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Journal articles on the topic 'Mitofusins'

Author: Grafiati

Published: 22 June 2024

Last updated: 31 July 2025

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1

Cohen, Mickael M., and David Tareste. "Recent insights into the structure and function of Mitofusins in mitochondrial fusion." F1000Research 7 (December 28, 2018): 1983. http://dx.doi.org/10.12688/f1000research.16629.1.

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Mitochondria undergo frequent fusion and fission events to adapt their morphology to cellular needs. Homotypic docking and fusion of outer mitochondrial membranes are controlled by Mitofusins, a set of large membrane-anchored GTPase proteins belonging to the dynamin superfamily. Mitofusins include, in addition to their GTPase and transmembrane domains, two heptad repeat domains, HR1 and HR2. All four regions are crucial for Mitofusin function, but their precise contribution to mitochondrial docking and fusion events has remained elusive until very recently. In this commentary, we first give an

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2

Wolf, Christina, Víctor López del Amo, Sabine Arndt, et al. "Redox Modifications of Proteins of the Mitochondrial Fusion and Fission Machinery." Cells 9, no. 4 (2020): 815. http://dx.doi.org/10.3390/cells9040815.

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Mitochondrial fusion and fission tailors the mitochondrial shape to changes in cellular homeostasis. Players of this process are the mitofusins, which regulate fusion of the outer mitochondrial membrane, and the fission protein DRP1. Upon specific stimuli, DRP1 translocates to the mitochondria, where it interacts with its receptors FIS1, MFF, and MID49/51. Another fission factor of clinical relevance is GDAP1. Here, we identify and discuss cysteine residues of these proteins that are conserved in phylogenetically distant organisms and which represent potential sites of posttranslational redox

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3

Anton, Vincent, and Mafalda Escobar-Henriques. "Stressresistenz durch Adaption der mitochondrialen Form." BIOspektrum 30, no. 4 (2024): 418–21. http://dx.doi.org/10.1007/s12268-024-2242-6.

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AbstractMitochondria are dynamic cellular compartments that can remodel their own shape and activity. They sense and convert cellular signals into informative triggers, allowing the cell to adapt to its ever-changing needs. We discovered that under stress this adaptation is performed by the E4 enzyme Ufd2/UBE4B, which tags mitochondrial fusion factors called mitofusins, thus signalling their degradation. Our findings highlight therapeutic intervention cues for mitofusin-associated diseases.

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4

LeBrasseur, Nicole. "Pro-diversity mitofusins." Journal of Cell Biology 176, no. 4 (2007): 373a. http://dx.doi.org/10.1083/jcb.1764iti3.

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5

Schiavon, Cara R., Rachel E. Turn, Laura E. Newman, and Richard A. Kahn. "ELMOD2 regulates mitochondrial fusion in a mitofusin-dependent manner, downstream of ARL2." Molecular Biology of the Cell 30, no. 10 (2019): 1198–213. http://dx.doi.org/10.1091/mbc.e18-12-0804.

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Mitochondria are essential and dynamic organelles undergoing constant fission and fusion. The primary players in mitochondrial morphology (MFN1/2, OPA1, DRP1) have been identified, but their mechanism(s) of regulation are still being elucidated. ARL2 is a regulatory GTPase that has previously been shown to play a role in the regulation of mitochondrial morphology. Here we demonstrate that ELMOD2, an ARL2 GTPase-activating protein (GAP), is necessary for ARL2 to promote mitochondrial elongation. We show that loss of ELMOD2 causes mitochondrial fragmentation and a lower rate of mitochondrial fus

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6

Koch, Linda. "Mitofusins and energy balance." Nature Reviews Endocrinology 9, no. 12 (2013): 691. http://dx.doi.org/10.1038/nrendo.2013.202.

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7

Escobar-Henriques, Mafalda. "Mitofusins: ubiquitylation promotes fusion." Cell Research 24, no. 4 (2014): 387–88. http://dx.doi.org/10.1038/cr.2014.23.

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8

Miao, Junru, Wei Chen, Pengxiang Wang, et al. "MFN1 and MFN2 Are Dispensable for Sperm Development and Functions in Mice." International Journal of Molecular Sciences 22, no. 24 (2021): 13507. http://dx.doi.org/10.3390/ijms222413507.

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MFN1 (Mitofusin 1) and MFN2 (Mitofusin 2) are GTPases essential for mitochondrial fusion. Published studies revealed crucial roles of both Mitofusins during embryonic development. Despite the unique mitochondrial organization in sperm flagella, the biological requirement in sperm development and functions remain undefined. Here, using sperm-specific Cre drivers, we show that either Mfn1 or Mfn2 knockout in haploid germ cells does not affect male fertility. The Mfn1 and Mfn2 double knockout mice were further analyzed. We found no differences in testis morphology and weight between Mfn-deficient

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9

Sloat, S. R., B. N. Whitley, E. A. Engelhart, and S. Hoppins. "Identification of a mitofusin specificity region that confers unique activities to Mfn1 and Mfn2." Molecular Biology of the Cell 30, no. 17 (2019): 2309–19. http://dx.doi.org/10.1091/mbc.e19-05-0291.

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Mitochondrial structure can be maintained at steady state or modified in response to changes in cellular physiology. This is achieved by the coordinated regulation of dynamic properties including mitochondrial fusion, division, and transport. Disease states, including neurodegeneration, are associated with defects in these processes. In vertebrates, two mitofusin paralogues, Mfn1 and Mfn2, are required for efficient mitochondrial fusion. The mitofusins share a high degree of homology and have very similar domain architecture, including an amino terminal GTPase domain and two extended helical b

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10

Alsayyah, Cynthia, Manish K. Singh, Maria Angeles Morcillo-Parra, et al. "Mitofusin-mediated contacts between mitochondria and peroxisomes regulate mitochondrial fusion." PLOS Biology 22, no. 4 (2024): e3002602. http://dx.doi.org/10.1371/journal.pbio.3002602.

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Mitofusins are large GTPases that trigger fusion of mitochondrial outer membranes. Similarly to the human mitofusin Mfn2, which also tethers mitochondria to the endoplasmic reticulum (ER), the yeast mitofusin Fzo1 stimulates contacts between Peroxisomes and Mitochondria when overexpressed. Yet, the physiological significance and function of these “PerMit” contacts remain unknown. Here, we demonstrate that Fzo1 naturally localizes to peroxisomes and promotes PerMit contacts in physiological conditions. These contacts are regulated through co-modulation of Fzo1 levels by the ubiquitin–proteasome

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11

R. Khalil, Rana, Mufeda AL-Ammar, and Hayder A. L. Mossa. "Mitofusin 1 as Marker of Oocyte Maturation in Relevance to ICSI Outcome in Infertile Females." IraQi Journal of Embryos and Infertility Researches 13, no. 2 (2023): 39–50. http://dx.doi.org/10.28969/ijeir.v13.i2.r4.23.

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Pro-fusion proteins as mitofusins-1 are required for controlling mitochondrial shape which determined by a dynamic balance between organelle fusion and fission and also supports oocyte development. When compare with somatic cell, mitochondria of oocyte are tiny and circular in presence. The aim is to study the mitofusin-1 in the follicular fluid as a marker for evaluating of oocyte maturation in women undergoing ICSI cycles. Fifty infertile females were included in cross-section study was undergoing ICSI procedure with age 20 to 42 years. After retrieval of oocyte and the number of oocytes was

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12

Brooks, Craig, Sung-Gyu Cho, Cong-Yi Wang, Tianxin Yang, and Zheng Dong. "Fragmented mitochondria are sensitized to Bax insertion and activation during apoptosis." American Journal of Physiology-Cell Physiology 300, no. 3 (2011): C447—C455. http://dx.doi.org/10.1152/ajpcell.00402.2010.

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Recent studies have shown mitochondrial fragmentation during cell stress and have suggested a role for the morphological change in mitochondrial injury and ensuing apoptosis. However, the underlying mechanism remains elusive. Here we demonstrate that mitochondrial fragmentation facilitates Bax insertion and activation in mitochondria, resulting in the release of apoptogenic factors. In HeLa cells, overexpression of mitofusins attenuated mitochondrial fragmentation during cisplatin- and azide-induced cell injury, which was accompanied by less apoptosis and less cytochrome c release from mitocho

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13

Schrepfer, Emilie, and Luca Scorrano. "Mitofusins, from Mitochondria to Metabolism." Molecular Cell 61, no. 5 (2016): 683–94. http://dx.doi.org/10.1016/j.molcel.2016.02.022.

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14

Ozcan, Umut. "Mitofusins: Mighty Regulators of Metabolism." Cell 155, no. 1 (2013): 17–18. http://dx.doi.org/10.1016/j.cell.2013.09.013.

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15

Giacomello, Marta, and Luca Scorrano. "The INs and OUTs of mitofusins." Journal of Cell Biology 217, no. 2 (2018): 439–40. http://dx.doi.org/10.1083/jcb.201801042.

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Mitofusins are outer membrane proteins essential for mitochondrial fusion. Their accepted topology posits that both N and C termini face the cytoplasm. In this issue, Mattie et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201611194) demonstrate instead that their C termini reside in the intermembrane space. These findings call for a revision of the current models of mitochondrial fusion.

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16

Dorn, Gerald W. "Mitofusins as mitochondrial anchors and tethers." Journal of Molecular and Cellular Cardiology 142 (May 2020): 146–53. http://dx.doi.org/10.1016/j.yjmcc.2020.04.016.

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17

Parekh, Anant. "Calcium Signalling: Mitofusins Promote Interorganellar Crosstalk." Current Biology 19, no. 5 (2009): R200—R203. http://dx.doi.org/10.1016/j.cub.2009.01.012.

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18

Engelhart, Emily A., and Suzanne Hoppins. "A catalytic domain variant of mitofusin requiring a wildtype paralog for function uncouples mitochondrial outer-membrane tethering and fusion." Journal of Biological Chemistry 294, no. 20 (2019): 8001–14. http://dx.doi.org/10.1074/jbc.ra118.006347.

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Mitofusins (Mfns) are dynamin-related GTPases that mediate mitochondrial outer-membrane fusion, a process that is required for mitochondrial and cellular health. In Mfn1 and Mfn2 paralogs, a conserved phenylalanine (Phe-202 (Mfn1) and Phe-223 (Mfn2)) located in the GTPase domain on a conserved β strand is part of an aromatic network in the core of this domain. To gain insight into the poorly understood mechanism of Mfn-mediated membrane fusion, here we characterize a Mitofusin mutant variant etiologically linked to Charcot–Marie–Tooth syndrome. From analysis of mitochondrial structure in cells

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19

Anton, Vincent, Ira Buntenbroich, Ramona Schuster, et al. "Plasticity in salt bridge allows fusion-competent ubiquitylation of mitofusins and Cdc48 recognition." Life Science Alliance 2, no. 6 (2019): e201900491. http://dx.doi.org/10.26508/lsa.201900491.

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Mitofusins are dynamin-related GTPases that drive mitochondrial fusion by sequential events of oligomerization and GTP hydrolysis, followed by their ubiquitylation. Here, we show that fusion requires a trilateral salt bridge at a hinge point of the yeast mitofusin Fzo1, alternatingly forming before and after GTP hydrolysis. Mutations causative of Charcot–Marie–Tooth disease massively map to this hinge point site, underlining the disease relevance of the trilateral salt bridge. A triple charge swap rescues the activity of Fzo1, emphasizing the close coordination of the hinge residues with GTP h

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20

Song, Zhiyin, Mariam Ghochani, J. Michael McCaffery, Terrence G. Frey, and David C. Chan. "Mitofusins and OPA1 Mediate Sequential Steps in Mitochondrial Membrane Fusion." Molecular Biology of the Cell 20, no. 15 (2009): 3525–32. http://dx.doi.org/10.1091/mbc.e09-03-0252.

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Mitochondrial fusion requires the coordinated fusion of the outer and inner membranes. Three large GTPases—OPA1 and the mitofusins Mfn1 and Mfn2—are essential for the fusion of mammalian mitochondria. OPA1 is mutated in dominant optic atrophy, a neurodegenerative disease of the optic nerve. In yeast, the OPA1 ortholog Mgm1 is required for inner membrane fusion in vitro; nevertheless, yeast lacking Mgm1 show neither outer nor inner membrane fusion in vivo, because of the tight coupling between these two processes. We find that outer membrane fusion can be readily visualized in OPA1-null mouse c

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21

Mattie, Sevan, Jan Riemer, Jeremy G. Wideman, and Heidi M. McBride. "A new mitofusin topology places the redox-regulated C terminus in the mitochondrial intermembrane space." Journal of Cell Biology 217, no. 2 (2017): 507–15. http://dx.doi.org/10.1083/jcb.201611194.

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Mitochondrial fusion occurs in many eukaryotes, including animals, plants, and fungi. It is essential for cellular homeostasis, and yet the underlying mechanisms remain elusive. Comparative analyses and phylogenetic reconstructions revealed that fungal Fzo1 and animal Mitofusin proteins are highly diverged from one another and lack strong sequence similarity. Bioinformatic analysis showed that fungal Fzo1 proteins exhibit two predicted transmembrane domains, whereas metazoan Mitofusins contain only a single transmembrane domain. This prediction contradicts the current models, suggesting that b

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22

De Vecchis, Dario, Antoine Taly, Marc Baaden, and Jérôme Hénin. "Mitochondrial Membrane Fusion: Computational Modeling of Mitofusins." Biophysical Journal 110, no. 3 (2016): 571a. http://dx.doi.org/10.1016/j.bpj.2015.11.3054.

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23

Schuster, Ramona, Vincent Anton, Tânia Simões, et al. "Dual role of a GTPase conformational switch for membrane fusion by mitofusin ubiquitylation." Life Science Alliance 3, no. 1 (2019): e201900476. http://dx.doi.org/10.26508/lsa.201900476.

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Mitochondria are essential organelles whose function is upheld by their dynamic nature. This plasticity is mediated by large dynamin-related GTPases, called mitofusins in the case of fusion between two mitochondrial outer membranes. Fusion requires ubiquitylation, attached to K398 in the yeast mitofusin Fzo1, occurring in atypical and conserved forms. Here, modelling located ubiquitylation to α4 of the GTPase domain, a critical helix in Ras-mediated events. Structure-driven analysis revealed a dual role of K398. First, it is required for GTP-dependent dynamic changes of α4. Indeed, mutations d

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24

Papanicolaou, Kyriakos N., Matthew M. Phillippo, and Kenneth Walsh. "Mitofusins and the mitochondrial permeability transition: the potential downside of mitochondrial fusion." American Journal of Physiology-Heart and Circulatory Physiology 303, no. 3 (2012): H243—H255. http://dx.doi.org/10.1152/ajpheart.00185.2012.

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Mitofusins (Mfn-1 and Mfn-2) are transmembrane proteins that bind and hydrolyze guanosine 5′-triphosphate to bring about the merging of adjacent mitochondrial membranes. This event is necessary for mitochondrial fusion, a biological process that is critical for organelle function. The broad effects of mitochondrial fusion on cell bioenergetics have been extensively studied, whereas the local effects of mitofusin activity on the structure and integrity of the fusing mitochondrial membranes have received relatively little attention. From the study of fusogenic proteins, theoretical models, and s

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25

Son, M. J., Y. Kwon, M.-Y. Son, et al. "Mitofusins deficiency elicits mitochondrial metabolic reprogramming to pluripotency." Cell Death & Differentiation 22, no. 12 (2015): 1957–69. http://dx.doi.org/10.1038/cdd.2015.43.

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26

Yu, Chia-Yi, Jian-Jong Liang, Jin-Kun Li, et al. "Dengue Virus Impairs Mitochondrial Fusion by Cleaving Mitofusins." PLOS Pathogens 11, no. 12 (2015): e1005350. http://dx.doi.org/10.1371/journal.ppat.1005350.

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27

Mourier, Arnaud, Elisa Motori, Eduardo Silva Ramos, et al. "Role of Mitofusins proteins in maintaining OXPHOS function." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1857 (August 2016): e15. http://dx.doi.org/10.1016/j.bbabio.2016.04.386.

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28

Santel, A., and M. T. Fuller. "Control of mitochondrial morphology by a human mitofusin." Journal of Cell Science 114, no. 5 (2001): 867–74. http://dx.doi.org/10.1242/jcs.114.5.867.

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Although changes in mitochondrial size and arrangement accompany both cellular differentiation and human disease, the mechanisms that mediate mitochondrial fusion, fission and morphogenesis in mammalian cells are not understood. We have identified two human genes encoding potential mediators of mitochondrial fusion. The mitofusins (Mfn1 and Mfn2) are homologs of the Drosophila protein fuzzy onion (Fzo) that associate with mitochondria and alter mitochondrial morphology when expressed by transient transfection in tissue culture cells. An internal region including a predicted bipartite transmemb

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29

Tanaka, Atsushi, Megan M. Cleland, Shan Xu, et al. "Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin." Journal of Cell Biology 191, no. 7 (2010): 1367–80. http://dx.doi.org/10.1083/jcb.201007013.

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Damage to mitochondria can lead to the depolarization of the inner mitochondrial membrane, thereby sensitizing impaired mitochondria for selective elimination by autophagy. However, fusion of uncoupled mitochondria with polarized mitochondria can compensate for damage, reverse membrane depolarization, and obviate mitophagy. Parkin, an E3 ubiquitin ligase that is mutated in monogenic forms of Parkinson’s disease, was recently found to induce selective autophagy of damaged mitochondria. Here we show that ubiquitination of mitofusins Mfn1 and Mfn2, large GTPases that mediate mitochondrial fusion,

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30

Samanas, Nyssa B., Emily A. Engelhart, and Suzanne Hoppins. "Defective nucleotide-dependent assembly and membrane fusion in Mfn2 CMT2A variants improved by Bax." Life Science Alliance 3, no. 5 (2020): e201900527. http://dx.doi.org/10.26508/lsa.201900527.

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Mitofusins are members of the dynamin-related protein family of large GTPases that harness the energy from nucleotide hydrolysis to remodel membranes. Mitofusins possess four structural domains, including a GTPase domain, two extended helical bundles (HB1 and HB2), and a transmembrane region. We have characterized four Charcot-Marie-Tooth type 2A–associated variants with amino acid substitutions in Mfn2 that are proximal to the hinge that connects HB1 and HB2. A functional defect was not apparent in cells as the mitochondrial morphology of Mfn2-null cells was restored by expression of any of t

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31

Pellattiero, Anna, and Luca Scorrano. "Flaming Mitochondria: The Anti-inflammatory Drug Leflunomide Boosts Mitofusins." Cell Chemical Biology 25, no. 3 (2018): 231–33. http://dx.doi.org/10.1016/j.chembiol.2018.02.014.

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32

Zhang, Lihong, Xiawei Dang, Antonietta Franco, Haiyang Zhao, and Gerald W. Dorn. "Piperine Derivatives Enhance Fusion and Axonal Transport of Mitochondria by Activating Mitofusins." Chemistry 4, no. 3 (2022): 655–68. http://dx.doi.org/10.3390/chemistry4030047.

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Piperine (1-piperoylpiperidine) is the major pungent component of black pepper (Piper nigrum) and exhibits a spectrum of pharmacological activities. The molecular bases for many of piperine’s biological effects are incompletely defined. We noted that the chemical structure of piperine generally conforms to a pharmacophore model for small bioactive molecules that activate mitofusin (MFN)-mediated mitochondrial fusion. Piperine, but not its isomer chavicine, stimulated mitochondrial fusion in MFN-deficient cells with EC50 of ~8 nM. We synthesized piperine analogs having structural features predi

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33

Ryan, Michael T., and Diana Stojanovski. "Mitofusins ‘bridge’ the gap between oxidative stress and mitochondrial hyperfusion." EMBO reports 13, no. 10 (2012): 870–71. http://dx.doi.org/10.1038/embor.2012.132.

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34

Daumke, Oliver, and Aurélien Roux. "Mitochondrial Homeostasis: How Do Dimers of Mitofusins Mediate Mitochondrial Fusion?" Current Biology 27, no. 9 (2017): R353—R356. http://dx.doi.org/10.1016/j.cub.2017.03.024.

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35

Santel, Ansgar. "Get the balance right: Mitofusins roles in health and disease." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1763, no. 5-6 (2006): 490–99. http://dx.doi.org/10.1016/j.bbamcr.2006.02.004.

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36

Ding, Wen-Xing, Fengli Guo, Hong-Min Ni, et al. "Parkin and Mitofusins Reciprocally Regulate Mitophagy and Mitochondrial Spheroid Formation." Journal of Biological Chemistry 287, no. 50 (2012): 42379–88. http://dx.doi.org/10.1074/jbc.m112.413682.

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37

Vlieghe, Anaïs, Kristina Niort, Hugo Fumat, Jean-Michel Guigner, Mickaël M. Cohen, and David Tareste. "Role of Lipids and Divalent Cations in Membrane Fusion Mediated by the Heptad Repeat Domain 1 of Mitofusin." Biomolecules 13, no. 9 (2023): 1341. http://dx.doi.org/10.3390/biom13091341.

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Mitochondria are highly dynamic organelles that constantly undergo fusion and fission events to maintain their shape, distribution and cellular function. Mitofusin 1 and 2 proteins are two dynamin-like GTPases involved in the fusion of outer mitochondrial membranes (OMM). Mitofusins are anchored to the OMM through their transmembrane domain and possess two heptad repeat domains (HR1 and HR2) in addition to their N-terminal GTPase domain. The HR1 domain was found to induce fusion via its amphipathic helix, which interacts with the lipid bilayer structure. The lipid composition of mitochondrial

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38

Ugarte-Uribe, Begoña, and Ana J. García-Sáez. "Membranes in motion: mitochondrial dynamics and their role in apoptosis." Biological Chemistry 395, no. 3 (2014): 297–311. http://dx.doi.org/10.1515/hsz-2013-0234.

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Abstract Mitochondrial dynamics is crucial for cell survival, development and homeostasis and impairment of these functions leads to neurologic disorders and metabolic diseases. The key components of mitochondrial dynamics have been identified. Mitofusins and OPA1 mediate mitochondrial fusion, whereas Drp1 is responsible for mitochondrial fission. In addition, an interplay between the proteins of the mitochondrial fission/fusion machinery and the Bcl-2 proteins, essential mediators in apoptosis, has been also described. Here, we review the molecular mechanisms regarding mitochondrial dynamics

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39

Papanicolaou, Kyriakos N., Ryosuke Kikuchi, Gladys A. Ngoh, et al. "Mitofusins 1 and 2 Are Essential for Postnatal Metabolic Remodeling in Heart." Circulation Research 111, no. 8 (2012): 1012–26. http://dx.doi.org/10.1161/circresaha.112.274142.

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40

Rakovic, Aleksandar, Anne Grünewald, Jan Kottwitz, et al. "Mutations in PINK1 and Parkin Impair Ubiquitination of Mitofusins in Human Fibroblasts." PLoS ONE 6, no. 3 (2011): e16746. http://dx.doi.org/10.1371/journal.pone.0016746.

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41

Brooks, C., Q. Wei, L. Feng, et al. "Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins." Proceedings of the National Academy of Sciences 104, no. 28 (2007): 11649–54. http://dx.doi.org/10.1073/pnas.0703976104.

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42

Du, Mengyan, Si Yu, Wenhua Su, et al. "Mitofusin 2 but not mitofusin 1 mediates Bcl-XL-induced mitochondrial aggregation." Journal of Cell Science 133, no. 20 (2020): jcs245001. http://dx.doi.org/10.1242/jcs.245001.

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ABSTRACTBcl-2 family proteins, as central players of the apoptotic program, participate in regulation of the mitochondrial network. Here, a quantitative live-cell fluorescence resonance energy transfer (FRET) two-hybrid assay was used to confirm the homo-/hetero-oligomerization of mitofusins 2 and 1 (MFN2 and MFN1), and also demonstrate the binding of MFN2 to MFN1 with 1:1 stoichiometry. A FRET two-hybrid assay for living cells co-expressing CFP-labeled Bcl-XL (an anti-apoptotic Bcl-2 family protein encoded by BCL2L1) and YFP-labeled MFN2 or MFN1 demonstrated the binding of MFN2 or MFN1 to Bcl

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43

Wiedemann, Nils, Sebastian B. Stiller, and Nikolaus Pfanner. "Activation and Degradation of Mitofusins: Two Pathways Regulate Mitochondrial Fusion by Reversible Ubiquitylation." Molecular Cell 49, no. 3 (2013): 423–25. http://dx.doi.org/10.1016/j.molcel.2013.01.027.

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44

Yin, Xiao-Ming, and Wen-Xing Ding. "The reciprocal roles of PARK2 and mitofusins in mitophagy and mitochondrial spheroid formation." Autophagy 9, no. 11 (2013): 1687–92. http://dx.doi.org/10.4161/auto.24871.

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45

Dietrich, Marcelo O., Zhong-Wu Liu, and Tamas L. Horvath. "Mitochondrial Dynamics Controlled by Mitofusins Regulate Agrp Neuronal Activity and Diet-Induced Obesity." Cell 155, no. 1 (2013): 188–99. http://dx.doi.org/10.1016/j.cell.2013.09.004.

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46

Lee, Crystal A., Lih-Shen Chin, and Lian Li. "Hypertonia-linked protein Trak1 functions with mitofusins to promote mitochondrial tethering and fusion." Protein & Cell 9, no. 8 (2017): 693–716. http://dx.doi.org/10.1007/s13238-017-0469-4.

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47

Bhatia, Divya, Eleni Kallinos, Edwin Patino, Maria Plataki, Augustine M. Choi, and Mary E. Choi. "Alveolar Type II Cell-Specific Mitofusins Modulate Kidney Fibrosis and Associated Lung Injury." Journal of the American Society of Nephrology 34, no. 11S (2023): 701. http://dx.doi.org/10.1681/asn.20233411s1701b.

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48

Wakai, Takuya, Yuichirou Harada, Kenji Miyado, and Tomohiro Kono. "Mitochondrial dynamics controlled by mitofusins define organelle positioning and movement during mouse oocyte maturation." MHR: Basic science of reproductive medicine 20, no. 11 (2014): 1090–100. http://dx.doi.org/10.1093/molehr/gau064.

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49

Chen, Hsiuchen, Scott A. Detmer, Andrew J. Ewald, Erik E. Griffin, Scott E. Fraser, and David C. Chan. "Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development." Journal of Cell Biology 160, no. 2 (2003): 189–200. http://dx.doi.org/10.1083/jcb.200211046.

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Mitochondrial morphology is determined by a dynamic equilibrium between organelle fusion and fission, but the significance of these processes in vertebrates is unknown. The mitofusins, Mfn1 and Mfn2, have been shown to affect mitochondrial morphology when overexpressed. We find that mice deficient in either Mfn1 or Mfn2 die in midgestation. However, whereas Mfn2 mutant embryos have a specific and severe disruption of the placental trophoblast giant cell layer, Mfn1-deficient giant cells are normal. Embryonic fibroblasts lacking Mfn1 or Mfn2 display distinct types of fragmented mitochondria, a

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Wu, Zhaofei, Yushan Zhu, Xingshui Cao, Shufeng Sun та Baolu Zhao. "Mitochondrial Toxic Effects of Aβ Through Mitofusins in the Early Pathogenesis of Alzheimer’s Disease". Molecular Neurobiology 50, № 3 (2014): 986–96. http://dx.doi.org/10.1007/s12035-014-8675-z.

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