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MiD49 and MiD51, new components of the mitochondrial fission machinery
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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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Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002 · cited 3×
“Division also takes place in cells undergoing differentiation and growth, and has a role in removing damaged and aging organelles through mitophagy (Twig et al, 2008; Westermann, 2010).”
BackgroundDynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007152 · Cited by 1,110 · cited 2×
“Other proteins have been implicated in mitochondrial fission, including endophilin BI (Karbowski et al, 2004), MARCH5 (Karbowski et al, 2007) and Mff (Gandre-Babbe & van der Bliek, 2008; Otera et al, 2010).”
BackgroundMitochondrial Dynamics in Mammalian Health and Disease
Liesa, M., Palacín, M., & Zorzano, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00030.2008 · Cited by 953
Chang, C., & Blackstone, C. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700083200 · Cited by 824
Yoon, Y., Krueger, E. W., Oswald, B. J., & McNiven, M. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5409-5420.2003 · Cited by 820
The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast
Bleazard, W., McCaffery, J. M., King, E. J., Bale, S., Mozdy, A. D., Tieu, Q., Nunnari, J. M., & Shaw, J. M. (1999) · Nature Cell Biology · doi:10.1038/13014 · Cited by 795
Gandre-Babbe, S., & van der Bliek, A. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1287 · Cited by 769
A Human Dynamin-related Protein Controls the Distribution of Mitochondria
Смирнова, Е. А., Shurland, D., Ryazantsev, S. N., & van der Bliek, A. M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.351 · Cited by 734
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The cell biology of mitochondrial membrane dynamics
Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550
Mitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397
Mitochondrial Dynamics in the Regulation of Nutrient Utilization and Energy Expenditure
Liesa, M., & Shirihai, O. S. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.002 · Cited by 1,341
“MiD49 and MiD51 have been recently described to recruit Drp1 to the mitochondria, although the role of MiD49- and MiD51-mediated recruitment in mitochondrial fission is still under investigation (Palmer et al., 2011; Losón et al., 2013).”
BackgroundFis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission
Losón, O. C., Song, Z., Chen, H., & Chan, D. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0721 · Cited by 1,235
“In particular, it was unclear why MiD overexpression causes mitochondrial elongation (Palmer et al., 2011; Zhao et al., 2011).”
BackgroundInfluentialMitochondrial dysfunction: mechanisms and advances in therapy
Yao, Z., Li, H., Liao, P., Chen, L., Pan, Y., Zheng, Y., Zhang, C., Liu, D., Zheng, M., & Gao, J. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01839-8 · Cited by 1,382
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196
Structure and function of ER membrane contact sites with other organelles
Phillips, M. J., & Voeltz, G. K. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.8 · Cited by 933
Mitochondrial dynamics and mitochondrial quality control
Ni, H.-M., Williams, J. A., & Ding, W.-X. (2015) · Redox Biology · doi:10.1016/j.redox.2014.11.006 · Cited by 931
“Mitochondrial fission and fusion and motility in mitophagy Mitochondria are dynamic organelles that continuously undergo fission and fusion, which are necessary for cell survival and adaptation to changing conditions needed for cell growth, division, and distribution of mitochondria during…”
BackgroundCellular and molecular mechanisms of mitochondrial function
Osellame, L. D., Blacker, T. S., & Duchen, M. R. (2012) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2012.05.003 · Cited by 930
“40 Recent studies have highlighted the absolute reliance on Drp1 activity and have illustrated how aberrant mitochondrial morphology affects viability at the level of the whole organism.”
BackgroundSelf-citationMechanisms of Mitochondrial Fission and FusionPreprint
van der Bliek, A. M., Shen, Q., & Kawajiri, S. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011072 · Cited by 903
“Knockdown and overexpression studies of Mid49, Mid51/Mief, and GDAP1 have independently shown effects on mitochondrial fission, suggesting that there are multiple ways to control fission (Niemann et al. 2005; Palmer et al. 2011; Zhao et al. 2011).”
BackgroundThe i -AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission
Anand, R., Wai, T., Baker, M. J., Kladt, N., Schauss, A. C., Rugarli, E., & Langer, T. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201308006 · Cited by 812
Pernas, L. F., & Scorrano, L. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105011 · Cited by 845
Distinct fission signatures predict mitochondrial degradation or biogenesis.
Kleele, T., Rey, T., Winter, J., Zaganelli, S., Mahecic, D., Perreten Lambert, H., Ruberto, F. P., Nemir, M., Wai, T., Pedrazzini, T., et al. (2021) · Nature · doi:10.1038/s41586-021-03510-6 · Cited by 794
Here, there, and everywhere: The importance of ER membrane contact sites
Wu, H., Carvalho, P., & Voeltz, G. K. (2018) · Science · doi:10.1126/science.aan5835 · Cited by 689
Pervasive functional translation of noncanonical human open reading frames
Chen, J., Brunner, A., Cogan, J. Z., Nuñez, J. K., Fields, A. P., Adamson, B., Itzhak, D. N., Li, J. Y., Mann, M., Leonetti, M. D., et al. (2020) · Science · doi:10.1126/science.aay0262 · Cited by 654
Mitochondria in health, disease, and aging
Harrington, J. S., Ryter, S. W., Plataki, M. E., Price, D. R., & Choi, A. M. K. (2023) · Physiological Reviews · doi:10.1152/physrev.00058.2021 · Cited by 641
Mitochondrial Dysfunction in Cancer
Boland, M. L., Chourasia, A. H., & Macleod, K. F. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00292 · Cited by 521
The endoplasmic reticulum–mitochondria connection: One touch, multiple functions
Marchi, S., Patergnani, S., & Pinton, P. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.015 · Cited by 475
New insights into the function and regulation of mitochondrial fission
Otera, H., Ishihara, N., & Mihara, K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.002 · Cited by 501
“Opposite knockdown phenotypes, however, are also reported; Palmer et al. found that knockdown of MiD49 or MiD51 alone does not affect mitochondrial morphology, whereas the knock-down of both causes mitochondrial elongation [76].”
BackgroundInfluentialVaranita, T., Soriano, M. E., Romanello, V., Zaglia, T., Quintana-Cabrera, R., Semenzato, M., Menabò, R., Costa, V., Civiletto, G., Pesce, P., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.007 · Cited by 460
“chondrial Cristae”
BackgroundMitochondrial dynamics in neurodegeneration
Itoh, K., Nakamura, K., Iijima, M., & Sesaki, H. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.10.006 · Cited by 486
Function and regulation of the divisome for mitochondrial fission
Kraus, F., Roy, K., Pucadyil, T. J., & Ryan, M. T. (2021) · Nature · doi:10.1038/s41586-021-03214-x · Cited by 445
Self-citationQuality control of the mitochondrion
Ng, M. Y. W., Wai, T., & Simonsen, A. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.02.009 · Cited by 468
Diverse roles of mitochondria in ischemic stroke
Yang, J., Mukda, S., & Chen, S. (2018) · Redox Biology · doi:10.1016/j.redox.2018.03.002 · Cited by 459
Novel Drp1 inhibitor diminishes aberrant mitochondrial fission and neurotoxicity
Qi, X., Qvit, N., Su, Y.-C., & Mochly‐Rosen, D. (2012) · Journal of Cell Science · doi:10.1242/jcs.114439 · Cited by 441
“However, recent data suggest that other proteins [Mff, MiD51 (MIEF1) and MiD49] substitute for Fis1 in mammals (Otera et al., 2010; Zhao et al., 2011).”
BackgroundInfluentialMitochondrial quality control and muscle mass maintenance.
Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434
“Recently, new components of the mammalian fission machinery were identified (Otera et al., 2010; Palmer et al., 2011; Zhao et al., 2011).”
BackgroundMitochondria: from cell death executioners to regulators of cell differentiation
Kasahara, A., & Scorrano, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.08.005 · Cited by 433
Molecular mechanisms of mitochondrial dynamics
Tábara, L. C., Segawa, M., & Prudent, J. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00785-1 · Cited by 445
“Whereas MFF, a tail-anchored protein, serves as a DRP1 receptor at both mitochondrial and peroxisomal membranes 127 , both MiD49 and MiD51 exhibit exclusive mitochondrial localization 128,129 .”
Zhao, J., Liu, T., Jin, S., Wang, X., Qu, M., Uhlén, P., Tomilin, N., Shupliakov, O., Lendahl, U., & Nistér, M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.198 · Cited by 370
Guo, X. L., Disatnik, M., Monbureau, M., Shamloo, M., Mochly‐Rosen, D., & Qi, X. (2013) · Journal of Clinical Investigation · doi:10.1172/jci70911 · Cited by 379
Structural basis of mitochondrial receptor binding and constriction by DRP1
Kalia, R., Wang, R. Y., Yusuf, A., Thomas, P. V., Agard, D. A., Shaw, J. M., & Frost, A. S. (2018) · Nature · doi:10.1038/s41586-018-0211-2 · Cited by 385
Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity
Bertholet, A. M., Delerue, T., Millet, A. M., Moulis, M. F., David, C., Daloyau, M., Arnauné-Pelloquin, L., Davezac, N., Mils, V., Miquel, M. C., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.011 · Cited by 363
Wu, W., Lin, C., Wu, K., Jiang, L., Wang, X., Li, W., Zhuang, H., Zhang, X., Chen, H. H., Li, S., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593102 · Cited by 370
“…(mitochondrial dynamics proteins of 49 and 51 kDa); however, the role of FIS1 and MID49/51 in mitochondrial fission and fusion is still controversial (Stojanovski et al , 2004; Gandre-Babbe & van der Bliek, 2008; Otera et al , 2010; Palmer et al , 2011, 2013; Zhao et al , 2011; Loson et al , 2013).”
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“Consistent with their role in mitochondrial fission, loss of MFF, MiD49, and MiD50 leads to mitochondrial hyperfusion and defected DRP1 recruitment to the mitochondria [10] [11] [12] .”
BackgroundMitofusin 2: from functions to disease
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Cooperative and independent roles of the Drp1 adaptors Mff, MiD49 and MiD51 in mitochondrial fission
Osellame, L. D., Singh, A. P., Stroud, D. A., Palmer, C. S., Stojanovski, D., Ramachandran, R., & Ryan, M. T. (2016) · Journal of Cell Science · doi:10.1242/jcs.185165 · Cited by 336
“…cytosolic GTPase that is recruited to the surface of the organelle by the adaptors Mff, MiD49 (also known as MIEF2) and MiD51 (also known as MIEF1) (Gandre-Babbe and van der Bliek, 2008; Ingerman et al., 2005; Legesse-Miller et al., 2003; Otera et al., 2010; Palmer et al., 2011; Zhao et al., 2011).”
BackgroundInfluentialSelf-citationDisatnik, M., Ferreira, J. C. B., Campos, J. C., Gomes, M. K., Dourado, P. M. M., Qi, X., & Mochly‐Rosen, D. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000461 · Cited by 340
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“Also in contrast to yeast, mammalian Drp1 recruitment to mitochondria requires Mff, MIEF1/MiD51, and/or MiD49 (Otera et al., 2010; Palmer et al., 2011; Zhao et al., 2011).”
BackgroundPalmer, 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
“Immunofluorescence Assays—Immunofluorescence assays were performed as described previously (25).”
BackgroundMethodInfluentialSelf-citationMitochondrial 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
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Shirihai, O. S., Song, M., & Dorn, G. W. (2015) · Circulation Research · doi:10.1161/circresaha.116.306374 · Cited by 311
“Other proteins that may help recruit Drp1 to OMM are mitochondrial dynamics protein of 49 and 51 kDa (MiD49 and MiD51).(30,31) Finally, there is intriguing evidence that Drp1 can bind to mitofusins and evoking a change in Mfn structure from a fusion-incompetent closed conformation to a fusion-competent open configurat…”
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
“…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 et al , 2011), and mitochondrial fission protein Fis1 (Yoon et al , 2003; Koch et al , 2005).”
Hall, A. R., Burke, N., Dongworth, R. K., & Hausenloy, D. J. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12516 · Cited by 294
“…fission proteins: human fission factor-1 (Fis1), mitochondrial fission factor (MFF), and mitochondrial dynamics proteins of 49 and 51 kDa (MiD49 and MiD51, respectively) (Yoon et al., 2003; Gandre-Babbe and van der Bliek, 2008; Otera et al., 2010; Palmer et al., 2011; Loson et al., 2013).”
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“Dynamin-related protein 1 (Drp1), a member of the dynamin family of GTPases, is the major protein involved in the division of membranes through translocation from the cytosol to the outer mitochondrial membrane where constricting rings are formed [77].”
BackgroundMitochondrial division ensures the survival of postmitotic neurons by suppressing oxidative damage
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“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…”
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“Abbreviations AGER Advanced Glycosylation End-Product Specific Receptor AIM2 Absent In Melanoma 2 AMBRA1 Autophagy and Beclin 1 Regulator 1 AMBRA1ActA AMBRA1 fusion protein that localizes in the mitochondria AMPK AMP-activated protein kinase ARIH1 Ariadne RBR E3 Ubiquitin Protein Ligase 1 Atg32 autophagy-related prote…”
BackgroundHuman Fis1 regulates mitochondrial dynamics through inhibition of the fusion machinery
Yu, R., Jin, S., Lendahl, U., Nistér, M., & Zhao, J. (2019) · The EMBO Journal · doi:10.15252/embj.201899748 · Cited by 253
“…which are anchored in the mitochondrial outer membrane and serve to mediate recruitment of Drp1 to the mitochondrial surface (Gandre-Babbe & van der Bliek, 2008; Otera et al , 2010; Palmer et al , 2011; Zhao et al , 2011; Koirala et al , 2013; Liu et al , 2013; Loson et al , 2013; Yu et al , 2017).”
Abnormalities of Mitochondrial Dynamics in Neurodegenerative Diseases
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Structure, function, and regulation of mitofusin‐2 in health and disease
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“Reduced or enhanced expression of these proteins promotes fusion, due to decreased Drp1 association with mitochondria, or the sequestration of Drp1 at the mitochondria surface, respectively (Palmer et al., 2011, 2013).”
BackgroundMitophagy and mitochondrial integrity in cardiac ischemia-reperfusion injury
Yang, M., Linn, B. S., Zhang, Y., & Ren, J. T. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.05.007 · Cited by 253
The constriction and scission machineries involved in mitochondrial fission
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“…encoded by MIEF2 and MIEF1, respectively), which are anchored in the outer mitochondrial membrane, bind to and orchestrate the assembly of the contractile Drp1 rings at constriction sites (Gandre-Babbe and van der Bliek, 2008; Losón et al., 2013; Otera et al., 2010; Palmer et al., 2013, 2011).”
BackgroundSelf-citationMitochondrial dynamics in the adult cardiomyocytes: which roles for a highly specialized cell?
Piquereau, J., Caffin, F., Novotová, M., Lemaire, C., Veksler, V., Garnier, A., Ventura‐Clapier, R., & Joubert, F. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00102 · Cited by 251
“Three other proteins have been described like the mitochondria fission factor (Mff) (Otera et al., 2010), the mitochondrial dynamics protein of 49 kDa (MiD49) or 51 kDa (MiD51) (Palmer et al., 2011).”
BackgroundLC3/GABARAPs drive ubiquitin-independent recruitment of Optineurin and NDP52 to amplify mitophagy
Padman, B. S., Nguyen, T. N., Uoselis, L., Skulsuppaisarn, M., Nguyen, L. K., & Lazarou, M. (2019) · Nature Communications · doi:10.1038/s41467-019-08335-6 · Cited by 250
Romani, P., Nirchio, N., Arboit, M., Barbieri, V., Tosi, A., Michielin, F., Shibuya, S., Benoist, T., Wu, D., Hindmarch, C. C. T., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00843-w · Cited by 235
Drp1-dependent mitochondrial fission via MiD49/51 is essential for apoptotic cristae remodeling
Otera, H., Miyata, N., Kuge, O., & Mihara, K. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201508099 · Cited by 229
“The MOM proteins Fis1, Mff, MiD49/MIEF2, and MiD51/MIEF1 are reported to act as receptors of Drp1 in mammals, but recent studies revealed that Fis1 has little or no role in mitochondrial fission (Otera et al., 2010; Palmer et al., 2011; Zhao et al., 2011).”
BackgroundMitochondrial diseases: from molecular mechanisms to therapeutic advances
Wen, H., Deng, H., Li, B., Chen, J., Zhu, J., Zhang, X., Yoshida, S., & Zhou, Y. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02044-3 · Cited by 284
mTORC1 as a Regulator of Mitochondrial Functions and a Therapeutic Target in Cancer
de la Cruz-López, K. G., Toledo-Guzmán, M. E., Sánchez, E. O., & Carrancá, A. G. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01373 · Cited by 223
“Moreover, in vitro experiments with HCC cells, demonstrated that mitochondrial fission significantly promoted the reprogramming of focal adhesion dynamics and lamellipodia formation mainly, by activating the CA2+/CaMKII/ERK/FAK pathway, which was associated with a greater capacity for migration and invasion (123, 125).”
BackgroundYue, W., Chen, Z., Liu, H., Chen, Y., Chen, M., Feng, D., Yan, C., Wu, H., Du, L., Wang, Y., et al. (2014) · Cell Research · doi:10.1038/cr.2014.20 · Cited by 218
Li, S., Xu, S., Roelofs, B. A., Boyman, L., Lederer, W. J., Sesaki, H., & Karbowski, M. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201404050 · Cited by 214
“…receptors of Drp1, or expression of a dominant-negative mutant of MARCH5, a mitochondria-associated E3 ubiquitin ligase, led to mitochondrial accumulation of Drp1 fission complexes associated with abnormal elongation of mitochondria (Karbowski et al., 2007; Palmer et al., 2011; Losón et al., 2013).”
InfluentialKotiadis, V. N., Duchen, M. R., & Osellame, L. D. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.041 · Cited by 216
“certain how these proteins mediate this process [99,100].”
BackgroundSelf-citationMutations in Fis1 disrupt orderly disposal of defective mitochondria
Shen, Q., Yamano, K., Head, B. P., Kawajiri, S., Cheung, J. T. M., Wang, C., Cho, J.-H., Hattori, N., Youle, R. J., & van der Bliek, A. M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-09-0525 · Cited by 209
“The small LGG-1 clusters in untreated cells were replaced by much larger clusters (Figure 2, A and B).”
BackgroundInfluentialMitochondrial Dynamics in Cardiovascular Health and Disease
Ong, S., Hall, A. R., & Hausenloy, D. J. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4777 · Cited by 213
“A number of additional mitochondrial fission proteins have recently been discovered including, amongst others, mitochondrial fission factor (MFF) (34, 77) and mitochondrial dynamics proteins of 49 and 51 kDa (MiD49/51) (78, 111).”
InfluentialMitochondrial division and fusion in metabolism
Roy, M., Reddy, P. H., Iijima, M., & Sesaki, H. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.02.001 · Cited by 215
Mitochondrial Dynamics in Stem Cells and Differentiation
Seo, B. J., Yoon, S. H., & Tae, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123893 · Cited by 208
“MIEF1/2 form foci and rings around mitochondria and directly recruit cytosolic Drp1 to the mitochondrial outer membrane surface [59], serving as adaptors linking Drp1 and Mff [58].”
BackgroundCoincident Phosphatidic Acid Interaction Restrains Drp1 in Mitochondrial Division
Adachi, Y., Itoh, K., Yamada, T., Cerveny, K. L., Suzuki, T. L., Macdonald, P. J., Frohman, M. A., Ramachandran, R., Iijima, M., & Sesaki, H. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.013 · Cited by 206
“Therefore, FCCP-induced mitochondrial fragmentation has been used extensively to assess mitochondrial division in previous studies (Li et al., 2015; Palmer et al., 2011).”
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197
Altered brain energetics induces mitochondrial fission arrest in Alzheimer’s Disease
Zhang, L., Trushin, S., Christensen, T. A., Bachmeier, B. V., Gateno, B., Schroeder, A., Yao, J., Itoh, K., Sesaki, H., Poon, W. W., et al. (2016) · Scientific Reports · doi:10.1038/srep18725 · Cited by 201
Mitochondrial dynamics and viral infections: A close nexus
Khan, M. A., Syed, G. H., Kim, S., & Siddiqui, A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.040 · Cited by 195
“Once recruited to the mitochondria, Drp1 oligomerizes as rings on mitochondrial tubules and causes scission of both outer and inner mitochondrial membranes [40, 41] .”
BackgroundInterchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
Koirala, S., Guo, Q., Kalia, R., Bui, H., Eckert, D. M., Frost, A. S., & Shaw, J. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300855110 · Cited by 201
“This aggregated mitochondrial phenotype also was observed when MiD49 and MiD51 were overexpressed in mammalian cells (24).”
BackgroundInfluentialHearts deficient in both Mfn1 and Mfn2 are protected against acute myocardial infarction
Hall, A. R., Burke, N., Dongworth, R. K., Kalkhoran, S. B., Dyson, A., Vicencio, J. M., Dorn, G. W., Yellon, D. M., & Hausenloy, D. J. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.139 · Cited by 197
“mitochondrial fission by interacting with human fission protein (hFis1),(13) mitochondrial fission factor (MFF),(14) and mitochondrial dynamics proteins of 49 and 51 kDa (MiD49/MiD51).(15)”
BackgroundFission and proliferation of peroxisomes
Schrader, M., Bonekamp, N. A., & Islinger, M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.014 · Cited by 189
Dysregulated Mitochondrial Dynamics and Metabolism in Obesity, Diabetes, and Cancer
Dai, W., & Jiang, L. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00570 · Cited by 186
“reported that a double knockdown of MiD49 and MiD51 leads to mitochondrial elongation and reduces recruitment of Drp1 to mitochondria (37).”
BackgroundZerihun, M., Sukumaran, S., & Qvit, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065785 · Cited by 198
The ever-growing complexity of the mitochondrial fission machinery
Pagliuso, A., Cossart, P., & Stavru, F. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2603-0 · Cited by 192
“As in the case of Mff [123], the interaction between Drp1 and MiDs also appears to be transient, requiring chemical crosslinking for its detection [124].”
BackgroundResultThe mitochondrial fission receptor Mff selectively recruits oligomerized Drp1
Liu, R., & Chan, D. C. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-08-0591 · Cited by 193
“Four receptors have been identified that recruit Drp1 to mitochondria: mitochondrial fission 1 protein (Fis1), mitochondrial fission factor (Mff), and mitochondrial dynamics proteins of 49 and 51 kDa (MiD49 and MiD51, respectively; Yoon et al., 2003; Gandre-Babbe and van der Bliek, 2008; Palmer et al., 2011; Zhao et a…”
InfluentialMitochondrial fission and fusion
Lee, H., & Yoon, Y. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160129 · Cited by 183
Neurodegeneration as a consequence of failed mitochondrial maintenance
Karbowski, M., & Neutzner, A. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0921-0 · Cited by 187
“While the mitochondrial fusion proteins are membrane-bound, Drp1 is cytosolic and its mitochondrial association and activity in mammalian cells depends on various accessory proteins [54, 70, 98, 101].”
BackgroundMitochondrial Fission in Human Diseases
Serasinghe, M. N., & Chipuk, J. E. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_38 · Cited by 186
“Several such receptor proteins have been described, including mitochondrial fission 1 (Fis1), mitochondrial fission factor (Mff), Mid 49/51 (MIEF1/2), and gangliosideinduced differentiation-associated protein 1 (GDAP) (Gandre-Babbe and van der Bliek 2008; Niemann et al. 2005; Palmer et al. 2011; Serasinghe and Yoon 20…”
InfluentialAt the right distance: ER-mitochondria juxtaposition in cell life and death
Naon, D., & Scorrano, L. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.05.011 · Cited by 178
“Other partners driving the localization of DRP1 to mitochondria include mitochondrial fission factor (MFF) and mitochondrial division (MiD) 49 and 51.”
InfluentialIs Mitochondrial Dysfunction a Common Root of Noncommunicable Chronic Diseases?
Díaz‐Vegas, A., Sánchez-Aguilera, P., Krycer, J. R., Morales, P. E., Monsalves‐Álvarez, M., Cifuentes, M., Rothermel, B. A., & Lavandero, S. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa005 · Cited by 179
Regulation of Mammalian Mitochondrial Dynamics: Opportunities and Challenges
Yu, R., Lendahl, U., Nistér, M., & Zhao, J. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00374 · Cited by 183
“It has been reported that the MOM-anchored protein FUNDC1 drives hypoxia-induced mitophagy through interacting with the key autophagy factor LC3 in mammals (236).”
BackgroundInfluentialSpecific Interaction with Cardiolipin Triggers Functional Activation of Dynamin-Related Protein 1
Bustillo-Zabalbeitia, I., Montessuit, S., Raemy, E., Basañez, G., Terrones, O., & Martinou, J.-C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102738 · Cited by 162
“Two prominent examples are the mitochondrial fission factor (Mff) and the mitochondrial dynamics proteins of 51 (MiD51 or MIEF1) and 49 kDa (MiD49 or MIEF2), which have been implicated both in Drp1 mitochondrial recruitment and in stimulation of mitochondrial fission [34–36].”
BackgroundMechanical force induces mitochondrial fission
Helle, S. C. J., Feng, Q., Aebersold, M. J., Hirt, L., Grüter, R. R., Vahid, A., Sirianni, A., Mostowy, S., Snedeker, J. G., Šarić, A., et al. (2017) · eLife · doi:10.7554/elife.30292 · Cited by 171
“DRP1 is a cytosolic protein, and is recruited to mitochondria by integral mitochondrial membrane adaptor molecules such as mitochondrial fission factor (MFF) (Gandre-Babbe and van der Bliek, 2008) and mitochondrial dynamic protein of 49/51 kDa (Mid49/51) (Palmer et al., 2011; Zhao et al., 2011).”
BackgroundWhy size matters – balancing mitochondrial dynamics in Alzheimer's disease
DuBoff, B., Feany, M. Β., & Götz, J. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.03.002 · Cited by 168
Chen, K., Dasgupta, A., Lin, J.-H., Potus, F., Bonnet, S., Iremonger, J., Fu, J. M., Mewburn, J. D., Wu, D., Dunham‐Snary, K. J., et al. (2018) · Circulation · doi:10.1161/circulationaha.117.031258 · Cited by 167
Xian, H., & Liou, Y. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00657-z · Cited by 177
A dimeric equilibrium intermediate nucleates Drp1 reassembly on mitochondrial membranes for fission
Macdonald, P. J., Stepanyants, N., Mehrotra, N., Mears, J. A., Qi, X., Sesaki, H., & Ramachandran, R. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-02-0728 · Cited by 169
Functional interplay between Parkin and Drp1 in mitochondrial fission and clearance
Buhlman, L. M., Damiano, M. G., Bertolin, G., Ferrando-Miguel, R., Lombès, A., Brice, A., & Corti, O. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.05.012 · Cited by 173
Onoue, K., Jofuku, A., Ban-Ishihara, R., Ishihara, T., Maeda, M., Koshiba, T., Itoh, T., Fukuda, M., Otera, H., Oka, T., et al. (2012) · Journal of Cell Science · doi:10.1242/jcs.111211 · Cited by 161
“Mammalian Drp1 recruitment requires the outer membrane proteins mitochondrial fission factor (Mff), mitochondrial dynamics (MiD)51/mitochondrial elongation factor (MIEF)1 and MiD49 (Gandre-Babbe and van der Bliek, 2008; Otera et al., 2010; Palmer et al., 2011; Zhao et al., 2011).”
BackgroundMitochondrial dynamics and mitophagy in lung disorders
Sharma, A. K., Ahmad, S., Ahmad, T., Ali, S., & Syed, M. A. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119876 · Cited by 161
Proliferation and fission of peroxisomes — An update
Schrader, M., Costello, J. L., Godinho, L. F., Azadi, A. S., & Islinger, M. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.09.024 · Cited by 170
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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