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Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission
Open accessAbstract
Mitochondrial morphology is controlled by two opposing processes: fusion and fission. Drp1 (dynamin-related protein 1) and hFis1 are two key players of mitochondrial fission, but how Drp1 is recruited to mitochondria and how Drp1-mediated mitochondrial fission is regulated in mammals is poorly understood. Here, we identify the vertebrate-specific protein MIEF1 (mitochondrial elongation factor 1; independently identified as MiD51), which is anchored to the outer mitochondrial membrane. Elevated MIEF1 levels induce extensive mitochondrial fusion, whereas depletion of MIEF1 causes mitochondrial fragmentation. MIEF1 interacts with and recruits Drp1 to mitochondria in a manner independent of hFis1, Mff (mitochondrial fission factor) and Mfn2 (mitofusin 2), but inhibits Drp1 activity, thus executing a negative effect on mitochondrial fission. MIEF1 also interacts with hFis1 and elevated hFis1 levels partially reverse the MIEF1-induced fusion phenotype. In addition to inhibiting Drp1, MIEF1 also actively promotes fusion, but in a manner distinct from mitofusins. In conclusion, our findings uncover a novel mechanism which controls the mitochondrial fusion-fission machinery in vertebrates. As MIEF1 is vertebrate-specific, these data also reveal important differences between yeast and vertebrates in the regulation of mitochondrial dynamics.
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“MIEF1/MiD51 and the variant MIEF2/MiD49 recruit DRP1 to mitochondria independent of MFF, but in contrast to MFF, inhibit DRP1 GTPase activity leading to mitochondrial elongation when MiD49/51 is overexpressed [92, 95, 96].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [95]
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Citations
Cites
Site-directed mutagenesis by overlap extension using the polymerase chain reaction
Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., & Pease, L. R. (1989) · Gene · doi:10.1016/0378-1119(89)90358-2 · Cited by 7,414
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
Dynamin-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
Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446
Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270
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
Mitochondria in neuroplasticity and neurological disorders
Mattson, M. P., Gleichmann, M., & Cheng, A. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.010 · Cited by 1,081
Ishihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S. O., Masuda, K., Otera, H., Nakanishi, Y., Nonaka, I., Goto, Y.-I., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1907 · Cited by 1,066
Cribbs, J. T., & Strack, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401062 · Cited by 1,061
Flagged first, then by citations
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Items 201–300 of 370
Yu, R., Liu, T., Jin, S., Ankarcrona, M., Lendahl, U., Nistér, M., & Zhao, J. (2021) · BMC Biology · doi:10.1186/s12915-021-01161-7 · Cited by 37
Self-citationChemical inhibition of mitochondrial fission via targeting the DRP1-receptor interaction
Yang, J., Chen, P., Cao, Y., Liu, S., Wang, W., Li, L., Li, J., Jiang, Z., Ma, Y., Chen, S., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.02.002 · Cited by 36
Milone, M., & Benarroch, E. E. (2012) · Neurology · doi:10.1212/wnl.0b013e3182563c46 · Cited by 37
Redox Modifications of Proteins of the Mitochondrial Fusion and Fission Machinery
Wolf, C., Amo, V. L. D., Arndt, S., Bueno, D., Tenzer, S., Hanschmann, E.-M., Berndt, C., & Methner, A. (2020) · Cells · doi:10.3390/cells9040815 · Cited by 37
Mitochondrial fission – changing perspectives for future progress
Kamerkar, S. C., Liu, A., & Higgs, H. N. (2025) · Journal of Cell Science · doi:10.1242/jcs.263640 · Cited by 43
Modeling Anesthetic Developmental Neurotoxicity Using Human Stem Cells
Bai, X., Twaroski, D. M., & Bosnjak, Z. J. (2013) · Seminars in Cardiothoracic and Vascular Anesthesia · doi:10.1177/1089253213495923 · Cited by 34
Hogarth, K. A., Costford, S. R., Yoon, G., Sondheimer, N., & Maynes, J. T. (2017) · Biochemical Genetics · doi:10.1007/s10528-017-9829-2 · Cited by 37
Cyclin C directly stimulates Drp1 GTP affinity to mediate stress-induced mitochondrial hyperfission
Ganesan, V., Willis, S. D., Chang, K., Beluch, S., Cooper, K. F., & Strich, R. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-07-0463 · Cited by 36
Hypoxia-induced elevated NDRG1 mediates apoptosis through reprograming mitochondrial fission in HCC
Guo, D., Xie, K., & Luo, X. (2020) · Gene · doi:10.1016/j.gene.2020.144552 · Cited by 34
Mid51/Fis1 mitochondrial oligomerization complex drives lysosomal untethering and network dynamics
Wong, Y. C., Kim, S., Cisneros, J., Molakal, C. G., Song, P., Lubbe, S. J., & Krainc, D. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202206140 · Cited by 33
Mangrulkar, S. V., Wankhede, N. L., Kale, M. B., Upaganlawar, A. B., Taksande, B. G., Umekar, M. J., Anwer, M. K., Dailah, H. G., Mohan, S., & Behl, T. (2023) · Neurotoxicity Research · doi:10.1007/s12640-023-00647-2 · Cited by 35
Zhao, Y., Sun, X., & Qi, X. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.11.031 · Cited by 33
When the Balance Tips: Dysregulation of Mitochondrial Dynamics as a Culprit in Disease
Kyriakoudi, S., Drousiotou, A., & Petrou, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094617 · Cited by 33
Bui, H., Karren, M. A., Bhar, D., & Shaw, J. M. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201207079 · Cited by 31
SAMM 50 Affects Mitochondrial Morphology through the Association of Drp1 in Mammalian Cells
Liu, S., Gao, Y., Zhang, C., Li, H., Pan, S., Wang, X., Du, S., Deng, Z., Wang, L., Song, Z., et al. (2016) · FEBS Letters · doi:10.1002/1873-3468.12170 · Cited by 29
Self-citationRojas-Charry, L., Cookson, M., Niño, A., Arboleda, H., & Arboleda, G. (2014) · NeuroToxicology · doi:10.1016/j.neuro.2014.04.007 · Cited by 29
Barbosa, D. J., Serrat, R., Mirra, S., Quevedo, M., de Barreda, E. G., Ávila, J., Ferreira, L. M., Branco, P. S., Fernandes, E. G. R., Bastos, M. D. L., et al. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu042 · Cited by 31
Seager, R., Ramesh, N. S., Cross, S., Guo, C., Wilkinson, K. A., & Henley, J. M. (2024) · Science Advances · doi:10.1126/sciadv.adq6223 · Cited by 32
Tumour microenvironment on mitochondrial dynamics and chemoresistance in cancer
Han, Y., Cho, U., Kim, S., Park, I. S., Cho, J., Dhanasekaran, D. N., & Song, Y. S. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1459594 · Cited by 28
Li, Y., Zhang, Y., Wang, X., Yang, Q., Zhou, X., Wu, J., Xu, Y., Zhao, Y., Lin, R., Xie, Y., et al. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02137-x · Cited by 29
Self-citationMitochondrial Dynamics: In Cell Reprogramming as It Is in Cancer
Prieto, J., & Torres, J. (2017) · Stem Cells International · doi:10.1155/2017/8073721 · Cited by 26
Yu, R., Jin, S., Ankarcrona, M., Lendahl, U., Nistér, M., & Zhao, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.706687 · Cited by 28
Self-citationFunctional Annotation of Proteome Encoded by Human Chromosome 22
Pinto, S. M., Manda, S. S., Kim, M., Taylor, K., Selvan, L. D. N., Balakrishnan, L., Subbannayya, T., Yan, F., Prasad, T. S. K., Gowda, H., et al. (2014) · Journal of Proteome Research · doi:10.1021/pr401169d · Cited by 28
Drp1 polymerization stabilizes curved tubular membranes similar to those of constricted mitochondria
Ugarte‐Uribe, B., Prévost, C., Das, K. K., Bassereau, P. M., & García‐Sáez, A. J. (2018) · Journal of Cell Science · doi:10.1242/jcs.208603 · Cited by 31
Mukherjee, A., Patra, U., Bhowmick, R., & Chawla‐Sarkar, M. (2018) · Cellular Microbiology · doi:10.1111/cmi.12831 · Cited by 29
Yang, Z., Zheng, H., Li, H., Chen, Y., Hou, D., Fan, Q., Song, J., Guo, L., & Liu, L. (2021) · Virus Research · doi:10.1016/j.virusres.2021.198549 · Cited by 27
Fatty acyl-coenzyme A activates mitochondrial division through oligomerization of MiD49 and MiD51
Liu, A., Kage, F., Abdulkareem, A. F., Aguirre-Huamani, M. P., Sapp, G., Aydin, H., & Higgs, H. N. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01400-3 · Cited by 29
Mui, D., & Zhang, Y. (2020) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2020.1784938 · Cited by 27
Membranes in motion: mitochondrial dynamics and their role in apoptosis
Ugarte‐Uribe, B., & García‐Sáez, A. J. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0234 · Cited by 26
Spermatozoa methylome and its sensitivity to water temperature in a teleost fish
Brionne, A., Goupil, A.-S., Kica, S., Lareyre, J., Labbé, C., & Laurent, A. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.164077 · Cited by 25
Molecular Basis of Mitochondrial and Peroxisomal Division Machineries
Imoto, Y., Itoh, K., & Fujiki, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155452 · Cited by 27
Morphological Pathways of Mitochondrial Division
Tandler, B., Hoppel, C. L., & Mears, J. A. (2018) · Antioxidants · doi:10.3390/antiox7020030 · Cited by 26
SAM50, a side door to the mitochondria: The case of cytotoxic proteases
Lionello, S., Marzaro, G., & Martinvalet, D. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105196 · Cited by 24
Mitochondrial dynamics in the neonatal brain – a potential target following injury?
Jones, A., & Thornton, C. (2022) · Bioscience Reports · doi:10.1042/bsr20211696 · Cited by 25
MTCH2 cooperates with MFN2 and lysophosphatidic acid synthesis to sustain mitochondrial fusion
Goldman, A., Mullokandov, M., Zaltsman, Y., Regev, L., Levin‐Zaidman, S., & Gross, A. (2023) · EMBO Reports · doi:10.1038/s44319-023-00009-1 · Cited by 25
Wang, Y., Katayama, A., Terami, T., Han, X., Nunoue, T., Zhang, D., Teshigawara, S., Eguchi, J., Nakatsuka, A., Murakami, K., et al. (2015) · Metabolism · doi:10.1016/j.metabol.2015.02.004 · Cited by 24
Titanium Dioxide Nanoparticles Induce Mitochondrial Dynamic Imbalance and Damage in HT22 Cells
Zhao, H., Chen, L., Zhong, G., Huang, Y., Zhang, X., Chu, C., Chen, L., & Wang, M. (2019) · Journal of Nanomaterials · doi:10.1155/2019/4607531 · Cited by 24
Role of Mitochondrial Dynamics in Cocaine’s Neurotoxicity
Wen, S., Aki, T., Funakoshi, T., Unuma, K., & Uemura, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105418 · Cited by 25
MDMA impairs mitochondrial neuronal trafficking in a Tau- and Mitofusin2/Drp1-dependent manner
Barbosa, D. J., Serrat, R., Mirra, S., Quevedo, M., de Barreda, E. G., Ávila, J., Fernandes, E. G. R., Bastos, M. D. L., Capela, J. P., Carvalho, F. D., et al. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1209-7 · Cited by 24
Choudhary, V., Kaddour‐Djebbar, I., Alaisami, R., Kumar, M. V., & Bollag, W. B. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2343 · Cited by 23
Canfield, S. G., Žaja, I., Godshaw, B. M., Twaroski, D. M., Bai, X., & Bosnjak, Z. J. (2016) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000001254 · Cited by 23
The Role of Mitochondria in Optic Atrophy With Autosomal Inheritance
Strachan, E. L., MacWhite-Begg, D., Crean, J. K. G., Reynolds, A., Kennedy, B. N., & O’Sullivan, N. C. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.784987 · Cited by 22
Numadate, A., Mita, Y., Matsumoto, Y., Fujii, S., & Hashimoto, Y. (2014) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c14-00333 · Cited by 22
Mechanisms of Modulation of Mitochondrial Architecture
Muñoz, J. P., Basei, F. L., Rojas, M. L., Galvis, D., & Antonio Zorzano, A. (2023) · Biomolecules · doi:10.3390/biom13081225 · Cited by 21
New interfaces on MiD51 for Drp1 recruitment and regulation
Ma, J., Zhai, Y., Chen, M., Zhang, K., Chen, Q., Pang, X., & Sun, F. (2019) · PLoS ONE · doi:10.1371/journal.pone.0211459 · Cited by 21
Regulation of nuclear DNA damage response by mitochondrial morphofunctional pathway
Oanh, N. T. K., Lee, H., Kim, Y., Min, S., Park, Y., Heo, J., Park, Y., Lim, W., & Cho, H. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac690 · Cited by 21
Alkafaas, S. S., Obeid, O. K., Radwan, M. A., Elsalahaty, M. I., Elkafas, S. S., Hafez, W., Janković, N., & Hessien, M. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107574 · Cited by 21
Identification of COX5B as a novel biomarker in high-grade glioma patients
Hu, T., & Xi, J. (2017) · OncoTargets and Therapy · doi:10.2147/ott.s139243 · Cited by 21
Structure of a mitochondrial fission dynamin in the closed conformation
Bohuszewicz, O., & Low, H. H. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0097-6 · Cited by 21
Mitochondrial fission and fusion in neurodegenerative diseases:Ca2+ signalling
Liu, X., Li, T., Tu, X., Xu, M., & Wang, J. (2025) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2025.103992 · Cited by 22
The dual role of autophagy in periprosthetic osteolysis
Yin, Z., Gong, G., Wang, X., Liu, W. X., Wang, B., & Yin, J. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1123753 · Cited by 20
Self-citationDrp1: Focus on Diseases Triggered by the Mitochondrial Pathway
Sun, F., Fang, M., Zhang, H., Song, Q., Li, S., Li, Y., Jiang, S., & Yang, L. (2024) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-024-01245-5 · Cited by 21
DRP3 and ELM1 are required for mitochondrial fission in the liverwort Marchantia polymorpha
Nagaoka, N., Yamashita, A., Kurisu, R., Watari, Y., Ishizuna, F., Tsutsumi, N., Ishizaki, K., Kohchi, T., & Arimura, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-04886-0 · Cited by 19
Open and cut: allosteric motion and membrane fission by dynamin superfamily proteins
Kalia, R., & Frost, A. S. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-10-0709 · Cited by 19
Zhao, Z., Ren, Y., Yuan, M., Liu, G., & Sun, J. P. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-07078-x · Cited by 23
Proteomic Profiling Revealed Mitochondrial Dysfunction in Photoreceptor Cells under Hyperglycemia
Lam, C. H.-I., Cheung, J. K.-W., Tse, D. Y., & Lam, T. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113366 · Cited by 17
Lee, B., Ahn, Y., Kang, S., Park, Y., Jeon, Y., Rho, J. M., & Kim, S.-W. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-02-0762 · Cited by 17
Determining the target protein localization in 3D using the combination of FIB-SEM and APEX2
Shi, Y., Wang, L., Zhang, J., Zhai, Y., & Sun, F. (2017) · Biophysics Reports · doi:10.1007/s41048-017-0043-x · Cited by 17
Li, N., Wu, Y., Zhu, L., Huang, Y. X. R., Liu, Z., Shi, M. Y., Soltys, D., Zhang, J., & Chang, Q. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.07.084 · Cited by 17
How to split up: lessons from mitochondria
Dikov, D., & Reichert, A. S. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.219 · Cited by 17
AlZaim, I., Eid, A. H., Abd‐Elrahman, K. S., & EL‐Yazbi, A. F. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115337 · Cited by 16
Mitochondrial dynamics and metabolism in induced pluripotency
Prieto, J., Ponsoda, X., Belmonte, J. C. I., & Torres, J. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.110870 · Cited by 18
Players in Mitochondrial Dynamics and Female Reproduction
Zou, W., Ji, D., Zhang, Z., Yang, L., & Cao, Y. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.717328 · Cited by 18
Sivakumar, A., Shanmugarajan, S., Ramasamy, S., & Balakrishnan, R. (2020) · APOPTOSIS · doi:10.1007/s10495-020-01616-2 · Cited by 15
How do plastids and mitochondria divide?
Yoshida, Y., & Mogi, Y. (2018) · Microscopy · doi:10.1093/jmicro/dfy132 · Cited by 13
Li, Y., Cui, X., Tian, Y., Zhao, Y., Gao, H., Yao, D., & Liu, L. (2022) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201023666220324123224 · Cited by 14
Li, W., Zhang, Y., Yan, W., Ling, G., Zhang, Y., Li, Y., Guo, S., Tan, N., Ma, L., Li, W., et al. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.103810 · Cited by 14
Mitochondrial Dynamics: Shaping Metabolic Adaptation
Cantó, C. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.05.004 · Cited by 15
Charif, M., Wong, Y. C., Kim, S., Guichet, A., Vignal‐Clermont, C., Zanlonghi, X., Bensaïd, P., Procaccio, V., Bonneau, D., Amati‐Bonneau, P., et al. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00431-w · Cited by 13
Wang, C., Liu, L., Wang, Y., & Xu, D. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16744 · Cited by 13
Zhuang, Y., Jiang, W., Zhao, Z., Li, W., Deng, Z., & Liu, J. (2024) · Channels · doi:10.1080/19336950.2024.2335467 · Cited by 14
Cell life-or-death events in osteoporosis: All roads lead to mitochondrial dynamics
Li, Z., Liang, S., Ke, L., Wang, M., Gao, K., Li, D., Xu, Z., Li, N., Zhang, P., & Cheng, W. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107383 · Cited by 14
Koppenol-Raab, M., Harwig, M., Posey, A. E., Egner, J. M., MacKenzie, K., & Hill, R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.724005 · Cited by 14
Overexpression of wild type or a Q311E mutant MB21D2 promotes a pro‐oncogenic phenotype in HNSCC
Gracilla, D. E., Korla, P. K., Lai, M., Chiang, A., Liou, W., & Sheu, J. J. (2020) · Molecular Oncology · doi:10.1002/1878-0261.12806 · Cited by 13
Su, F., Sui, X. Y., Xu, J., Liu, Q., Li, J., Liu, W., Xu, Y., Zhang, Z., & Tao, F. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176188 · Cited by 14
Novel animal pole‐enriched maternal mRNAs are preferentially expressed in neural ectoderm
Grant, P. A., Yan, B., Johnson, M. A., Johnson, D. L. E., & Moody, S. A. (2013) · Developmental Dynamics · doi:10.1002/dvdy.24082 · Cited by 12
Bassot, A., Chen, J., & Simmen, T. (2021) · Contact · doi:10.1177/25152564211001213 · Cited by 12
Whole Cell Cryo-Electron Tomography Suggests Mitochondria Divide by Budding
Hu, G. (2014) · Microscopy and Microanalysis · doi:10.1017/s1431927614001317 · Cited by 13
Plant mitochondrial dynamics and the role of membrane lipids
Pan, R., & Hu, J. (2015) · Plant Signaling & Behavior · doi:10.1080/15592324.2015.1050573 · Cited by 12
Mitophagy: A Potential Target for Pressure Overload‐Induced Cardiac Remodelling
Shao, R., Li, J., Qu, T., Liao, Y., & Chen, M. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2849985 · Cited by 11
Remodeling of Mitochondria in Apoptosis
Perkins, G. A., & Ellisman, M. H. (2016) · Springer eBooks · doi:10.1007/978-1-4939-3612-0_5 · Cited by 10
Valproic acid regulates MIEF1 through MST2-HIPPO to suppress breast cancer growth
Du, S., Wang, X., Hu, Y., Zhang, S., Wang, D., Zhang, Q., & Liu, S. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120976 · Cited by 9
Self-citationZerihun, M., & Qvit, N. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1275370 · Cited by 9
Mitochondrial Fission and Fusion
Hewitt, V. L., & Whitworth, A. J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803783-6.00003-1 · Cited by 10
Xie, C., Li, K., Li, Y., Peng, X., Teng, B., He, K., Jin, A., Wang, W., & Wei, Z. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.881487 · Cited by 8
Label-Free Visualization of Ultrastructural Features of Artificial Synapses via Cryo-EM
Gopalakrishnan, G., Yam, P. T., Madwar, C., Bostina, M., Rouiller, I., Colman, D., & Lennox, R. B. (2011) · ACS Chemical Neuroscience · doi:10.1021/cn200094j · Cited by 8
Buckley, Y., Stoll, M. S. K., Hoppel, C. L., & Mears, J. A. (2024) · Journal of Cell Science · doi:10.1242/jcs.263459 · Cited by 7
A novel role for Myosin-Va in mitochondrial fissionPreprint
Araujo, J. S., da Silva-Júnior, R. M. P., Zhang, T., Schiavon, C. R., Chu, Q., Wu, M., Pontes, C. L. S., Souza, A. D. O., Alberici, L. C., dos Santos, A. M., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/655803 · Cited by 8
Aggarwal, S., Singh, V. K., Chakraborty, A., Cha, S., Dimitriou, A., de Crescenzo, C., Izikson, O., Yu, L. C., Plebani, R., Tzika, A. A., et al. (2024) · mBio · doi:10.1128/mbio.01292-24 · Cited by 6
Mitochondrial dynamics and signaling in stem cell differentiation
Verma, R. K., Madan, S., & Rikhy, R. (2026) · Journal of Cell Science · doi:10.1242/jcs.263847 · Cited by 6
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Metadata
- Authors
- Zhao, J., Liu, T., Jin, S., Wang, X., Qu, M., Uhlén, P., Tomilin, N., Shupliakov, O., Lendahl, U., & Nistér, M.
- Affiliations
- Karolinska University Hospital (SE)
- Karolinska Institutet (SE)
- Corresponding author
- Zhao, Jian
- Lendahl, Urban
- Nistér, Monica
- Venue
- The EMBO Journal
- Published
- 2011-06-24
- Volume
- 30
- Issue
- 14
- Pages
- 2762-2778
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3160255
- OpenAlex
- W1960363048
- Cited by
- 370
- References
- 54
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 14 · 2023: 22 · 2022: 17 · 2021: 30 · 2020: 25 · 2019: 19 · 2018: 27 · 2017: 27 · 2016: 27 · 2015: 33 · 2014: 38 · 2013: 37 · 2012: 26
- FWCI
- 14.04
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- University of Rochester
- Cancerfonden
- Karolinska Institutet
- Knut och Alice Wallenbergs Stiftelse
- Vetenskapsrådet
- Deutsches Zentrum für Neurodegenerative Erkrankungen
- Barncancerfonden
- Cancerföreningen i Stockholm
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke
- 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, Drp1, mitochondrial fusion, mitochondrial fission, mitochondrial dynamics, mitochondrial outer membrane, mitochondrial fragmentation, mitofusins
- MeSH terms
- Cross-Linking Reagents, Cytoplasm, Fluorescent Antibody Technique, Glioma, HeLa Cells, Humans, Immunoenzyme Techniques, Membrane Fusion, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Neuroblastoma, Peptide Elongation Factors, Protein Binding, RNA, Messenger, Subcellular Fractions, Tumor Cells, Cultured, Blotting, Western, Apoptosis, Reverse Transcriptase Polymerase Chain Reaction, GTP Phosphohydrolases, Mitochondrial Proteins, Dynamins, RNA, Small Interfering, Immunoprecipitation, Mitochondrial Membranes
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