Mammalian Dynamin-like Protein DLP1 Tubulates Membranes
Open accessAbstract
Dynamins are large GTPases with mechanochemical properties that are known to constrict and tubulate membranes. A recently identified mammalian dynamin-like protein (DLP1) is essential for the proper cellular distribution of mitochondria and the endoplasmic reticulum in cultured cells. In this study, we investigated the ability of DLP1 to remodel membranes similar to conventional dynamin. We found that the expression of a GTPase-defective mutant, DLP1-K38A, in cultured cells led to the formation of large cytoplasmic aggregates. Electron microscopy (EM) of cells expressing DLP1-K38A revealed that these aggregates were comprised of membrane tubules of a consistent diameter. High-magnification EM revealed the presence of many regular striations along individual membrane tubules, and immunogold labeling confirmed the association of DLP1 with these structures. Biochemical experiments with the use of recombinant DLP1 and labeled GTP demonstrated that DLP1-K38A binds but does not hydrolyze or release GTP. Furthermore, the affinity of DLP1-K38A for membrane is increased compared with wild-type DLP1. To test whether DLP1 could tubulate membrane in vitro, recombinant DLP1 was combined with synthetic liposomes and nucleotides. We found that DLP1 protein alone assembled into sedimentable macromolecular structures in the presence of guanosine-5′-O-(3-thio)triphosphate (GTPγS) but not GTP. EM of the GTPγS-treated DLP1 revealed clusters of stacked helical ring structures. When liposomes were included with DLP1, formation of long membrane tubules similar in size to those formed in vivo was observed. Addition of GTPγS greatly enhanced membrane tubule formation, suggesting the GTP-bound form of DLP1 deforms liposomes into tubules as the DLP1-K38A does in vivo. These results provide the first evidence that the dynamin family member, DLP1, is able to tubulate membranes both in living cells and in vitro. Furthermore, these findings also indicate that despite the limited homology to conventional dynamins (35%) these proteins remodel membranes in a similar manner.
Integrity signals
Registry
Cites
Statistics
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?
Although DRP1 can tubulate membranes, it cannot complete membrane scission.
“Although DRP1 can tubulate the membranes, it cannot complete membrane scission [84].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [84]
Cites
The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392 · see citing works
Induction of mutant dynamin specifically blocks endocytic coated vesicle formation.
Damke, H., Baba, T., Warnock, D. E., & Schmid, S. L. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.4.915 · Cited by 1,203 · see citing works
Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
Hinshaw, J. E., & Schmid, S. L. (1995) · Nature · doi:10.1038/374190a0 · Cited by 824 · see citing works
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 · see citing works
Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals
Takei, K., McPherson, P. S., Schmid, S. L., & Camilli, P. V. D. (1995) · Nature · doi:10.1038/374186a0 · Cited by 768 · see citing works
Dynamin-mediated Internalization of Caveolae
Henley, J. R., Krueger, E. W. A., Oswald, B. J., & McNiven, M. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.1.85 · Cited by 767 · see citing works
Self-citationA 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 · see citing works
Mutations in human dynamin block an intermediate stage in coated vesicle formation
van der Bliek, A., Redelmeier, T., Damke, H., Tisdale, E. J., Meyerowitz, E. M., & Schmid, S. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.122.3.553 · Cited by 698 · see citing works
Dynamin Undergoes a GTP-Dependent Conformational Change Causing Vesiculation
Sweitzer, S. M., & Hinshaw, J. E. (1998) · Cell · doi:10.1016/s0092-8674(00)81207-6 · Cited by 682 · see citing works
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 · see citing works
Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
Takei, K., Slepnev, V. I., Haucke, V., & Camilli, P. V. D. (1999) · Nature Cell Biology · doi:10.1038/9004 · Cited by 657 · see citing works
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 · see citing works
Effects of mutant rat dynamin on endocytosis
Herskovits, J. S., Burgess, C. C., Obar, R., & Vallee, R. B. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.122.3.565 · Cited by 456 · see citing works
GTPase activity of dynamin and resulting conformation change are essential for endocytosis
Marks, B., Stowell, M. H. B., Vallis, Y., Mills, I. G., Gibson, A., Hopkins, C. R., & McMahon, H. T. (2001) · Nature · doi:10.1038/35065645 · Cited by 455 · see citing works
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 423 · see citing works
Stowell, M. H. B., Marks, B., Wigge, P., & McMahon, H. T. (1999) · Nature Cell Biology · doi:10.1038/8997 · Cited by 378 · see citing works
Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis
Sever, S., Muhlberg, A. B., & Schmid, S. L. (1999) · Nature · doi:10.1038/19024 · Cited by 369 · see citing works
The dynamin family of mechanoenzymes: pinching in new places
McNiven, M. A., Cao, H., Pitts, K. R., & Yoon, Y. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01538-8 · Cited by 343 · see citing works
Self-citationGeneration of Coated Intermediates of Clathrin-Mediated Endocytosis on Protein-Free Liposomes
Takei, K., Haucke, V., Slepnev, V. I., Farsad, K., Salazar, M. A. G., Chen, H., & Camilli, P. V. D. (1998) · Cell · doi:10.1016/s0092-8674(00)81228-3 · Cited by 340 · see citing works
Rab GTPases: master regulators of membrane trafficking
Pfeffer, S. R. (1994) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(94)90071-x · Cited by 330 · see citing works
Role of Dynamin in the Formation of Transport Vesicles from the Trans-Golgi Network
Jones, S. M., Howell, K. E., Henley, J. R., Cao, H., & McNiven, M. A. (1998) · Science · doi:10.1126/science.279.5350.573 · Cited by 318 · see citing works
Self-citationPitts, K. R., Yoon, Y., Krueger, E. W., & McNiven, M. A. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.12.4403 · Cited by 311 · see citing works
Self-citationARF: a key regulatory switch in membrane traffic and organelle structure
Donaldson, J. G., & Klausner, R. D. (1994) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(94)90072-8 · Cited by 261 · see citing works
Functional diversity in the dynamin family
van der Bliek, A. M., & van der Bliek, A. M. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01490-1 · Cited by 259 · see citing works
Dynamin family of mechanoenzymes
Danino, D., & Hinshaw, J. E. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00236-2 · Cited by 196 · see citing works
Yoon, Y., Pitts, K. R., Dahan, S., & McNiven, M. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.4.779 · Cited by 183 · see citing works
Self-citationMcNiven, M. A. (1998) · Cell · doi:10.1016/s0092-8674(00)81414-2 · Cited by 174 · see citing works
Self-citationLlorente, A., Rapak, A., Schmid, S. L., van Deurs, B., & Sandvig, K. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.3.553 · Cited by 124 · see citing works
Shin, H., Shinotsuka, C., Torii, S., Murakami, K., & Nakayama, K. (1997) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021784 · Cited by 122 · see citing works
Association of a dynamin-like protein with the Golgi apparatus in mammalian cells.
Henley, J. R., & McNiven, M. A. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.133.4.761 · Cited by 114 · see citing works
Self-citationStirling, J. W., & Graff, P. S. (1995) · Journal of Histochemistry & Cytochemistry · doi:10.1177/43.2.7529784 · Cited by 110 · see citing works
Imoto, M., Tachibana, I., & Urrutia, R. A. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.10.1341 · Cited by 109 · see citing works
Nicoziani, P., Vilhardt, F., Llorente, A., Hilout, L., Courtoy, P. J., Sandvig, K., & van Deurs, B. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.2.481 · Cited by 97 · see citing works
Shin, H., Takatsu, H., Mukai, H., Munekata, E., Murakami, K., & Nakayama, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.5.2780 · Cited by 67 · see citing works
Kamimoto, T., Nagai, Y., Onogi, H., Muro, Y., Wakabayashi, T., & Hagiwara, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.2.1044 · Cited by 55 · see citing works
Dynamin II Binds to theTrans-Golgi Network
Maier, O., Knoblich, M., & Westermann, P. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0876 · Cited by 54 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Mitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479 · see citing works
Calcium, ATP, and ROS: a mitochondrial love-hate triangle
Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2004 · Cited by 2,575 · see citing works
Self-citationER Tubules Mark Sites of Mitochondrial Division
Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072 · see citing works
Mitochondria: More Than Just a Powerhouse
McBride, H. M., Neuspiel, M., & Wasiak, S. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.054 · Cited by 1,985 · see citing works
Mitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397 · see citing works
The 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 · see citing works
Yu, T., Robotham, J. L., & Yoon, Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511154103 · Cited by 1,246 · see citing works
Self-citationCogliati, S., Frezza, C., Soriano, M. E., Varanita, T., Quintana-Cabrera, R., Corrado, M., Cipolat, S., Costa, V., Casarin, A., Gomes, L. C., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.032 · Cited by 1,265 · see citing works
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196 · see citing works
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 · see citing works
Mitochondrial Fusion and Fission in Mammals
Chan, D. C. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104638 · Cited by 972 · see citing works
Mitochondrial Dynamics in Mammalian Health and Disease
Liesa, M., Palacín, M., & Zorzano, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00030.2008 · Cited by 953 · see citing works
Structure and function of ER membrane contact sites with other organelles
Phillips, M. J., & Voeltz, G. K. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.8 · Cited by 933 · see citing works
Wang, Z., Jiang, H., Chen, S., Du, F., & Wang, X. (2012) · Cell · doi:10.1016/j.cell.2011.11.030 · Cited by 949 · see citing works
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 · see citing works
Self-citationThe 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 · see citing works
Mitochondrial fission in apoptosis
Youle, R. J., & Karbowski, M. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1697 · Cited by 773 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Nitric oxide‐induced mitochondrial fission is regulated by dynamin‐related GTPases in neurons
Barsoum, M. J., Yuan, H., Gerencser, A. A., Liot, G., Kushnareva, Y., Gräber, S., Kovács, I., Lee, W. D., Waggoner, J., Cui, J., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601253 · Cited by 658 · see citing works
MiD49 and MiD51, new components of the mitochondrial fission machinery
Palmer, C. S., Osellame, L. D., Laine, D., Koutsopoulos, O. S., Frazier, A. E., & Ryan, M. T. (2011) · The EMBO Reports · doi:10.1038/embor.2011.54 · Cited by 649 · see citing works
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 592 · see citing works
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 · see citing works
Multiple dynamin family members collaborate to drive mitochondrial division
Lee, J. E., Westrate, L. M., Wu, H., Page, C., & Voeltz, G. K. (2016) · Nature · doi:10.1038/nature20555 · Cited by 512 · see citing works
Wasiak, S., Zunino, R., & McBride, H. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610042 · Cited by 519 · see citing works
New insights into the function and regulation of mitochondrial fission
Otera, H., Ishihara, N., & Mihara, K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.002 · Cited by 476 · see citing works
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
Yu, T., Sheu, S.-S., Robotham, J. L., & Yoon, Y. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn104 · Cited by 462 · see citing works
Self-citationMitochondrial dynamics in neurodegeneration
Itoh, K., Nakamura, K., Iijima, M., & Sesaki, H. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.10.006 · Cited by 464 · see citing works
Interferon‐Induced Mx Proteins: Dynamin‐Like GTPases with Antiviral Activity
Haller, O., & Kochs, G. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.31003.x · Cited by 460 · see citing works
Olichon, A., Emorine, L. J., Descoins, E., Pelloquin, L., Brichese, L., Gas, N., Guillou, E., Delettre, C., Valette, A., Hamel, C., et al. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02985-x · Cited by 430 · see citing works
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 423 · see citing works
Conformational changes in Dnm1 support a contractile mechanism for mitochondrial fission
Mears, J. A., Lackner, L. L., Fang, S., Ingerman, E., Nunnari, J. M., & Hinshaw, J. E. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1949 · Cited by 418 · see citing works
Molecular mechanisms of mitochondrial dynamics
Tábara, L. C., Segawa, M., & Prudent, J. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00785-1 · Cited by 431 · see citing works
Mitochondrial dynamics and division in budding yeast
Shaw, J. M., & Nunnari, J. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02246-2 · Cited by 375 · see citing works
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 · see citing works
Self-citationZhao, J., Liu, T., Jin, S., Wang, X., Qu, M., Uhlén, P., Tomilin, N., Shupliakov, O., Lendahl, U., & Nistér, M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.198 · Cited by 370 · see citing works
Sumo1 Conjugates Mitochondrial Substrates and Participates in Mitochondrial Fission
Harder, Z., Zunino, R., & McBride, H. M. (2004) · Current Biology · doi:10.1016/j.cub.2004.02.004 · Cited by 367 · see citing works
Determinants and outcomes of mitochondrial dynamics
Quintana–Cabrera, R., & Scorrano, L. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.012 · Cited by 345 · see citing works
Manor, U., Bartholomew, S. R., Golani, G., Christenson, E. T., Kozlov, M. M., Higgs, H. N., Spudich, J. A., & Lippincott‐Schwartz, J. (2015) · eLife · doi:10.7554/elife.08828 · Cited by 341 · see citing works
Germain, M., Mathai, J. P., McBride, H. M., & Shore, G. C. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600592 · Cited by 337 · see citing works
Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology
Stojanovski, D., Koutsopoulos, O. S., Okamoto, K., & Ryan, M. T. (2004) · Journal of Cell Science · doi:10.1242/jcs.01058 · Cited by 332 · see citing works
Determinants and Functions of Mitochondrial Behavior
Labbè, K., Murley, A., & Nunnari, J. M. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155756 · Cited by 315 · see citing works
Palmer, C. S., Elgass, K. D., Parton, R. G., Osellame, L. D., Stojanovski, D., & Ryan, M. T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.479873 · Cited by 301 · see citing works
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 · see citing works
Self-citationNeuspiel, M., Zunino, R., Gangaraju, S., Rippstein, P. U., & McBride, H. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501599200 · Cited by 308 · see citing works
Mitochondrial dynamics in cell death and neurodegeneration
Cho, D., Nakamura, T., & Lipton, S. A. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0435-2 · Cited by 299 · see citing works
Yu, T., Jhun, B. S., & Yoon, Y. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3284 · Cited by 286 · see citing works
Self-citationMutant huntingtin and mitochondrial dysfunction
Bossy‐Wetzel, E., Petrilli, A. M., & Knott, A. B. (2008) · Trends in Neurosciences · doi:10.1016/j.tins.2008.09.004 · Cited by 269 · see citing works
Endophilin B1 is required for the maintenance of mitochondrial morphology
Karbowski, M., Jeong, S., & Youle, R. J. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200407046 · Cited by 264 · see citing works
Mitochondrial division ensures the survival of postmitotic neurons by suppressing oxidative damage
Kageyama, Y., Zhang, Z., Roda, R. H., Fukaya, M., Wakabayashi, J., Wakabayashi, N., Kensler, T. W., Reddy, P. H., Iijima, M., & Sesaki, H. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201110034 · Cited by 256 · see citing works
Molecular mechanisms and physiologic functions of mitochondrial dynamics
Otera, H., & Mihara, K. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr002 · Cited by 251 · see citing works
The constriction and scission machineries involved in mitochondrial fission
Kraus, F., & Ryan, M. T. (2017) · Journal of Cell Science · doi:10.1242/jcs.199562 · Cited by 244 · see citing works
Váradi, A., Johnson-Cadwell, L. I., Cirulli, V., Yoon, Y., Allan, V., & Rutter, G. A. (2004) · Journal of Cell Science · doi:10.1242/jcs.01299 · Cited by 242 · see citing works
Self-citationMitochondrial dynamics in the adult cardiomyocytes: which roles for a highly specialized cell?
Piquereau, J., Caffin, F., Novotová, M., Lemaire, C., Veksler, V., Garnier, A., Ventura‐Clapier, R., & Joubert, F. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00102 · Cited by 235 · see citing works
Zhu, P.-P., Patterson, A. D., Stadler, J., Seeburg, D. P., Sheng, M., & Blackstone, C. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404105200 · Cited by 221 · see citing works
Mitochondrial Dynamics in Diabetes
Yoon, Y., Galloway, C. A., Jhun, B. S., & Yu, T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3286 · Cited by 216 · see citing works
Self-citationThe BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy
Ren, G., Vajjhala, P., Lee, J. S., Winsor, B., & Munn, A. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.70.1.37-120.2006 · Cited by 219 · see citing works
Figueroa‐Romero, C., Iñiguez-Lluhı́, J. A., Stadler, J., Chang, C., Arnoult, D., Keller, P. J., Hong, Y. H., Blackstone, C. D., & Feldman, E. L. (2009) · The FASEB Journal · doi:10.1096/fj.09-136630 · Cited by 201 · see citing works
Coincident Phosphatidic Acid Interaction Restrains Drp1 in Mitochondrial Division
Adachi, Y., Itoh, K., Yamada, T., Cerveny, K. L., Suzuki, T. L., Macdonald, P. J., Frohman, M. A., Ramachandran, R., Iijima, M., & Sesaki, H. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.013 · Cited by 198 · see citing works
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
Fission and proliferation of peroxisomes
Schrader, M., Bonekamp, N. A., & Islinger, M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.014 · Cited by 189 · see citing works
Zerihun, M., Sukumaran, S., & Qvit, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065785 · Cited by 189 · see citing works
Mitochondrial fusion and division: Regulation and role in cell viability
Bénard, G., & Karbowski, M. (2009) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2008.12.012 · Cited by 182 · see citing works
The ever-growing complexity of the mitochondrial fission machinery
Pagliuso, A., Cossart, P., & Stavru, F. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2603-0 · Cited by 184 · see citing works
Lee, H., Smith, S. B., & Yoon, Y. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.762567 · Cited by 190 · see citing works
Self-citationMitochondrial fission and fusion
Lee, H., & Yoon, Y. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160129 · Cited by 183 · see citing works
Self-citationConstriction of the mitochondrial inner compartment is a priming event for mitochondrial division
Cho, B., Cho, H. M., Jo, Y., Kim, H. D., Song, M., Moon, C., Kim, H., Kim, K., Sesaki, H., Rhyu, I. J., et al. (2017) · Nature Communications · doi:10.1038/ncomms15754 · Cited by 179 · see citing works
Mitochondrial Dynamics in Mammals
Chen, H., & Chan, D. C. (2004) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(04)59005-1 · Cited by 180 · see citing works
Morphological dynamics of mitochondria — A special emphasis on cardiac muscle cells
Hom, J., & Sheu, S. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.02.023 · Cited by 179 · see citing works
Chang, C., Manlandro, C. M., Arnoult, D., Stadler, J., Posey, A. E., Hill, R. B., & Blackstone, C. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.142430 · Cited by 180 · see citing works
Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1
Yu, T., Fox, R. J., Burwell, L. S., & Yoon, Y. (2005) · Journal of Cell Science · doi:10.1242/jcs.02537 · Cited by 172 · see citing works
Self-citationDynamin‐related proteins and Pex11 proteins in peroxisome division and proliferation
Thoms, S., & Erdmann, R. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04939.x · Cited by 169 · see citing works
A Role for the Ancient SNARE Syntaxin 17 in Regulating Mitochondrial Division
Arasaki, K., Shimizu, H., Mogari, H., Nishida, N., Hirota, N., Furuno, A., Kudo, Y., Baba, M., Baba, N., Cheng, J., et al. (2015) · Developmental Cell · doi:10.1016/j.devcel.2014.12.011 · Cited by 167 · see citing works
A dimeric equilibrium intermediate nucleates Drp1 reassembly on mitochondrial membranes for fission
Macdonald, P. J., Stepanyants, N., Mehrotra, N., Mears, J. A., Qi, X., Sesaki, H., & Ramachandran, R. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-02-0728 · Cited by 163 · see citing works
6-Hydroxydopamine (6-OHDA) induces Drp1-dependent mitochondrial fragmentation in SH-SY5Y cells
Gómez-Lázaro, M., Bonekamp, N. A., Galindo, M. F., Jordán, J., & Schrader, M. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.009 · Cited by 162 · see citing works
Bossy, B., Petrilli, A. M., Klinglmayr, E., Chen, J., Lütz‐Meindl, U., Knott, A. B., Masliah, E., Schwarzenbacher, R., & Bossy‐Wetzel, E. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100552 · Cited by 162 · see citing works
Functional and morphological impact of ER stress on mitochondria
Vannuvel, K., Renard, P., Raes, M. J., & Arnould, T. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24360 · Cited by 155 · see citing works
Mitochondrial morphology—emerging role in bioenergetics
Galloway, C. A., Lee, H., & Yoon, Y. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.035 · Cited by 150 · see citing works
Self-citationSantel, A., & Frank, S. (2008) · IUBMB Life · doi:10.1002/iub.71 · Cited by 147 · see citing works
Fis1, DLP1, and Pex11p coordinately regulate peroxisome morphogenesis
Kobayashi, S., Tanaka, A., & Fujiki, Y. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.02.028 · Cited by 145 · see citing works
Mitochondrial outer membrane permeabilization during apoptosis: The role of mitochondrial fission
Landes, T., & Martinou, J. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.01.021 · Cited by 140 · see citing works
Koch, A., Schneider, G., Lüers, G. H., & Schrader, M. (2004) · Journal of Cell Science · doi:10.1242/jcs.01268 · Cited by 144 · see citing works
Hom, J., Gewandter, J. S., Michael, L., Sheu, S., & Yoon, Y. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21051 · Cited by 142 · see citing works
Self-citationMitochondrial Morphology in Metabolic Diseases
Galloway, C. A., & Yoon, Y. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4779 · Cited by 141 · see citing works
Self-citationThe many shapes of mitochondrial death
Cereghetti, G. M., & Scorrano, L. (2006) · Oncogene · doi:10.1038/sj.onc.1209605 · Cited by 140 · see citing works
Mitochondrial Dynamics and Apoptosis—the ER Connection
Hoppins, S. C., & Nunnari, J. M. (2012) · Science · doi:10.1126/science.1224709 · Cited by 135 · see citing works
Mitochondria and peroxisomes: Are the ‘Big Brother’ and the ‘Little Sister’ closer than assumed?
Schrader, M., & Yoon, Y. (2007) · BioEssays · doi:10.1002/bies.20659 · Cited by 136 · see citing works
Self-citationAccola, M. A., Huang, B. Q., Masri, A. A., & McNiven, M. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201641200 · Cited by 135 · see citing works
Self-citationEndoplasmic 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
Shared components of mitochondrial and peroxisomal division
Schrader, M. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.01.004 · Cited by 134 · see citing works
The molecular mechanism and cellular functions of mitochondrial division
Lackner, L. L., & Nunnari, J. M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.11.011 · Cited by 133 · see citing works
Mcl-1 involvement in mitochondrial dynamics is associated with apoptotic cell death
Morciano, G., Giorgi, C., Balestra, D., Marchi, S., Perrone, D., Pinotti, M., & Pinton, P. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-01-0028 · Cited by 127 · see citing works
Sever, S. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00347-2 · Cited by 129 · see citing works
Boscolo, A., Milanović, D., Starr, J. A., Sanchez, V., Oklopcic, A., Moy, L., Ori, C., Erişir, A., & Jevtović‐Todorović, V. (2013) · Anesthesiology · doi:10.1097/aln.0b013e318289bc9b · Cited by 128 · see citing works
Mitochondrial Dynamics: Functional Link with Apoptosis
Otera, H., & Mihara, K. (2012) · International Journal of Cell Biology · doi:10.1155/2012/821676 · Cited by 128 · see citing works
Regulation of mitochondrial fission by intracellular Ca2+ in rat ventricular myocytes
Hom, J., Yu, T., Yoon, Y., Porter, G. A., Jr., & Sheu, S. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.03.018 · Cited by 128 · see citing works
Self-citationHuang, P., Galloway, C. A., & Yoon, Y. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020655 · Cited by 124 · see citing works
Self-citationWu, D., Dasgupta, A., Chen, K., Neuber‐Hess, M. S., Patel, J. J., Hurst, T. E., Mewburn, J. D., Lima, P. D. A., Alizadeh, E., Martin, A. Y., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201901467r · Cited by 123 · see citing works
- Authors
- Yoon, Y., Pitts, K. R., & McNiven, M. A.
- Affiliations
- Mayo Clinic (US)
- Venue
- Molecular Biology of the Cell
- Published
- 2001-09
- Volume
- 12
- Issue
- 9
- Pages
- 2894-2905
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC59722
- OpenAlex
- W2124540225
- Cited by
- 285
- References
- 36
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 5 · 2023: 5 · 2022: 4 · 2021: 9 · 2020: 8 · 2019: 12 · 2018: 10 · 2017: 14 · 2016: 12 · 2015: 14 · 2014: 11 · 2013: 15 · 2012: 16
- FWCI
- 3.40
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5k01dk002648-03)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK44650, DK 02648, R37DK044650, R01DK044650)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- dynamin-like protein, membrane tubulation, GTPase activity, GTP hydrolysis, GTP gamma S, membrane remodeling, mitochondrial distribution, cytoplasmic aggregates, liposome deformation
- MeSH terms
- Animals, Cell Line, Cell Membrane, Guanosine Triphosphate, Cricetinae, Hydrolysis, Liposomes, Mammals, Membrane Fusion, Microscopy, Electron, Microscopy, Fluorescence, Microtubule-Associated Proteins, Proteins, Time Factors, Amino Acid Substitution, GTP Phosphohydrolases, Mitochondrial Proteins, Dynamins
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
