2019) · Angiogenesis · doi:10.1007/s10456-019-09680-2 · Cited by 47
Seo, B. J., Choi, J., La, H., Habib, O., Choi, Y., Hong, K., & Tae, J. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101599 · Cited by 44
Aung, L. H. H., Jumbo, J. C. C., Wang, Y., & Li, P. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.06.006 · Cited by 45
“Mff serves as a Drp1 adaptor, promoting the recruitment and association of Drp1 to the mitochondrial surface.(85,86,88) MiD49/MIEF2 has an N-terminal TM domain that is attached to the OMM, followed by the NTD domain.”
BackgroundEpigenetic signature: implications for mitochondrial quality control in human aging
D’Aquila, P., Montesanto, A., Rango, F. D., Guarasci, F., Passarino, G., & Bellizzi, D. (2019) · Aging · doi:10.18632/aging.101832 · Cited by 42
Li, G., Xu, K., Xing, W., Yang, H., Li, Y., Wang, X., Zhou, J., An, J., Dong, L., Zhang, X., et al. (2022) · Hypertension · doi:10.1161/hypertensionaha.122.19126 · Cited by 44
Mitochondria: At the crossroads between mechanobiology and cell metabolism
Su, É., Villard, C., & Manneville, J. (2023) · Biology of the Cell · doi:10.1111/boc.202300010 · Cited by 44
Multiple paths to peroxisomes: Mechanism of peroxisome maintenance in mammals
Hua, R., & Kim, P. K. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.09.026 · Cited by 43
Zhang, C., Wang, J., Zhu, J., Chen, Y., & Han, X. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.134702 · Cited by 44
Ovarian Cancer: A Landscape of Mitochondria with Emphasis on Mitochondrial Dynamics
Rasmo, D. D., Cormio, A., Cormio, G., & Signorile, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021224 · Cited by 44
“The recruitment of DRP1 is also mediated by the mitochondrial receptor FIS1, mitochondrial dynamics proteins of 49 kDa and 51 kDa (MID49 and MID51), and the mitochondrial fission factor (MFF) [92].”
BackgroundMitochondrial Function and Reactive Oxygen/Nitrogen Species in Skeletal Muscle
Chen, M., Li, Y., Deng, S., Zhao, Y., Lian, Z., & Yu, K. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.826981 · Cited by 49
“It then works in conjunction with MFF and FIS1 to wrap around and constrict the mitochondria to promote the fission of the mitochondrial network (Ingerman et al., 2005; Otera et al., 2010; Losón et al., 2013) (Figure 2).”
BackgroundCellular Bioenergetics: Experimental Evidence for Alcohol-induced Adaptations
Simon, L., & Molina, P. E. (2022) · Function · doi:10.1093/function/zqac039 · Cited by 45
Nolden, K. A., Harwig, M. C., & Hill, R. B. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105380 · Cited by 42
“Known Drp1-recruiting proteins in mammals include mitochondrial fi ssion protein 1 (Fis1), Mff, MiD49, and MiD51 (13 – 19).”
BackgroundThe role of mitochondrial dynamics in disease
Wang, Y., Dai, X., Li, H., Jiang, H., Zhou, J.-F., Zhang, S., Guo, J., Shen, L., Yang, H., Lin, J. M., et al. (2023) · MedComm · doi:10.1002/mco2.462 · Cited by 41
“7,47 48–50 In 2021, FIS1 was reported to recruit DRP1 to participate in mitochondrial asymmetrical fission, whereas MFF seems to be uniquely related to symmetrical fission.”
BackgroundChan, W. S., Ng, C. F., Pang, B. P. S., Hang, M., Tse, M. C. L., Iu, E. C. Y., Ooi, X. C., Yang, X., Kim, J. K., Lee, C. W., et al. (2024) · Science Signaling · doi:10.1126/scisignal.adh2783 · Cited by 47
“AMPK-mediated phosphorylation of Ser 146 in mitochondrial fission factor (MFF), a mitochondrial membrane protein that recruits DRP1 to the mitochondria ( 48 ), was also enhanced by exercise training in Fl/Fl muscle but not in MBKO muscle (Fig.”
BackgroundSinha, J. K., Jorwal, K., Singh, D. K. K., Han, S. S., Bhaskar, R., & Ghosh, S. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04474-0 · Cited by 46
“…initiated by ER-mediated membrane contraction, recruits proteins like mitochondrial fission 1 protein (FIS1), MFF, mitochondrial dynamics proteins of 49 kDa and 51 kDa to the mitochondrial surface to assemble Drp1 interaction is vital for fission and its inhibition leads to dysfunction [83].”
Park, S. J., Lee, H., Jo, D. S., Jo, Y. K., Shin, J. H., Kim, H. B., Seo, H. M., Rubinsztein, D. C., Koh, J., Lee, E. K., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.10.017 · Cited by 42
“Drp1 primarily located in the cytosol is recruited to the mitochondria and interacts with outer membrane anchoring proteins such as Fis1, mitochondria fission factor, mitochondria dynamics protein 49 and 50 kDa [6,17,18].”
BackgroundMi RNA ‐30a inhibits AEC s‐II apoptosis by blocking mitochondrial fission dependent on Drp‐1
Mao, C., Zhang, J., Lin, S., Jing, L., Xiang, J., Wang, M., Wang, B., Xu, P., Liu, W., Song, X., et al. (2014) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12420 · Cited by 42
“Drp-1 is actively targeted to the outer mitochondrial membrane by non-GTPase receptor proteins, including mitochondrial fission protein 1, mitochondrial fission factor and mitochondrial elongation factor 1 [44, 45].”
BackgroundLu, Y., Rolland, S. G. M., & Conradt, B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103218108 · Cited by 41
“It has recently been suggested that the outer mitochondrial membrane protein Mff can act as a receptor for Drp1 in mammalian cells (13, 46).”
BackgroundmiR-27 regulates mitochondrial networks by directly targeting the mitochondrial fission factor
Tak, H., Kim, J., Jayabalan, A. K., Lee, H., Kang, H., Cho, D., Ohn, T., Nam, S. W., Kim, W., & Lee, E. K. (2014) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.73 · Cited by 42
Steffen, J. B. M., Falfushynska, H., Piontkivska, H., & Sokolova, I. M. (2020) · Frontiers in Marine Science · doi:10.3389/fmars.2020.604411 · Cited by 46
Regulatory Roles of PINK1-Parkin and AMPK in Ubiquitin-Dependent Skeletal Muscle Mitophagy
Seabright, A. P., & Lai, Y. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.608474 · Cited by 46
Mitochondrial dynamics in macrophages: divide to conquer or unite to survive?
Afroz, S. F., Raven, K. D., Lawrence, G. M. E. P., Kapétanovic, R., Schroder, K., & Sweet, M. J. (2023) · Biochemical Society Transactions · doi:10.1042/bst20220014 · Cited by 44
Ortiz-Sandoval, C. G., Hughes, S. C., Dacks, J. B., & Simmen, T. (2014) · Cellular Logistics · doi:10.4161/21592799.2014.986399 · Cited by 41
Saita, S., Ishihara, T., Maeda, M., Iemura, S., Natsume, T., Mihara, K., & Ishihara, N. (2016) · Genes to Cells · doi:10.1111/gtc.12351 · Cited by 43
Self-citationMitochondrial Dynamics: ER Actin Tightens the Drp1 Noose
Prudent, J., & McBride, H. M. (2016) · Current Biology · doi:10.1016/j.cub.2016.01.009 · Cited by 43
Remote Ischemic Conditioning Influences Mitochondrial Dynamics
Cellier, L., Tamareille, S., Kalakech, H., Guillou, S., Lenaers, G., Prunier, F., & Mirebeau‐Prunier, D. (2015) · Shock · doi:10.1097/shk.0000000000000500 · Cited by 41
“This finding may be related to the existence of other adaptor proteins, apart from FIS1, which are able to bind to DRP1 to promote fission, such as the mitochondrial fission factor (MFF) (28) or mitochondrial elongation factor (MIEF1) (29).”
BackgroundClinical and Biochemical Features in a Patient With Mitochondrial Fission Factor Gene Alteration
Nasca, A., Nardecchia, F., Commone, A., Semeraro, M., Legati, A., Garavaglia, B., Ghezzi, D., & Leuzzi, V. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00625 · Cited by 42
“Knockdown of MFF results in mitochondrial elongation and formation of tubular peroxisomes (Otera et al., 2010; Itoyama et al., 2013).”
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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