MITOL Regulates Endoplasmic Reticulum-Mitochondria Contacts via Mitofusin2

Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development

Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works

Mitofusin 2 tethers endoplasmic reticulum to mitochondria

de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442 · see citing works

Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca ²⁺ Responses

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ER Tubules Mark Sites of Mitochondrial Division

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Sigma-1 Receptor Chaperones at the ER- Mitochondrion Interface Regulate Ca2+ Signaling and Cell Survival

Hayashi, T., & Su, T.-P. (2007) · Cell · doi:10.1016/j.cell.2007.08.036 · Cited by 1,826 · see citing works

Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A

Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572 · see citing works

Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels

Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413 · see citing works

Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin

Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369 · see citing works

An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen

Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275 · see citing works

Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling

Mukhopadhyay, D., & Riezman, H. (2007) · Science · doi:10.1126/science.1127085 · Cited by 1,221 · see citing works

Phospholipid synthesis in a membrane fraction associated with mitochondria.

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Polyubiquitin chains: polymeric protein signals

Pickart, C. M., & Fushman, D. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.09.009 · Cited by 1,052 · see citing works

Structural Basis of Mitochondrial Tethering by Mitofusin Complexes

Koshiba, T., Detmer, S. A., Kaiser, J. T., Chen, H., McCaffery, J. M., & Chan, D. C. (2004) · Science · doi:10.1126/science.1099793 · Cited by 910 · see citing works

Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy

Gegg, M. E., Cooper, J. M., Chau, K.-Y., Rojo, M., Schapira, A. H. V., & Taanman, J.-W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq419 · Cited by 910 · see citing works

Dynamics of mitochondria in living cells: Shape changes, dislocations, fusion, and fission of mitochondria

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Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity

Ishihara, N., Eura, Y., & Mihara, K. (2004) · Journal of Cell Science · doi:10.1242/jcs.01565 · Cited by 731 · see citing works

Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo

Rojo, M., Legros, F., Chateau, D., & Lombès, A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.8.1663 · Cited by 555 · see citing works

Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA.

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The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division

Karbowski, M., Neutzner, A., & Youle, R. J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611064 · Cited by 474 · see citing works

Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion

Eura, Y. (2003) · Journal of Biochemistry · doi:10.1093/jb/mvg150 · Cited by 445 · see citing works

MARCH‐V is a novel mitofusin 2‐ and Drp1‐binding protein able to change mitochondrial morphology

Nakamura, N., Kimura, Y. N., Tokuda, M., Honda, S., & Hirose, S. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400790 · Cited by 419 · see citing works

A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics

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Stress-Induced Phosphorylation and Proteasomal Degradation of Mitofusin 2 Facilitates Mitochondrial Fragmentation and Apoptosis

Leboucher, G. P., Tsai, Y. C., Yang, M., Shaw, K. C., Zhou, M., Veenstra, T. D., Glickman, M. H., & Weissman, A. M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.041 · Cited by 334 · see citing works

Bcl‐2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types.

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Presenilin 2 modulates endoplasmic reticulum (ER)–mitochondria interactions and Ca 2+ cross-talk

Zampese, E., Fasolato, C., Kipanyula, M. J., Bortolozzi, M., Pozzan, T., & Pizzo, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100735108 · Cited by 285 · see citing works

Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1

Park, Y.-Y., Lee, S., Karbowski, M., Neutzner, A., Youle, R. J., & Cho, H. (2010) · Journal of Cell Science · doi:10.1242/jcs.061481 · Cited by 244 · see citing works

The intracellular redox state is a core determinant of mitochondrial fusion

Shutt, T. E., Geoffrion, M., Milne, R. W., & McBride, H. M. (2012) · EMBO Reports · doi:10.1038/embor.2012.128 · Cited by 243 · see citing works

Mitofusin-2 regulates mitochondrial and endoplasmic reticulum morphology and tethering: The role of Ras

de Brito, O. M., & Scorrano, L. (2009) · Mitochondrion · doi:10.1016/j.mito.2009.02.005 · Cited by 153 · see citing works

Mitochondrial Ubiquitin Ligase MITOL Ubiquitinates Mutant SOD1 and Attenuates Mutant SOD1-induced Reactive Oxygen Species Generation

Yonashiro, R., Sugiura, A., Miyachi, M., Fukuda, T., Matsushita, N., Inatome, R., Ogata, Y., Suzuki, T., Dohmae, N., & Yanagi, S. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-02-0112 · Cited by 143 · see citing works

Control of Mitochondrial Morphology Through Differential Interactions of Mitochondrial Fusion and Fission Proteins

Huang, P., Galloway, C. A., & Yoon, Y. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020655 · Cited by 124 · see citing works

Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome-independent turnover of Fzo1

Escobar‐Henriques, M., Westermann, B., & Langer, T. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512079 · Cited by 119 · see citing works

Ugo1 and Mdm30 act sequentially during Fzo1-mediated mitochondrial outer membrane fusion

den Brave, F., Fres, J. M., Schauss, A. C., Pinson, B., Praefcke, G. J. K., Langer, T., & Escobar‐Henriques, M. (2011) · Journal of Cell Science · doi:10.1242/jcs.073080 · Cited by 92 · see citing works

Mitochondrial ubiquitin ligase MITOL blocks S-nitrosylated MAP1B-light chain 1-mediated mitochondrial dysfunction and neuronal cell death

Yonashiro, R., Kimijima, Y., Shimura, T., Kawaguchi, K., Fukuda, T., Inatome, R., & Yanagi, S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114985109 · Cited by 78 · see citing works

Sequential requirements for the GTPase domain of the mitofusin Fzo1 and the ubiquitin ligase SCFMdm30 in mitochondrial outer membrane fusion

Cohen, M. M., Amiott, E. A., Day, A. R., Leboucher, G. P., Pryce, E. N., Glickman, M. H., McCaffery, J. M., Shaw, J. M., & Weissman, A. M. (2011) · Journal of Cell Science · doi:10.1242/jcs.079293 · Cited by 76 · see citing works

A mitochondrial ubiquitin ligase MITOL controls cell toxicity of polyglutamine-expanded protein

Sugiura, A., Yonashiro, R., Fukuda, T., Matsushita, N., Nagashima, S., Inatome, R., & Yanagi, S. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.09.001 · Cited by 76 · see citing works

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 · see citing works

UPR, autophagy, and mitochondria crosstalk underlies the ER stress response

Senft, D., & Ronai, Z. A. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.01.002 · Cited by 1,121 · see citing works

Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions

Csordás, G., Weaver, D., & Hajnóczky, G. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.009 · Cited by 625 · see citing works

Critical reappraisal confirms that Mitofusin 2 is an endoplasmic reticulum–mitochondria tether

Naon, D., Zaninello, M., Giacomello, M., Varanita, T., Grespi, F., Lakshminaranayan, S., Serafini, A., Semenzato, M., Herkenne, S., Hernández-Alvarez, M. I., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606786113 · Cited by 521 · see citing works

Mitochondrial quality control and muscle mass maintenance.

Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434 · see citing works

The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass

Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works

Endoplasmic reticulum-mitochondria tethering in neurodegenerative diseases

Liu, Y., & Zhu, X. (2017) · Translational Neurodegeneration · doi:10.1186/s40035-017-0092-6 · Cited by 132 · see citing works

Mitochondrial ubiquitin ligase alleviates Alzheimer’s disease pathology via blocking the toxic amyloid-β oligomer generation

Takeda, K., Uda, A., Mitsubori, M., Nagashima, S., Iwasaki, H., Ito, N., Shiiba, I., Ishido, S., Matsuoka, M., Inatome, R., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-01720-2 · Cited by 32 · see citing works

Mitochondrial fusion and function in Charcot–Marie–Tooth type 2A patient fibroblasts with mitofusin 2 mutations

Amiott, E. A., Lott, P. C., Soto, J. E., Kang, P. B., McCaffery, J. M., DiMauro, S., Abel, E. D., Flanigan, K. M., Lawson, V. H., & Shaw, J. M. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.01.010 · Cited by 107 · see citing works

Physiological functions of mitochondrial fusion

Chen, H., & Chan, D. C. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05615.x · Cited by 221 · see citing works

Mitochondrial dynamics and neurodegeneration

Chan, D. C., Detmer, S. A., & Chen, H. (2007) · The FASEB Journal · doi:10.1096/fasebj.21.5.a96-b · Cited by 2 · see citing works

Mitofusin 2: A Mitochondria-Shaping Protein with Signaling Roles Beyond Fusion

de Brito, O. M., & Scorrano, L. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1934 · Cited by 152 · see citing works

Mitochondrial dynamics as a bridge between mitochondrial dysfunction and insulin resistance

Zorzano, A., Liesa, M., & Palacı́n, M. (2009) · Archives of Physiology and Biochemistry · doi:10.1080/13813450802676335 · Cited by 123 · see citing works