Mitochondrial Trafficking in Neurons
Open accessAbstract
Neurons, perhaps more than any other cell type, depend on mitochondrial trafficking for their survival. Recent studies have elucidated a motor/adaptor complex on the mitochondrial surface that is shared between neurons and other animal cells. In addition to kinesin and dynein, this complex contains the proteins Miro (also called RhoT1/2) and milton (also called TRAK1/2) and is responsible for much, although not necessarily all, mitochondrial movement. Elucidation of the complex has permitted inroads for understanding how this movement is regulated by a variety of intracellular signals, although many mysteries remain. Regulating mitochondrial movement can match energy demand to energy supply throughout the extraordinary architecture of these cells and can control the clearance and replenishing of mitochondria in the periphery. Because the extended axons of neurons contain uniformly polarized microtubules, they have been useful for studying mitochondrial motility in conjunction with biochemical assays in many cell types.
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MECA functions to sustain mitochondria in regions with elevated demand for mitochondrial activity, influencing the quantity and quality of mitochondria inherited by daughter cells.
“MECA functions to sustain mitochondria in regions with elevated demand for mitochondrial activity, thereby influencing the quantity and quality of mitochondria inherited by daughter cells [31].”
From Mitochondrial anchor protein Num11 is key to pathogenicity of <i>Candida albicans</i> by affecting mitochondrial function and cell wall masking (2025) · cites this paper as [31]
The Summary (page unavailable) says neuronal trafficking machinery retains mitochondria where calcium buffering and energy production are in high demand. It identifies milton and Miro, not MECA, as part of that machinery. The paper discusses postmitotic neurons and does not support the claim about the quantity or quality of mitochondria inherited by daughter cells. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe cellular distribution of mitochondria is controlled both by their translocation along the microtubule system and by their retention at specific metabolically active sites within the cell.
“The cellular distribution of mitochondria is controlled both by their translocation along the microtubule system and by their retention at specific metabolic active sites within the cell [137].”
From RhoA Signaling in Neurodegenerative Diseases (2022) · cites this paper as [137]
MECA in S. cerevisiae is a critical structure that links mitochondria with the endoplasmic reticulum and plasma membrane.
“Notably, research has identified the mitochondria-endoplasmic reticulum-cortex anchor (MECA) in S. cerevisiae as a critical structure that links mitochondria with the endoplasmic reticulum and plasma membrane [31].”
From Mitochondrial anchor protein Num11 is key to pathogenicity of <i>Candida albicans</i> by affecting mitochondrial function and cell wall masking (2025) · cites this paper as [31]
The section on the motor/adaptor complex discusses Miro and milton in neuronal mitochondrial transport and briefly mentions the yeast protein Gem1p. Searches for MECA and for a yeast mitochondrial tether to the endoplasmic reticulum and plasma membrane found no passage addressing the claimed structure or its function. (LLM, conf=0.74)
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Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227 · see citing works
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in <i>PINK1</i>
Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481 · see citing works
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273 · see citing works
Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)
Kimura, K., Ito, M., Amano, M., Chihara, K., Fukata, Y., Nakafuku, M., Yamamori, B., Feng, J., Nakano, T., Okawa, K., et al. (1996) · Science · doi:10.1126/science.273.5272.245 · Cited by 2,889 · see citing works
The Molecular Motor Toolbox for Intracellular Transport
Vale, R. D. (2003) · Cell · doi:10.1016/s0092-8674(03)00111-9 · Cited by 1,982 · see citing works
Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
Clark, I. E., Dodson, M. W., Jiang, C., Cao, J. H., Huh, J. R., Seol, J. H., Yoo, S. J., Hay, B. A., & Guo, M. (2006) · Nature · doi:10.1038/nature04779 · Cited by 1,788 · see citing works
Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
Park, J., Lee, S. B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.-M., et al. (2006) · Nature · doi:10.1038/nature04788 · Cited by 1,705 · see citing works
Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572 · see citing works
Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369 · see citing works
Mitochondrial pathology and apoptotic muscle degeneration in <i>Drosophila parkin</i> mutants
Greene, J. C., Whitworth, A. J., Kuo, I., Andrews, L. A., Feany, M. B., & Pallanck, L. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0737556100 · Cited by 1,203 · see citing works
The axonal transport of mitochondria
Saxton, W. M., & Hollenbeck, P. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.053850 · Cited by 1,198 · see citing works
Gauthier, L. R., Charrin, B. C., Borrell-Pagès, M., Dompierre, J. P., Rangone, H., Cordelières, F. P., De Mey, J., MacDonald, M. E., Leßmann, V., Humbert, S., et al. (2004) · Cell · doi:10.1016/j.cell.2004.06.018 · Cited by 1,178 · see citing works
PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility
Wang, X., Winter, D., Ashrafi, G., Schlehe, J. S., Wong, Y. L., Selkoe, D. J., Rice, S. E., Steen, J. A. J., LaVoie, M. J., & Schwarz, T. L. (2011) · Cell · doi:10.1016/j.cell.2011.10.018 · Cited by 1,161 · see citing works
Self-citationBroad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy
Chan, N. C., Salazar, A. M., Pham, A. H., Sweredoski, M. J., Kolawa, N. J., Graham, R. L. J., Hess, S., & Chan, D. C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr048 · Cited by 993 · see citing works
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 · see citing works
The PINK1/Parkin pathway regulates mitochondrial morphology
Poole, A. C., Thomas, R. E., Andrews, L. A., McBride, H. M., Whitworth, A. J., & Pallanck, L. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709336105 · Cited by 885 · see citing works
The Mechanism of Ca2+-Dependent Regulation of Kinesin-Mediated Mitochondrial Motility
Wang, X., & Schwarz, T. L. (2009) · Cell · doi:10.1016/j.cell.2008.11.046 · Cited by 871 · see citing works
Self-citationWatanabe, N., Madaule, P., Reid, T., Ishizaki, T., Watanabe, G., Kakizuka, A., Saito, Y., Nakao, K., Jockusch, B. M., & Narumiya, S. (1997) · The EMBO Journal · doi:10.1093/emboj/16.11.3044 · Cited by 823 · see citing works
Yang, Y., Gehrke, S., Imai, Y., Huang, Z., Ouyang, Y., Wang, J.-W., Yang, L., Beal, M. F., Vogel, H., & Lu, B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602493103 · Cited by 798 · see citing works
The axonal transport of mitochondria
Hollenbeck, P. J., & Saxton, W. M. (2005) · Journal of Cell Science · doi:10.1242/jcs.02745 · Cited by 771 · see citing works
Role of Axonal Transport in Neurodegenerative Diseases
Vos, K. J. D., Grierson, A. J., Ackerley, S., & Miller, C. C. J. (2008) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.31.061307.090711 · Cited by 734 · see citing works
Miro1 Is a Calcium Sensor for Glutamate Receptor-Dependent Localization of Mitochondria at Synapses
MacAskill, A. F., Rinholm, J. E., Twelvetrees, A. E., Arancibia‐Cárcamo, I. L., Muir, J., Fransson, Å., Aspenström, P., Attwell, D., & Kittler, J. T. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.030 · Cited by 677 · see citing works
Hirokawa, N. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.94.1.129 · Cited by 676 · see citing works
Glater, E. E., Megeath, L. J., Stowers, R. S., & Schwarz, T. L. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601067 · Cited by 667 · see citing works
Self-citationTanaka, Y., Kanai, Y., Okada, Y., Nonaka, S., Takeda, S., Harada, A., & Hirokawa, N. (1998) · Cell · doi:10.1016/s0092-8674(00)81459-2 · Cited by 654 · see citing works
Axonal Transport of Mitochondria to Synapses Depends on Milton, a Novel Drosophila Protein
Stowers, R. S., Megeath, L. J., Górska‐Andrzejak, J., Meinertzhagen, I. A., & Schwarz, T. L. (2002) · Neuron · doi:10.1016/s0896-6273(02)01094-2 · Cited by 643 · see citing works
Self-citationMisko, A. L., Jiang, S., Wegorzewska, I., Milbrandt, J., & Baloh, R. H. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.6248-09.2010 · Cited by 643 · see citing works
The GTPase dMiro Is Required for Axonal Transport of Mitochondria to Drosophila Synapses
Guo, X., Macleod, G. T., Wellington, A. J., Hu, F., Panchumarthi, S., Schoenfield, M., Marin, L., Charlton, M. P., Atwood, H. L., & Zinsmaier, K. E. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.027 · Cited by 619 · see citing works
KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria
Nangaku, M., Sato-Yoshitake, R., Okada, Y., Noda, Y., Takemura, R., Yamazaki, H., & Hirokawa, N. (1994) · Cell · doi:10.1016/0092-8674(94)90012-4 · Cited by 598 · see citing works
Kang, J.-S., Tian, J.-H., Pan, P.-Y., Zald, P., Li, C., Deng, C., & Sheng, Z.-H. (2008) · Cell · doi:10.1016/j.cell.2007.11.024 · Cited by 598 · see citing works
Kinesin-related gene unc-104 is required for axonal transport of synaptic vesicles in C. elegans
Hall, D. H., & Hedgecock, E. M. (1991) · Cell · doi:10.1016/0092-8674(91)90391-b · Cited by 564 · see citing works
Bidirectional Ca <sup>2+</sup> -dependent control of mitochondrial dynamics by the Miro GTPase
Saotome, M., Safiulina, D., Szabadkai, G., Das, S., Fransson, Å., Aspenstrom, P., Rizzuto, R., & Hajnóczky, G. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808953105 · Cited by 538 · see citing works
Axonal mitochondrial transport and potential are correlated
Miller, K. E., & Sheetz, M. P. (2004) · Journal of Cell Science · doi:10.1242/jcs.01130 · Cited by 512 · see citing works
The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking.
Fransson, S., Ruusala, A., & Aspenström, P. (2006) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2006.03.163 · Cited by 479 · see citing works
Control of mitochondrial motility and distribution by the calcium signal
Yi, M., Weaver, D., & Hajnóczky, G. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406038 · Cited by 476 · see citing works
TRAK/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendrites
van Spronsen, M., Mikhaylova, M., Lipka, J., Schlager, M. A., van den Heuvel, D. J., Kuijpers, M., Wulf, P. S., Keijzer, N., Demmers, J., Kapitein, L. C., et al. (2013) · Neuron · doi:10.1016/j.neuron.2012.11.027 · Cited by 450 · see citing works
The regulation of bidirectional mitochondrial transport is coordinated with axonal outgrowth
Morris, R. L., & Hollenbeck, P. J. (1993) · Journal of Cell Science · doi:10.1242/jcs.104.3.917 · Cited by 442 · see citing works
The Mitochondrial Fusion-Promoting Factor Mitofusin Is a Substrate of the PINK1/Parkin Pathway
Poole, A. C., Thomas, R. E., Yu, S., Vincow, E. S., & Pallanck, L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010054 · Cited by 440 · see citing works
Imaging axonal transport of mitochondria in vivo
Misgeld, T., Kerschensteiner, M., Bareyre, F. M., Burgess, R. W., & Lichtman, J. W. (2007) · Nature Methods · doi:10.1038/nmeth1055 · Cited by 419 · see citing works
Atypical Rho GTPases Have Roles in Mitochondrial Homeostasis and Apoptosis
Fransson, Å., Ruusala, A., & Aspenström, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208609200 · Cited by 392 · see citing works
Mitochondrial Trafficking to Synapses in Cultured Primary Cortical Neurons
Chang, D. T. W., Honick, A. S., & Reynolds, I. J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1012-06.2006 · Cited by 391 · see citing works
Desmin Cytoskeleton Linked to Muscle Mitochondrial Distribution and Respiratory Function
Milner, D. J., Mavroidis, M., Weisleder, N. L., & Capetanaki, Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1283 · Cited by 385 · see citing works
Hurd, D. D., & Saxton, W. M. (1996) · Genetics · doi:10.1093/genetics/144.3.1075 · Cited by 379 · see citing works
Liu, S., Sawada, T., Lee, S., Yu, W., Silverio, G., Alapatt, P., Millan, I., Shen, A., Saxton, W., Kanao, T., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002537 · Cited by 371 · see citing works
Mitochondrial ‘kiss‐and‐run’: interplay between mitochondrial motility and fusion–fission dynamics
Liu, X., Weaver, D., Shirihai, O. S., & Hajnóczky, G. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.255 · Cited by 344 · see citing works
Mitochondrial Quality Control Mediated by PINK1 and Parkin: Links to ParkinsonismPreprint
Narendra, D. P., Walker, J. E., & Youle, R. J. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011338 · Cited by 341 · see citing works
Moving Mitochondria: Establishing Distribution of an Essential Organelle
Frederick, R. L., & Shaw, J. M. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00644.x · Cited by 329 · see citing works
YONEKAWA, Y., Harada, A., Okada, Y., Funakoshi, T., Kanai, Y., Takei, Y., Terada, S., Noda, T., & Hirokawa, N. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.2.431 · Cited by 326 · see citing works
Glutamate Decreases Mitochondrial Size and Movement in Primary Forebrain Neurons
Rintoul, G. L., Filiano, A. J., Brocard, J. B., Kress, G. J., & Reynolds, I. J. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-21-07881.2003 · Cited by 326 · see citing works
Nerve Growth Factor Signaling Regulates Motility and Docking of Axonal Mitochondria
Chada, S. R., & Hollenbeck, P. J. (2004) · Current Biology · doi:10.1016/j.cub.2004.07.027 · Cited by 296 · see citing works
Weihofen, A., Craig, K. J. T., Ostaszewski, B. L., Cookson, M., & Selkoe, D. J. (2009) · Biochemistry · doi:10.1021/bi8019178 · Cited by 290 · see citing works
In situ localization of mitochondrial DNA replication in intact mammalian cells.
Davis, A. F., & Clayton, D. A. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.4.883 · Cited by 277 · see citing works
Pathogenic huntingtin inhibits fast axonal transport by activating JNK3 and phosphorylating kinesin
Morfini, G. A., You, Y., Pollema, S. L., Kaminska, A., Liu, K., Yoshioka, K., Björkblom, B., Coffey, E. T., Bagnato, C., Han, D. K. M., et al. (2009) · Nature Neuroscience · doi:10.1038/nn.2346 · Cited by 276 · see citing works
HDAC6 Regulates Mitochondrial Transport in Hippocampal Neurons
Chen, S., Owens, G. C., Makarenkova, H. P., & Edelman, D. B. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010848 · Cited by 270 · see citing works
A novel CDK5‐dependent pathway for regulating GSK3 activity and kinesin‐driven motility in neurons
Morfini, G. A., Szebenyi, G., Brown, H. J., Pant, H. C., Pigino, G. F., DeBoer, S. R., Beffert, U., & Brady, S. T. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600237 · Cited by 268 · see citing works
Quantitative imaging of energy expenditure in human brain
Zhu, X., Qiao, H., Du, F., Xiong, Q., Liu, X., Zhang, X., Uǧurbil, K., & Chen, W. (2012) · NeuroImage · doi:10.1016/j.neuroimage.2012.02.013 · Cited by 267 · see citing works
Local translation of extranuclear lamin B promotes axon maintenance
Yoon, B. C., Jung, H., Dwivedy, A., O'Hare, C. M., Zivraj, K. H., & Holt, C. E. (2012) · Cell · doi:10.1016/j.cell.2011.11.064 · Cited by 263 · see citing works
Mitochondrial GTPase mitofusin 2 mutation in Charcot?Marie?Tooth neuropathy type 2A
Kijima, K., Numakura, C., Izumino, H., Umetsu, K., Nezu, A., Shiiki, T., Ogawa, M., Ishizaki, Y., Kitamura, T., Shozawa, Y., et al. (2004) · Human Genetics · doi:10.1007/s00439-004-1199-2 · Cited by 251 · see citing works
Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway
Frederick, R. L., McCaffery, J. M., Cunningham, K. W., Okamoto, K., & Shaw, J. M. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200405100 · Cited by 247 · see citing works
MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons
Mandelkow, E.-M., Thies, E., Trinczek, B., Biernat, J., & Mandelkow, E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401085 · Cited by 236 · see citing works
Syntabulin-mediated anterograde transport of mitochondria along neuronal processes
Cai, Q., Gerwin, C. M., & Sheng, Z. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200506042 · Cited by 230 · see citing works
<i>Drosophila</i>Miro Is Required for Both Anterograde and Retrograde Axonal Mitochondrial Transport
Russo, G. J., Louie, K., Wellington, A., Macleod, G. T., Hu, F., Panchumarthi, S., & Zinsmaier, K. E. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.5417-08.2009 · Cited by 217 · see citing works
Human Myo19 Is a Novel Myosin that Associates with Mitochondria
Quintero, O. A., DiVito, M. M., Adikes, R. C., Kortan, M. B., Case, L. B., Lier, A., Panaretos, N. S., Slater, S. Q., Rengarajan, M., Feliu, M., et al. (2009) · Current Biology · doi:10.1016/j.cub.2009.10.026 · Cited by 204 · see citing works
Mitochondrial dynamics and Ca2+ signaling
Szabadkai, G., Simoni, A. M., Bianchi, K., Stefani, D. D., Leo, S., Wieckowski, M. R., & Rizzuto, R. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.04.002 · Cited by 204 · see citing works
Mitochondrial movement and positioning in axons: the role of growth factor signaling
Chada, S. R., & Hollenbeck, P. J. (2003) · Journal of Experimental Biology · doi:10.1242/jeb.00263 · Cited by 202 · see citing works
JNK mediates pathogenic effects of polyglutamine-expanded androgen receptor on fast axonal transport
Morfini, G. A., Pigino, G. F., Szebenyi, G., You, Y., Pollema, S. L., & Brady, S. T. (2006) · Nature Neuroscience · doi:10.1038/nn1717 · Cited by 198 · see citing works
Evidence That Myosin Activity Opposes Microtubule-Based Axonal Transport of Mitochondria
Pathak, D., Sepp, K. J., & Hollenbeck, P. J. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1621-10.2010 · Cited by 188 · see citing works
Ohno, N., Kidd, G. J., Mahad, D., Kiryu‐Seo, S., Avishai, A., Komuro, H., & Trapp, B. D. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0095-11.2011 · Cited by 187 · see citing works
Barkus, R. V., Klyachko, O., Horiuchi, D., Dickson, B. J., & Saxton, W. M. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-03-0261 · Cited by 185 · see citing works
A Drosophila kinesin required for synaptic bouton formation and synaptic vesicle transport
Pack-Chung, E., Kurshan, P. T., Dickman, D. K., & Schwarz, T. L. (2007) · Nature Neuroscience · doi:10.1038/nn1936 · Cited by 183 · see citing works
Self-citationMechanisms of Mitochondria-Neurofilament Interactions
Wagner, O. I., Lifshitz, J., Janmey, P. A., Lindén, M., McIntosh, T. K., & Leterrier, J. F. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-27-09046.2003 · Cited by 179 · see citing works
Brickley, K., & Stephenson, F. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.236018 · Cited by 176 · see citing works
Taking Rho GTPases to the next level: The cellular functions of atypical Rho GTPases
Aspenström, P., Ruusala, A., & Pacholsky, D. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.07.022 · Cited by 172 · see citing works
GRIF-1 and OIP106, Members of a Novel Gene Family of Coiled-Coil Domain Proteins
Brickley, K., Smith, M. J., Beck, M., & Stephenson, F. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409095200 · Cited by 168 · see citing works
Iyer, S. P. N., Akimoto, Y., & Hart, G. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209384200 · Cited by 163 · see citing works
Mitochondrial biogenesis in the axons of vertebrate peripheral neurons
Amiri, M., & Hollenbeck, P. J. (2008) · Developmental Neurobiology · doi:10.1002/dneu.20668 · Cited by 161 · see citing works
Association of Mitochondria with Plectin and Desmin Intermediate Filaments in Striated Muscle
Reipert, S. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4626 · Cited by 157 · see citing works
Vimentin intermediate filaments modulate the motility of mitochondria
Nekrasova, O. E., Mendez, M. G., Chernoivanenko, I. S., Tyurin‐Kuzmin, P. A., Kuczmarski, E. R., Gelfand, V. I., Goldman, R. D., & Minin, A. А. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-09-0766 · Cited by 151 · see citing works
Verburg, J., & Hollenbeck, P. J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2614-08.2008 · Cited by 150 · see citing works
The PINK1/Parkin pathway: a mitochondrial quality control system?
Whitworth, A. J., & Pallanck, L. J. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9253-3 · Cited by 136 · see citing works
High resolution imaging of live mitochondria
Jakobs, S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.04.004 · Cited by 133 · see citing works
Flying through the Drosophila Cytoskeletal Genome
Goldstein, L. S. B., & Gunawardena, S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.2.f63 · Cited by 132 · see citing works
Cho, K., Cai, Y., Yi, H., Yeh, A., Aslanukov, A., & Ferreira, P. A. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00647.x · Cited by 130 · see citing works
ADP Regulates Movements of Mitochondria in Neurons
Mironov, S. L. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.092981 · Cited by 129 · see citing works
Winter, L., Abrahamsberg, C., & Wiche, G. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200710151 · Cited by 128 · see citing works
Mitochondrial Dynamics and Peripheral Neuropathy
Baloh, R. H. (2007) · The Neuroscientist · doi:10.1177/1073858407307354 · Cited by 127 · see citing works
Rezniczek, G. A. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg345 · Cited by 123 · see citing works
Beck, M., Brickley, K., Wilkinson, H. L., Sharma, S., Smith, M. J., Chazot, P. L., Pollard, S., & Stephenson, F. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200438200 · Cited by 114 · see citing works
A Specific Light Chain of Kinesin Associates with Mitochondria in Cultured Cells
Khodjakov, A. L., Lizunova, E. M., Minin, A. А., Koonce, M. P., & Gyoeva, F. K. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.2.333 · Cited by 106 · see citing works
López‐Doménech, G., Serrat, R., Mirra, S., D’Aniello, S., Somorjai, I., Abad, A., Vitureira, N., García‐Arumí, E., Alonso, M. T., Rodríguez-Prados, M., et al. (2012) · Nature Communications · doi:10.1038/ncomms1829 · Cited by 106 · see citing works
Regulation of mitochondria distribution by RhoA and formins
Minin, A. A., Kulik, A. V., Gyoeva, F. K., Li, Y., Goshima, G., & Gelfand, V. I. (2006) · Journal of Cell Science · doi:10.1242/jcs.02762 · Cited by 102 · see citing works
Milton controls the early acquisition of mitochondria byDrosophilaoocytes
Cox, R. T., & Spradling, A. C. (2006) · Development · doi:10.1242/dev.02514 · Cited by 101 · see citing works
O-GlcNAc cycling: Implications for neurodegenerative disorders
Lazarus, B. D., Love, D. C., & Hanover, J. A. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.03.008 · Cited by 99 · see citing works
HUMMR, a hypoxia- and HIF-1α–inducible protein, alters mitochondrial distribution and transport
Li, Y., Lim, S., Hoffman, D. L., Aspenström, P., Federoff, H. J., & Rempe, D. A. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200811033 · Cited by 96 · see citing works
The novel protein KBP regulates mitochondria localization by interaction with a kinesin-like protein
Wozniak, M. J., Melzer, M., Dorner, C., Häring, H., & Lammers, R. (2005) · BMC Cell Biology · doi:10.1186/1471-2121-6-35 · Cited by 91 · see citing works
Lyons, D. A., Naylor, S. G., Mercurio, S., Dominguez, C. X., & Talbot, W. S. (2008) · Development · doi:10.1242/dev.012377 · Cited by 91 · see citing works
Dynein Light Chain LC8 Regulates Syntaphilin-Mediated Mitochondrial Docking in Axons
Chen, Y., Gerwin, C. M., & Sheng, Z. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1472-09.2009 · Cited by 88 · see citing works
Local synthesis of nuclear‐encoded mitochondrial proteins in the presynaptic nerve terminal
Gioio, A. E., Eyman, M., Zhang, H., Lavina, Z. S., Giuditta, A., & Kaplan, B. B. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1096 · Cited by 85 · see citing works
Smith, M. J., Pozo, K., Brickley, K., & Stephenson, F. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600522200 · Cited by 82 · see citing works
Górska‐Andrzejak, J., Stowers, R. S., Borycz, J. A., et al. (2003) · The Journal of Comparative Neurology · doi:10.1002/cne.10750 · Cited by 79 · see citing works
Tanaka, K., Sugiura, Y., Ichishita, R., Mihara, K., & Oka, T. (2011) · Journal of Cell Science · doi:10.1242/jcs.086470 · Cited by 79 · see citing works
Tao, G., Looi, K., Toivola, D. M., Strnad, P., Zhou, Q., Liao, J., Wei, Y., Habtezion, A., & Omary, M. B. (2009) · Journal of Cell Science · doi:10.1242/jcs.051862 · Cited by 77 · see citing works
Fujita, T., Maturana, A. D., Ikuta, J., et al. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.07.050 · Cited by 74 · see citing works
Ratner, N., Bloom, G. S., & Brady, S. T. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-19-07717.1998 · Cited by 73 · see citing works
Regulation of axonal trafficking of cytochrome c oxidase IV mRNA
Aschrafi, A., Natera-Naranjo, O., Gioio, A. E., & Kaplan, B. B. (2010) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2010.01.009 · Cited by 72 · see citing works
Ikuta, J., Maturana, A. D., Fujita, T., Okajima, T., Tatematsu, K., Tanizawa, K., & Kuroda, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.11.142 · Cited by 70 · see citing works
Stürmer, K., Baumann, O., & Walz, B. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.6.2273 · Cited by 62 · see citing works
Becker, C. G., & Becker, T. (2000) · The Journal of Comparative Neurology · doi:10.1002/1096-9861(20001120)427:3 · Cited by 61 · see citing works
Kugelberg, E. (2014) · Nature reviews. Immunology · doi:10.1038/nri3628 · Cited by 58 · see citing works
Grishin, A., Li, H., Levitan, E. S., & Zaks-Makhina, E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602439200 · Cited by 48 · see citing works
GRIF1 binds Hrs and is a new regulator of endosomal trafficking
Kirk, E., Chin, L., & Li, L. (2006) · Journal of Cell Science · doi:10.1242/jcs.03249 · Cited by 39 · see citing works
Yang, Z., & Steele, D. S. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.00029.x · Cited by 37 · see citing works
Mironov, S. L. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.04.009 · Cited by 36 · see citing works
Pozo, K. B. K., & Stephenson, F. A. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.10.011 · Cited by 36 · see citing works
Bittar, H. E. T., Lecuona, E., Grillo, D., Szleifer, I. G., Nekrasova, O. E., Gelfand, V. I., & Sznajder, J. I. (2009) · The FASEB Journal · doi:10.1096/fj.09-137802 · Cited by 19 · see citing works
Axonal Transport: CDKs as Traffic Signals for Motor-ists along the Axon?
Holzbaur, E. L. F. (2010) · Current Biology · doi:10.1016/j.cub.2010.06.016 · Cited by 6 · see citing works
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Mitochondrial dynamics in adaptive and maladaptive cellular stress responses
Eisner, V., Picard, M., & Hajnóczky, G. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0133-0 · Cited by 622 · see citing works
A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation
Li, X., Rydzewski, N., Hider, A., Zhang, X., Yang, J., Wang, W., Gao, Q., Cheng, X., & Xu, H. (2016) · Nature Cell Biology · doi:10.1038/ncb3324 · Cited by 387 · see citing works
Glycolytic enzymes localize to synapses under energy stress to support synaptic function
Jang, S., Nelson, J. C., Bend, E. G., Rodríguez-Laureano, L., Tueros, F. G., Cartagenova, L., Underwood, K., Jorgensen, E. M., & Colón-Ramos, D. A. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.011 · Cited by 270 · see citing works
RhoA Signaling in Neurodegenerative Diseases
Schmidt, S. I., Blaabjerg, M., Freude, K., & Meyer, M. (2022) · Cells · doi:10.3390/cells11091520 · Cited by 110 · see citing works
A PGAM5–KEAP1–Nrf2 complex is required for stress-induced mitochondrial retrograde trafficking
O'Mealey, G. B., Plafker, K. S., Berry, W. L., Janknecht, R., Chan, J. Y., & Plafker, S. M. (2017) · Journal of Cell Science · doi:10.1242/jcs.203216 · Cited by 99 · see citing works
Mitochondrial Dysfunctions: A Red Thread across Neurodegenerative Diseases
Stanga, S., Caretto, A., Boido, M., & Vercelli, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103719 · Cited by 90 · see citing works
Decreased sirtuin deacetylase activity in LRRK2 G2019S iPSC-derived dopaminergic neurons
Schwab, A. J., Sison, S. L., Meade, M. R., Broniowska, K. A., Corbett, J. A., & Ebert, A. D. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.10.010 · Cited by 80 · see citing works
BDNF pro-peptide regulates dendritic spines via caspase-3
Guo, J., Ji, Y., Ding, Y., Jiang, W., Sun, Y., Lu, B., & Nagappan, G. (2016) · Cell Death & Disease · doi:10.1038/cddis.2016.166 · Cited by 76 · see citing works
Mitochondrial dynamic abnormalities in amyotrophic lateral sclerosis
Jiang, Z., Wang, W., Perry, G., Zhu, X., & Wang, X. (2015) · Translational Neurodegeneration · doi:10.1186/s40035-015-0037-x · Cited by 66 · see citing works
Distribution and Apoptotic Function of Outer Membrane Proteins Depend on Mitochondrial Fusion
Weaver, D., Eisner, V., Liu, X., Várnai, P., Hunyady, L., Gross, A., & Hajnóczky, G. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.048 · Cited by 58 · see citing works
Yang, G., Niu, X., Zhuang, T., Zhu, X., Xu, Q., Wang, H., Shao, J., Wang, C., Yang, Y., Wang, T., et al. (2025) · Virulence · doi:10.1080/21505594.2025.2519149 · Cited by 4 · see citing works
“MECA functions to sustain mitochondria in regions with elevated demand for mitochondrial activity, thereby influencing the quantity and quality of mitochondria inherited by daughter cells [31].”
- Authors
- Schwarz, T. L.
- Affiliations
- Boston Children's Hospital (US)
- Corresponding author
- Schwarz, T. L.
- ORCID
- Schwarz, T. L.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2013-06-01
- Volume
- 5
- Issue
- 6
- Pages
- a011304-a011304
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC3660831
- OpenAlex
- W2131454864
- Cited by
- 525
- References
- 116
- Citations by year
- 2026: 16 · 2025: 20 · 2024: 28 · 2023: 43 · 2022: 40 · 2021: 53 · 2020: 55 · 2019: 54 · 2018: 53 · 2017: 52 · 2016: 39 · 2015: 35 · 2014: 30 · 2013: 5 · 2012: 1
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial trafficking, neurons, mitochondrial motility, Miro, John Milton, kinesin, dynein, axons, microtubule polarity, energy demand, mitochondrial clearance
- MeSH terms
- Biological Transport, Calcium, Microtubules, Mitochondria, Neurons, Mitochondrial Proteins, Adaptor Proteins, Vesicular Transport
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