The DOI matches its Crossref record; 135 of the 135 references it cites were found in a registry or an index.
Mitochondrial fusion and fission in cell life and death
Abstract
Mitochondria are dynamic organelles that constantly fuse and divide. These processes (collectively termed mitochondrial dynamics) are important for mitochondrial inheritance and for the maintenance of mitochondrial functions. The core components of the evolutionarily conserved fusion and fission machineries have now been identified, and mechanistic studies have revealed the first secrets of the complex processes that govern fusion and fission of a double membrane-bound organelle. Mitochondrial dynamics was recently recognized as an important constituent of cellular quality control. Defects have detrimental consequences on bioenergetic supply and contribute to the pathogenesis of neurodegenerative diseases. These findings open exciting new directions to explore mitochondrial biology.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“On the contrary, mitochondria fission promotes the removal of dysfunctional mitochondria via an autophagic process termed mitophagy (Westermann, 2010).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Westermann, 2010
In the citing paper
“The maintenance of a healthy cellular mitochondrial network is dependent on the balance between fusion and fission cycles (Westermann, 2010)”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Westermann, 2010
In the citing paper
“Indeed, mitochondria fusion allows the exchange of damaged mtDNA with intact mtDNA resulting from the intimate interaction between isolated mitochondria.”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Westermann, 2010
Citations
Cites
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388
Regulation mechanisms and signaling pathways of autophagy
He, C., & Klionsky, D. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102808-114910 · Cited by 3,609
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
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944
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
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755
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
The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
Li, Z., Okamoto, K.-I., Hayashi, Y., & Sheng, M. (2004) · Cell · doi:10.1016/j.cell.2004.11.003 · Cited by 1,498
Mitochondria Supply Membranes for Autophagosome Biogenesis during Starvation
Hailey, D. W., Rambold, A. S., Satpute‐Krishnan, P., Mitra, K., Sougrat, R., Kim, P. K., & Lippincott‐Schwartz, J. (2010) · Cell · doi:10.1016/j.cell.2010.04.009 · Cited by 1,491
Translocation of Proteins into Mitochondria
Neupert, W., & Herrmann, J. M. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.163409 · Cited by 1,486
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 · cited 1×
“Disruption of fusion in mammalian cells also leads to mitochondrial heterogeneity and dysfunction, possibly as a consequence of nucleoid loss in individual mitochondri”
BackgroundThe dynamin superfamily: universal membrane tubulation and fission molecules?
Praefcke, G. J. K., & McMahon, H. T. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1313 · Cited by 1,370
Functions and dysfunctions of mitochondrial dynamics
Detmer, S. A., & Chan, D. C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2275 · Cited by 1,369
Alexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330
OPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300
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
Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission.
Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., & Mihara, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607279200 · Cited by 1,226
Chen, H., Vermulst, M., Wang, Y. E., Chomyn, A., Prolla, T. A., McCaffery, J. M., & Chan, D. C. (2010) · Cell · doi:10.1016/j.cell.2010.02.026 · Cited by 1,211
Olichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., & Lenaers, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200677200 · Cited by 1,168
Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129
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
Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
Lee, Y.-J., Jeong, S.-Y., Karbowski, M., Smith, C. L., & Youle, R. J. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-04-0294 · Cited by 1,042
Control of mitochondrial morphology by a human mitofusin
Santel, A., & Fuller, M. T. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.867 · Cited by 1,012
Mitochondrial fragmentation in neurodegeneration.
Knott, A. B., Perkins, G., Schwarzenbacher, R., & Bossy-Wetzel, E. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2417 · Cited by 1,002
Mitochondrial fusion protects against neurodegeneration in the cerebellum
Chen, H., McCaffery, J. M., & Chan, D. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.026 · Cited by 924
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
Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
Ishihara, N., Fujita, Y., Oka, T., & Mihara, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601184 · Cited by 899
Karbowski, M., Lee, Y.-J., Gaume, B., Jeong, S.-Y., Frank, S., Nechushtan, A., Santel, A., Fuller, M., Smith, C. L., & Youle, R. J. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200209124 · Cited by 846
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
Song, Z., Chen, H., Fiket, M., Alexander, C., & Chan, D. C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704110 · Cited by 818
SLP‐2 is required for stress‐induced mitochondrial hyperfusion
Tondera, D., Grandemange, S., Jourdain, A. A., Karbowski, M., Mattenberger, Y., Herzig, S., Cruz, S. D., Clerc, P., Lauria, I., Merkwirth, C., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.89 · Cited by 796
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
The Machines that Divide and Fuse Mitochondria
Hoppins, S., Lackner, L., & Nunnari, J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.071905.090048 · Cited by 790
Mitochondrial fission in apoptosis
Youle, R. J., & Karbowski, M. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1697 · Cited by 773
Gandre-Babbe, S., & van der Bliek, A. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1287 · Cited by 769
Cipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K., Metzger, K., Frezza, C., Annaert, W. G., D'adamio, L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.021 · Cited by 756
A Lethal Defect of Mitochondrial and Peroxisomal Fission
Waterham, H. R., Koster, J., van Roermund, C. W. T., Mooyer, P. A. W., Wanders, R. J. A., & Leonard, J. V. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa064436 · Cited by 749
Mitochondrial Morphology and Dynamics in Yeast and Multicellular Eukaryotes
Okamoto, K., & Shaw, J. M. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.093019 · Cited by 737
Drosophila Parkin requires PINK1 for mitochondrial translocation and ubiquitinates Mitofusin
Ziviani, E., Tao, R. N., & Whitworth, A. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913485107 · Cited by 735
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
Mechanisms of membrane fusion: disparate players and common principles
Martens, S., & McMahon, H. T. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2417 · Cited by 734
Mozdy, A. D., McCaffery, J. M., & Shaw, J. M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.2.367 · Cited by 731
Deng, H., Dodson, M. W., Huang, H., & Guo, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803998105 · Cited by 705
AN ELECTRON MICROSCOPE STUDY OF THE MITOCHONDRIAL STRUCTURE
Palade, G. E. (1953) · Journal of Histochemistry & Cytochemistry · doi:10.1177/1.4.188 · Cited by 691
C. elegans Dynamin-Related Protein DRP-1 Controls Severing of the Mitochondrial Outer Membrane
Labrousse, A. M., Zappaterra, M. D., Rube, D. A., & van der Bliek, A. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80391-3 · Cited by 670
The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice
Wakabayashi, J., Zhang, Z., Wakabayashi, N., Tamura, Y., Fukaya, M., Kensler, T. W., Iijima, M., & Sesaki, H. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903065 · Cited by 667
hFis1, a Novel Component of the Mammalian Mitochondrial Fission Machinery
James, D. I., Parone, P. A., Mattenberger, Y., & Martinou, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303758200 · Cited by 653
Mitra, K., Wunder, C., Roysam, B., Lin, G., & Lippincott‐Schwartz, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904875106 · Cited by 648
Role of Bax and Bak in mitochondrial morphogenesis
Karbowski, M., Norris, K. L., Cleland, M. M., Jeong, S.-Y., & Youle, R. J. (2006) · Nature · doi:10.1038/nature05111 · Cited by 625
Dnm1 forms spirals that are structurally tailored to fit mitochondria
Ingerman, E., Perkins, E. M., Marino, M., Mears, J. A., McCaffery, J. M., Hinshaw, J. E., & Nunnari, J. (2005) · Journal of Cell Biology · doi:10.1083/jcb.200506078 · Cited by 621
Developmentally Regulated Mitochondrial Fusion Mediated by a Conserved, Novel, Predicted GTPase
Hales, K. G., & Fuller, M. T. (1997) · Cell · doi:10.1016/s0092-8674(00)80319-0 · Cited by 611
Cargo-Selected Transport from the Mitochondria to Peroxisomes Is Mediated by Vesicular Carriers
Neuspiel, M., Schauss, A. C., Braschi, E., Zunino, R., Rippstein, P. U., Rachubinski, R. A., Andrade-Navarro, M. A., & McBride, H. M. (2008) · Current Biology · doi:10.1016/j.cub.2007.12.038 · Cited by 607
Regulation of OPA1 processing and mitochondrial fusion by m -AAA protease isoenzymes and OMA1
Ehses, S., Lauria, I., Mancuso, G., Bernacchia, A., Geimer, S., Tondera, D., Martinou, J., Westermann, B., Rugarli, E. I., & Langer, T. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200906084 · Cited by 596
Mitochondria are morphologically and functionally heterogeneous within cells
Collins, T. J., Berridge, M. J., Lipp, P., & Bootman, M. D. (2002) · The EMBO Journal · doi:10.1093/emboj/21.7.1616 · Cited by 588
Mitochondrial Fusion in Yeast Requires the Transmembrane GTPase Fzo1p
Hermann, G. J., Thatcher, J., Mills, J. P., Hales, K. G., Fuller, M., Nunnari, J., & Shaw, J. (1998) · Journal of Cell Biology · doi:10.1083/jcb.143.2.359 · Cited by 572
Rojo, M., Legros, F., Chateau, D., & Lombès, A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.8.1663 · Cited by 555
Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery
Yang, Y., Ouyang, Y., Yang, L., Beal, M. F., McQuibban, G. A., Vogel, H. S., & Lu, B. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711845105 · Cited by 549
Wasiak, S., Zunino, R., & McBride, H. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610042 · Cited by 537
Division versus Fusion: Dnm1p and Fzo1p Antagonistically Regulate Mitochondrial Shape
Sesaki, H., & Jensen, R. E. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.4.699 · Cited by 531
GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
Roux, A., Uyhazi, K., Frost, A., & Camilli, P. D. (2006) · Nature · doi:10.1038/nature04718 · Cited by 524
Versatility of the mitochondrial protein import machinery
Pfanner, N., & Geissler, A. (2001) · Nature reviews. Molecular cell biology · doi:10.1038/35073006 · Cited by 521
Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells
Head, B., Griparic, L., Amiri, M., Gandre-Babbe, S., & van der Bliek, A. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200906083 · Cited by 515
The organization and inheritance of the mitochondrial genome
Chen, X. J., & Butow, R. A. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1708 · Cited by 496
Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage
Griparić, L., Kanazawa, T., & van der Bliek, A. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704112 · Cited by 486
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 485
Mitochondrial filaments and clusters as intracellular power-transmitting cables
Skulachev, V. P. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01735-7 · Cited by 477
Mitochondrial Inner-Membrane Fusion and Crista Maintenance Requires the Dynamin-Related GTPase Mgm1
Meeusen, S., DeVay, R. M., Block, J., Cassidy-Stone, A., Wayson, S. M., McCaffery, J. M., & Nunnari, J. M. (2006) · Cell · doi:10.1016/j.cell.2006.09.021 · Cited by 474
Mitochondrial Fusion Intermediates Revealed in Vitro
Meeusen, S. L., McCaffery, J., & Nunnari, J. (2004) · Science · doi:10.1126/science.1100612 · Cited by 466
Genetic Basis of Mitochondrial Function and Morphology in Saccharomyces cerevisiae
Dimmer, K. S., Fritz, S., Fuchs, F., Messerschmitt, M., Weinbach, N., Neupert, W., & Westermann, B. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-12-0588 · Cited by 443
CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology
Han, X.-J., Lü, Y.-F., Li, S.-A., Kaitsuka, T., Sato, Y., Tomizawa, K., Nairn, A. C., Takei, K., Matsui, H., & Matsushita, M. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200802164 · Cited by 435
Nakada, K., Inoue, K., Ono, T., Isobe, K., Ogura, A., Goto, Y., Nonaka, I., & Hayashi, J. (2001) · Nature Medicine · doi:10.1038/90976 · Cited by 430
The Dynamin-related GTPase, Dnm1p, Controls Mitochondrial Morphology in Yeast
Otsuga, D., Keegan, B. R., Brisch, E., Thatcher, J. W., Hermann, G. J., Bleazard, W., & Shaw, J. M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.333 · Cited by 429
Ono, T., Isobe, K., Nakada, K., & Hayashi, J.-I. (2001) · Nature Genetics · doi:10.1038/90116 · Cited by 420
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
Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
McQuibban, G. A., Saurya, S., & Freeman, M. (2003) · Nature · doi:10.1038/nature01633 · Cited by 400
Loss of Parkin or PINK1 Function Increases Drp1-dependent Mitochondrial Fragmentation
Lutz, A. K., Exner, N., Fett, M. E., Schlehe, J. S., Kloos, K., Lämmermann, K., Brunner, B., Kurz-Drexler, A., Vogel, F., Reichert, A. S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.035774 · Cited by 388
Herlan, M., Vogel, F., Bornhövd, C., Neupert, W., & Reichert, A. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211311200 · Cited by 378
A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics
Yonashiro, R., Ishido, S., Kyo, S., Fukuda, T., Gotō, E., Matsuki, Y., Ohmura‐Hoshino, M., Sada, K., Hotta, H., Yamamura, H., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601249 · Cited by 378
Tieu, Q., & Nunnari, J. M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.2.353 · Cited by 375
Dynamin-like protein 1 is involved in peroxisomal fission
Koch, A., Thiemann, M., Grabenbauer, M., Yoon, Y., McNiven, M. A., & Schrader, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211761200 · Cited by 374
Rapaport, D., Brunner, M., Neupert, W., & Westermann, B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20150 · Cited by 370
Wong, E. D., Wagner, J. A., Gorsich, S. W., McCaffery, J. M., Shaw, J. M., & Nunnari, J. M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.2.341 · Cited by 356
Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins
Brooks, C., Wei, Q., Feng, L., Dong, G., Tao, Y., Mei, L., Xie, Z.-J., & Dong, Z. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703976104 · Cited by 351
MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission
Braschi, E., Zunino, R., & McBride, H. M. (2009) · EMBO Reports · doi:10.1038/embor.2009.86 · Cited by 350
Behavior of Mitochondria in the Living Cell
Bereiter‐Hahn, J. (1990) · International review of cytology · doi:10.1016/s0074-7696(08)61205-x · Cited by 329
DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
Jagasia, R., Grote, P., Westermann, B., & Conradt, B. (2005) · Nature · doi:10.1038/nature03316 · Cited by 319
Frequent fusion and fission of plant mitochondria with unequal nucleoid distribution
Arimura, S., Yamamoto, J., Aida, G. P., Nakazono, M., & Tsutsumi, N. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401077101 · Cited by 310
Mitochondrial fission proteins regulate programmed cell death in yeastPreprint
Fannjiang, Y., Cheng, W., Lee, S. J., Qi, B., Pevsner, J., McCaffery, J. M., Hill, R. B., Basáñez, G., & Hardwick, J. M. (2004) · Genes & Development · doi:10.1101/gad.1247904 · Cited by 309
A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells
Koch, A., Yoon, Y., Bonekamp, N. A., McNiven, M. A., & Schrader, M. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-02-0159 · Cited by 308
Beckman, K. B., & Ames, B. N. (2000) · Elsevier eBooks · doi:10.1016/b978-044482650-3/50027-4 · Cited by 307
Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion
DeVay, R. M., Domínguez‐Ramírez, L., Lackner, L. L., Hoppins, S. C., Stahlberg, H., & Nunnari, J. M. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200906098 · Cited by 288
Amchenkova, A. A., Bakeeva, L. E., Chentsov, Y. S., Skulachev, V. P., & Zorov, D. B. (1988) · The Journal of cell biology · doi:10.1083/jcb.107.2.481 · Cited by 284
Griffin, E. E., Graumann, J., & Chan, D. C. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200503148 · Cited by 265
The SUMO protease SENP5 is required to maintain mitochondrial morphology and function
Zunino, R., Schauss, A. C., Rippstein, P. U., Andrade-Navarro, M. A., & McBride, H. M. (2007) · Journal of Cell Science · doi:10.1242/jcs.03418 · Cited by 262
UGO1 Encodes an Outer Membrane Protein Required for Mitochondrial Fusion
Sesaki, H., & Jensen, R. E. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.6.1123 · Cited by 252
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
The mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells
Tondera, D., Czauderna, F., Paulick, K., Schwarzer, R., Kaufmann, J., & Santel, A. (2005) · Journal of Cell Science · doi:10.1242/jcs.02415 · Cited by 239
Separate fusion of outer and inner mitochondrial membranes
Malka, F., Guillery, O., Cifuentes-Díaz, C., Guillou, E., Belenguer, P., Lombès, A., & Rojo, M. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400488 · Cited by 233
Herlan, M., Bornhövd, C., Hell, K., Neupert, W., & Reichert, A. S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403022 · Cited by 223
Tieu, Q., Okreglak, V., Naylor, K., & Nunnari, J. M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205031 · Cited by 217
Merz, S., & Westermann, B. (2009) · Genome Biology · doi:10.1186/gb-2009-10-9-r95 · Cited by 213
Self-citationDynamin-related proteins Vps1p and Dnm1p control peroxisome abundance inSaccharomyces cerevisiae
Kuravi, K. V., Nagotu, S., Krikken, A. M., Sjollema, K. A., Deckers, M., Erdmann, R., Marten Veenhuis, A., & van der Klei, I. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.03166 · Cited by 200
Ugo1p Links the Fzo1p and Mgm1p GTPases for Mitochondrial Fusion
Sesaki, H., & Jensen, R. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401363200 · Cited by 198
Constriction and Dnm1p Recruitment Are Distinct Processes in Mitochondrial Fission
Legesse-Miller, A., Massol, R., & Kirchhausen, T. L. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-10-0657 · Cited by 197
A dynamin-like protein (ADL2b), rather than FtsZ, is involved in Arabidopsis mitochondrial division
Arimura, S., & Tsutsumi, N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082663299 · Cited by 194
Mitochondrial Fusion Is Increased by the Nuclear Coactivator PGC-1β
Liesa, M., Borda-d'Agua, B., Medina‐Gómez, G., Lelliott, C. J., Paz, J. C., Rojo, M., Palacín, M., Vidal‐Puig, A., & Antonio Zorzano, A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003613 · Cited by 182
Cohen, M. M., Leboucher, G. P., Livnat‐Levanon, N., Glickman, M. H., & Weissman, A. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-02-0227 · Cited by 176
Mitochondrial FtsZ in a Chromophyte Alga
Beech, P. L., Nheu, T. V., Schultz, T. F., Herbert, S., Lithgow, T. J., Gilson, P. R., & McFadden, G. I. (2000) · Science · doi:10.1126/science.287.5456.1276 · Cited by 174
Role of Essential Genes in Mitochondrial Morphogenesis inSaccharomyces cerevisiae
Altmann, K., & Westermann, B. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0678 · Cited by 165
The C. elegans Opa1 Homologue EAT-3 Is Essential for Resistance to Free Radicals
Kanazawa, T., Zappaterra, M., Hasegawa, A., Wright, A. P., Newman-Smith, E. D., BUTTLE, K. F., McDonald, K. L., Mannella, C. A., & van der Bliek, A. M. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000022 · Cited by 164
Connection of the Mitochondrial Outer and Inner Membranes by Fzo1 Is Critical for Organellar Fusion
Fritz, S., Rapaport, D., Klanner, E., Neupert, W., & Westermann, B. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.4.683 · Cited by 156
Breckenridge, D. G., Kang, B., Kokel, D., Mitani, S., Staehelin, L. A., & Xue, D. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.015 · Cited by 149
Structural basis for recruitment of mitochondrial fission complexes by Fis1
Zhang, Y., & Chan, D. C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706441104 · Cited by 141
Mdm30 Is an F-Box Protein Required for Maintenance of Fusion-competent Mitochondria in Yeast
Fritz, S., Weinbach, N., & Westermann, B. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0831 · Cited by 140
Mechanistic Analysis of a Dynamin Effector
Lackner, L. L., Horner, J. S., & Nunnari, J. M. (2009) · Science · doi:10.1126/science.1176921 · Cited by 137
The inner membrane protein Mdm33 controls mitochondrial morphology in yeast
Messerschmitt, M., Jakobs, S., Vogel, F., Fritz, S., Dimmer, K., Neupert, W., & Westermann, B. (2003) · Journal of Cell Biology · doi:10.1083/jcb.200211113 · Cited by 132
Altmann, K., Frank, M., Neumann, D., Jakobs, S., & Westermann, B. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709099 · Cited by 130
Yarosh, W., Monserrate, J. P., Tong, J. J., Tse, S., Le, P. K., Nguyen, K., Brachmann, C. B., Wallace, D. C., & Huang, T. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.0040006 · Cited by 128
Role of Mitochondrial Remodeling in Programmed Cell Death in Drosophila melanogaster
Goyal, G., Fell, B., Sarin, A., Youle, R. J., & Sriram, V. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.02.002 · Cited by 124
Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p
Jakobs, S., Martini, N., Schauss, A. C., Egner, A., Westermann, B., & Hell, S. W. (2003) · Journal of Cell Science · doi:10.1242/jcs.00423 · Cited by 119
Eura, Y., Ishihara, N., Oka, T., & Mihara, K. (2006) · Journal of Cell Science · doi:10.1242/jcs.03253 · Cited by 115
OPA1 cleavage depends on decreased mitochondrial ATP level and bivalent metals
Baricault, L., Ségui, B., Guégand, L., Olichon, A., Valette, A., Larminat, F., & Lenaers, G. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.08.008 · Cited by 109
Yeast Mitochondrial Division and Distribution Require the Cortical Num1 Protein
Cerveny, K. L., Studer, S. L., Jensen, R. E., & Sesaki, H. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.01.017 · Cited by 106
Arimura, S., Fujimoto, M., Doniwa, Y., Kadoya, N., Nakazono, M., Sakamoto, W., & Tsutsumi, N. (2008) · The Plant Cell · doi:10.1105/tpc.108.058578 · Cited by 101
Mitochondrial outer and inner membrane fusion requires a modified carrier protein
Hoppins, S. C., Horner, J. S., Song, C., McCaffery, J. M., & Nunnari, J. M. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200809099 · Cited by 99
Takahara, M., Takahashi, H., Matsunaga, S., Miyagishima, S., Takano, H., Sakai, A., Kawano, S., & Kuroiwa, T. (2000) · Molecular Genetics and Genomics · doi:10.1007/s004380000307 · Cited by 95
ADL2a, like ADL2b, is involved in the control of higher plant mitochondrial morphology*
Logan, D. C., Scott, I., & Tobin, A. K. (2004) · Journal of Experimental Botany · doi:10.1093/jxb/erh073 · Cited by 94
Scott, I., Tobin, A. K., & Logan, D. C. (2006) · Journal of Experimental Botany · doi:10.1093/jxb/erj096 · Cited by 91
Schauss, A. C., Bewersdorf, J., & Jakobs, S. (2006) · Journal of Cell Science · doi:10.1242/jcs.03026 · Cited by 70
Mdm36 Is a Mitochondrial Fission-promoting Protein inSaccharomyces cerevisiae
Hammermeister, M., Schödel, K., & Westermann, B. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-02-0096 · Cited by 56
Amiott, E. A., Cohen, M. M., Saint-Georges, Y., Weissman, A. M., & Shaw, J. M. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-07-0622 · Cited by 45
Cited by
Sorted by citations
Pathophysiology of type 2 diabetes mellitus
Galicia-Garcia, U., Benito-Vicente, A., Jebari, S., Larrea-Sebal, A., Siddiqi, H., Uribe, K. B., Ostolaza, H., & Martín, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176275 · Cited by 3,360
“This process generates energy to maintain cell viability under unfavorable conditions and protects the cell during stress conditions [136,139].”
BackgroundYoule, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273
Lagadinou, E. D., Sach, A., Callahan, K. P., Rossi, R. M., Neering, S. J., Minhajuddin, M., Ashton, J. M., Pei, S., Grose, V., O’Dwyer, K. M., et al. (2013) · Cell stem cell · doi:10.1016/j.stem.2012.12.013 · Cited by 1,465
“These included the SLC25A42 and SLC25A38 mitochondrial carriers that transport metabolites and amino acids across the mitochondrial membrane, and the gene FIS1, which is critical for mitochondrial dynamics and fission (Figure 3A) (Westermann, 2010).”
BackgroundMitochondria in Apoptosis: Bcl-2 Family Members and Mitochondrial Dynamics
Martinou, J., & Youle, R. J. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.06.017 · Cited by 1,395
“The core components of the fusion and fission machineries have been identified as the dynamin-related proteins Drp1, mitofusins (Mfn) 1 and 2, and Opa1 (Box 1) (reviewed in Westermann, 2010).”
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
“The opposing processes of fusion and fission (division) regulate mitochondrial morphology and function (Westermann, 2010; Chan, 2012; Youle and van der Bliek, 2012).”
Background
Metadata
- Authors
- Westermann, B.
- Affiliations
- University of Bayreuth (DE)
- Corresponding author
- Westermann, Benedikt
- ORCID
- Westermann, Benedikt
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2010-11-23
- Volume
- 11
- Issue
- 12
- Pages
- 872-884
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2032234589
- Cited by
- 2,002
- References
- 135
- Citations by year
- 2026: 91 · 2025: 109 · 2024: 158 · 2023: 135 · 2022: 134 · 2021: 192 · 2020: 184 · 2019: 125 · 2018: 113 · 2017: 141 · 2016: 117 · 2015: 119 · 2014: 107 · 2013: 95 · 2012: 118
- FWCI
- 7.67
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- ERef Bayreuth (University of Bayreuth) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- 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
- mitochondrial fusion, mitochondrial fission, mitochondrial dynamics, mitochondrial inheritance, mitochondrial quality control, mitochondrial bioenergetics, neurodegenerative diseases
- MeSH terms
- Animals, Humans, Membrane Fusion, Mitochondria, Models, Biological, Cell Death, Cytokinesis, Cell Proliferation, Genes, Mitochondrial, Mitochondrial Membranes
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review