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MiD49 and MiD51, new components of the mitochondrial fission machinery
Open accessAbstract
Mitochondria form intricate networks through fission and fusion events. Here, we identify mitochondrial dynamics proteins of 49 and 51 kDa (MiD49 and MiD51, respectively) anchored in the mitochondrial outer membrane. MiD49/51 form foci and rings around mitochondria similar to the fission mediator dynamin-related protein 1 (Drp1). MiD49/51 directly recruit Drp1 to the mitochondrial surface, whereas their knockdown reduces Drp1 association, leading to unopposed fusion. Overexpression of MiD49/51 seems to sequester Drp1 from functioning at mitochondria and cause fused tubules to associate with actin. Thus, MiD49/51 are new mediators of mitochondrial division affecting Drp1 action at mitochondria.
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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 [91]
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“Previous studies found that Drp1 function is controlled by several posttranslational modifications, such as phosphorylation (Palmer et al., 2011b), SUMOylation (Braschi et al., 2009; Guo et al., 2013), and ubiquitylation (Horn et al., 2011).”
BackgroundInfluentialMitochondrial Dynamics: An Emerging Paradigm in Ischemia-Reperfusion Injury
Calo, L., Dong, Y., Kumar, R., Przyklenk, K., & Sanderson, T. H. (2013) · Current Pharmaceutical Design · doi:10.2174/138161281939131127110701 · Cited by 53
Mitophagy: An Emerging Target in Ocular Pathology
Skeie, J. M., Nishimura, D. Y., Wang, C. L., Schmidt, G. A., Aldrich, B. T., & Greiner, M. A. (2021) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.62.3.22 · Cited by 55
Mitochondrial Fission: Regulation and ER Connection
Lee, H., & Yoon, Y. (2014) · Molecules and Cells · doi:10.14348/molcells.2014.2329 · Cited by 53
“Fis1, mitochondrial fission factor (Mff), mitochondrial dynamics protein of 49 kDa and 51 kDa (MiD49/MiD51), and mitochondrial elongation factor 1 (MIEF1, identical to MiD51) have all been suggested to function as DLP1 receptors (Otera et al., 2010; Palmer et al., 2011; 2013; Zhao et al., 2011).”
BackgroundCompletion of BAX recruitment correlates with mitochondrial fission during apoptosis
Maes, M. E., Grosser, J. A., Fehrman, R. L., Schlamp, C. L., & Nickells, R. W. (2019) · Scientific Reports · doi:10.1038/s41598-019-53049-w · Cited by 57
Mitochondrial Dynamics Imbalance: A Strategy for Promoting Viral Infection
Ren, Z., Zhang, X., Ding, T., Zhong, Z., Hu, H., Xu, Z., & Deng, J. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01992 · Cited by 50
“Therefore, when MiDs are overexpressed, inactive S637 phosphorylated Drp1 is recruited into mitochondria in large quantities, eventually leading to mitochondrial elongation (Palmer et al., 2011; Zhao et al., 2011).”
BackgroundMitochondrial Membrane Remodeling
Yang, Z., Wang, L., Yang, C., Pu, S., Guo, Z., Wu, Q., Zhou, Z., & Zhao, H. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.786806 · Cited by 54
Mitochondrial Dynamics as a Therapeutic Target for Treating Cardiac Diseases
Ong, S., & Hausenloy, D. J. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_7 · Cited by 50
“…James et al. 2003; Stojanovski et al. 2004); Mitochondrial fission factor – Mff (Gandre-Babbe and van der Bliek 2008; Otera et al. 2010; Losón et al. 2013); mitochondrial dynamics proteins of 49 and 51 kDa – MiD49/51 (Palmer et al. 2011, 2013; Losón et al. 2013, 2014, 2015)) have been suggested.”
Mitochondrial quality control in amyotrophic lateral sclerosis: towards a common pathway?
Khalil, B., & Liévens, J.-C. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.211179 · Cited by 51
Molecular Machinery and Pathophysiology of Mitochondrial Dynamics
Chiu, Y., Lin, S., Kuo, C.-H., & Li, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.743892 · Cited by 50
“In mammalian cells, Drp1 receptors identified include Fis1, Mff, and Mid49/51 (Otera et al., 2010; Palmer et al., 2011; Zhao et al., 2011; Loson et al., 2013); all three can recruit Drp1 to the OMM with Mff having the strongest binding effect (Loson et al., 2013).”
BackgroundFang, C., Ren, P., Bian, G., Wang, J., Bai, J., Huang, J., Ding, Y., Li, X., Li, M., & Hou, Z. (2023) · EMBO Reports · doi:10.15252/embr.202256635 · Cited by 49
“Recruited Drp1 and its adaptors (Fis1, MiD49, MiD50, and Mff) assemble mitochondrial divisome around OMM to mediate membrane constriction and scission in a GTP-dependent manner (Gandre-Babbe & van der Bliek, 2008; Otera et al , 2010; Palmer et al , 2011).”
Zhou, L., Li, R., Liu, C.-Y., Sun, T., Aung, L. H. H., Chen, C., Gao, J., Zhao, Y., & Wang, K. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.037 · Cited by 49
A unique dynamin-related protein is essential for mitochondrial fission in Toxoplasma gondii
Melatti, C., Pieperhoff, M. S., Lemgruber, L., Pohl, E., Sheiner, L., & Meissner, M. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007512 · Cited by 45
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Mitochondrial Dynamics and Liver Cancer
Hernández‐Álvarez, M. I., & Antonio Zorzano, A. (2021) · Cancers · doi:10.3390/cancers13112571 · Cited by 50
Xiao, L., Xian, H., Lee, K. Y., Xiao, B., Wang, H., Yu, F., Shen, H., & Liou, Y. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.673343 · Cited by 46
Recent insights into the structure and function of Mitofusins in mitochondrial fusion
Cohen, M. M., & Tareste, D. C. (2018) · F1000Research · doi:10.12688/f1000research.16629.1 · Cited by 49
Imaging Mitochondrial Functions: From Fluorescent Dyes to Genetically-Encoded Sensors
Gökerküçük, E. B., Tramier, M., & Bertolin, G. (2020) · Genes · doi:10.3390/genes11020125 · Cited by 47
The relevance of mitochondrial morphology for human disease
Navaratnarajah, T., Anand, R., Reichert, A. S., & Distelmaier, F. (2021) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2021.105951 · Cited by 49
Viral Infection Modulates Mitochondrial Function
Li, X., Wu, K., Zeng, S., Zhao, F., Fan, J., Li, Z., Yi, L., Ding, H., Zhao, M., Fan, S., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084260 · Cited by 49
“When MiDs are overexpressed, they recruit a large number of inactive S637 phosphorylated Drp1 into mitochondria to mediate mitochondrial elongation [21,22].”
BackgroundLong COVID-19 and the Heart: Is Cardiac Mitochondria the Missing Link?
Chang, X., Ismail, N. I., Rahman, A., Xu, D., Chan, R. W. Y., Ong, S., & Ong, S. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0126 · Cited by 53
“…fission factor (Mff), and the interaction mechanism between Fis1 and Drp1 also plays a role in regulating mitochondrial fission (Smirnova et al, 1998; Liu and Chan, 2015; Otera et al, 2010; Zhou et al, 2017) and MiD49/51 (Loso´n et al, 2014; Otera et al, 2016; Palmer et al, 2013; Palmer et al, 2011).”
Mitochondrial dynamics and inter-mitochondrial communication in the heart
Cao, Y., & Zheng, M. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.01.017 · Cited by 49
Mohamed, D. I., Ezzat, S. F., Elayat, W. M., El-Kharashi, O. A., El-Kareem, H. F. A., Nahas, H. H. A., Abdel‐Wahab, B. A., Alshawwa, S. Z., Saleh, A., Helmy, Y. A., et al. (2022) · Pharmaceuticals · doi:10.3390/ph15070832 · Cited by 46
“On the other hand, MID51 is a mitochondrial membrane protein that mediates mitochondrial fission [38,93,94].”
BackgroundLinking mitochondrial dynamics to mitochondrial protein quality control
Haroon, S., & Vermulst, M. (2016) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2016.04.004 · Cited by 46
Splitting up the powerhouse: structural insights into the mechanism of mitochondrial fission
Richter, V., Singh, A. P., Kvansakul, M., Ryan, M. T., & Osellame, L. D. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1950-y · Cited by 48
Self-citationMitochondrial 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
Wnt Signaling and Its Impact on Mitochondrial and Cell Cycle Dynamics in Pluripotent Stem Cells
Rasmussen, M. L., Ortolano, N. A., Romero-Morales, A. I., & Gama, V. (2018) · Genes · doi:10.3390/genes9020109 · Cited by 44
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Regulation of neuronal bioenergetics as a therapeutic strategy in neurodegenerative diseases
Onyango, I. G., Bennett, J. P., & Stokin, G. B. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.303007 · Cited by 45
“Loson OC, Song Z, Chen H, Chan DC (2013) Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission.”
BackgroundInfluentialHu, D., Liu, Z., & Qi, X. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.746873 · Cited by 44
“There are indications that MFF and MiD49/51 interact to form a complex that mediates DRP1-dependent fission (Palmer et al., 2011).”
Background
Metadata
- Authors
- Palmer, C. S., Osellame, L. D., Laine, D., Koutsopoulos, O. S., Frazier, A. E., & Ryan, M. T.
- Affiliations
- La Trobe University (AU)
- Corresponding author
- Ryan, Michael T
- Venue
- The EMBO Reports
- Published
- 2011-04-21
- Volume
- 12
- Issue
- 6
- Pages
- 565-573
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC3128275
- OpenAlex
- W2005607645
- Cited by
- 649
- References
- 32
- Citations by year
- 2026: 18 · 2025: 34 · 2024: 40 · 2023: 36 · 2022: 48 · 2021: 63 · 2020: 56 · 2019: 47 · 2018: 44 · 2017: 48 · 2016: 45 · 2015: 48 · 2014: 43 · 2013: 45 · 2012: 24
- FWCI
- 15.70
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Medical Research Council
- National Health and Medical Research Council
- 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
- MiD51, mitochondrial fission, mitochondrial dynamics, Drp1, mitochondrial outer membrane, mitochondrial fusion, actin, mitochondrial division, dynamin-related proteins
- MeSH terms
- Actins, Amino Acid Sequence, Animals, Carbonyl Cyanide m-Chlorophenyl Hydrazone, Cell Line, Chlorocebus aethiops, HeLa Cells, Humans, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Molecular Sequence Data, Peptide Elongation Factors, Uncoupling Agents, Sequence Alignment, Receptors, Cytoplasmic and Nuclear, COS Cells, Protein Transport, Mitochondrial Proteins, RNA Interference, Mitochondrial Membranes, Mice, Membrane Potential, Mitochondrial
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