Mitochondrial matrix Ca 2 + as an intrinsic signal regulating mitochondrial motility in axons
Open accessAbstract
The proper distribution of mitochondria is particularly vital for neurons because of their polarized structure and high energy demand. Mitochondria in axons constantly move in response to physiological needs, but signals that regulate mitochondrial movement are not well understood. Aside from producing ATP, Ca 2+ buffering is another main function of mitochondria. Activities of many enzymes in mitochondria are also Ca 2+ -dependent, suggesting that intramitochondrial Ca 2+ concentration is important for mitochondrial functions. Here, we report that mitochondrial motility in axons is actively regulated by mitochondrial matrix Ca 2+ . Ca 2+ entry through the mitochondrial Ca 2+ uniporter modulates mitochondrial transport, and mitochondrial Ca 2+ content correlates inversely with the speed of mitochondrial movement. Furthermore, the miro1 protein plays a role in Ca 2+ uptake into the mitochondria, which subsequently affects mitochondrial movement.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
Ca2+ is a key regulator of mitochondria motility and docking.
“it has been largely described that Ca2+ is a key regulator of mitochondria motility and docking44–49,107.”
From CYFIP1 governs the development of cortical axons by modulating calcium availability (2025) · cites this paper as [48]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter
Baughman, J. M., Perocchi, F., Girgis, H. S., Plovanich, M. E., Belcher-Timme, C. A., Sancak, Y., Bao, X., Strittmatter, L., Goldberger, O., Bogorad, R., et al. (2011) · Nature · doi:10.1038/nature10234 · Cited by 1,926 · see citing works
A high signal-to-noise Ca2+ probe composed of a single green fluorescent protein
Nakai, J., Ohkura, M., & Imoto, K. (2001) · Nature Biotechnology · doi:10.1038/84397 · Cited by 1,619 · see citing works
A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
Stefani, D. D., Raffaello, A., Teardo, E., Szabò, I., & Rizzuto, R. (2011) · Nature · doi:10.1038/nature10230 · Cited by 1,431 · see citing works
The mitochondrial calcium uniporter is a highly selective ion channel
Kirichok, Y., Krapivinsky, G., & Clapham, D. E. (2004) · Nature · doi:10.1038/nature02246 · Cited by 1,409 · see citing works
Role of calcium ions in regulation of mammalian intramitochondrial metabolism
McCormack, J. G., Halestrap, A. P., & Denton, R. M. (1990) · Physiological Reviews · doi:10.1152/physrev.1990.70.2.391 · Cited by 1,398 · 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
Mitochondria in neuroplasticity and neurological disorders
Mattson, M. P., Gleichmann, M., & Cheng, A. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.010 · Cited by 1,081 · see citing works
MICU1 encodes a mitochondrial EF hand protein required for Ca2+ uptake
Perocchi, F., Gohil, V. M., Girgis, H. S., Bao, X. R., McCombs, J. E., Palmer, A. E., & Mootha, V. K. (2010) · Nature · doi:10.1038/nature09358 · Cited by 881 · 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
Regulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming
Jouaville, L. S., Pinton, P., Bastianutto, C., Rutter, G. A., & Rizzuto, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13807 · Cited by 814 · 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
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
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
Mitochondria: The Hub of Cellular Ca2+Signaling
Szabadkai, G., & Duchen, M. R. (2008) · Physiology · doi:10.1152/physiol.00046.2007 · Cited by 403 · 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
Control of mitochondrial transport and localization in neurons
MacAskill, A. F., & Kittler, J. T. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.11.002 · Cited by 372 · see citing works
Calcium homeostasis, selective vulnerability and Parkinson's disease
Chan, C. S., Gertler, T. S., & Surmeier, D. J. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2009.01.006 · Cited by 239 · see citing works
Mitochondrial trafficking and morphology in healthy and injured neurons
Chang, D. T. W., & Reynolds, I. J. (2006) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.09.003 · Cited by 228 · see citing works
The pattern and mechanism of mitochondrial transport in axons
Hollenbeck, P. J. (1996) · Frontiers in bioscience · doi:10.2741/a118 · Cited by 219 · 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
Verburg, J., & Hollenbeck, P. J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2614-08.2008 · Cited by 150 · see citing works
Mitochondrial transport and docking in axons
Cai, Q., & Sheng, Z. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.03.024 · Cited by 105 · see citing works
Single fluorescent protein-based Ca2+sensors with increased dynamic range
Souslova, E. A., Belousov, V. V., Lock, J. G., Strömblad, S., Kasparov, S., Bolshakov, A. P., Pinelis, V. G., Labas, Y. A., Lukyanov, S., Mayr, L. M., et al. (2007) · BMC Biotechnology · doi:10.1186/1472-6750-7-37 · Cited by 104 · see citing works
The Miro GTPases: At the heart of the mitochondrial transport machinery
Reis, K., Fransson, Å., & Aspenström, P. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.04.015 · Cited by 98 · see citing works
García‐Rivas, G., Guerrero-Hernández, A., Guerrero‐Serna, G., Rodríguez‐Zavala, J. S., & Zazueta, C. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04771.x · Cited by 98 · see citing works
Plasticity of Mitochondrial Calcium Signaling
Csordás, G., & Hajnóczky, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305248200 · Cited by 88 · see citing works
Montero, M., Lobatón, C. D., Moreno, A., & Álvarez, J. (2002) · The FASEB Journal · doi:10.1096/fj.02-0553fje · Cited by 81 · see citing works
Mitochondrial Calcium Homeostasis: Mechanisms and Molecules
Vandecasteele, G., Szabadkai, G., & Rizzuto, R. (2001) · IUBMB Life · doi:10.1080/15216540152846028 · Cited by 67 · 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
Vay, L., Hernández‐SanMiguel, E., Domingo, J. S., Lobatón, C. D., Moreno, A., Montero, M., & Álvarez, J. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2006.126391 · Cited by 51 · see citing works
Karahashi, H., Nagata, K., Ishii, K., & Amano, F. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00045-4 · Cited by 36 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Mitochondria as sensors and regulators of calcium signalling
Rizzuto, R., De Stefani, D., Raffaello, A., & Mammucari, C. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3412 · Cited by 1,781 · see citing works
Synaptic Energy Use and Supply
Harris, J. J., Jolivet, R., & Attwell, D. (2012) · Neuron · doi:10.1016/j.neuron.2012.08.019 · Cited by 1,747 · see citing works
Mitochondrial transport in neurons: impact on synaptic homeostasis and neurodegeneration
Sheng, Z., & Cai, Q. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3156 · Cited by 906 · see citing works
Mitochondria at the neuronal presynapse in health and disease
Devine, M. J., & Kittler, J. T. (2018) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.170 · Cited by 615 · see citing works
Ahmad, T., Mukherjee, S., Pattnaik, B., Kumar, M., Singh, S., Kumar, M., Rehman, R., Tiwari, B. K., Jha, K. A., Barhanpurkar, A. P., et al. (2014) · The EMBO Journal · doi:10.1002/embj.201386030 · Cited by 542 · see citing works
Mitochondria-lysosome contacts regulate mitochondrial Ca 2+ dynamics via lysosomal TRPML1
Peng, W., Wong, Y. C., & Krainc, D. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2003236117 · Cited by 342 · see citing works
Trushina, E. V., Nemutlu, E., Zhang, S., Christensen, T. A., Camp, J. J., Mesa, J., Siddiqui, A., Tamura, Y., Sesaki, H., Wengenack, T. M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032737 · Cited by 268 · see citing works
Babenko, V., Silachev, D., Popkov, V., Zorova, L., Pevzner, I., Plotnikov, E., Sukhikh, G., & Zorov, D. (2018) · Molecules · doi:10.3390/molecules23030687 · Cited by 242 · see citing works
Uittenbogaard, M. N., & Chiaramello, A. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140305224906 · Cited by 240 · see citing works
Lee, K., Huh, S., Lee, S., Wu, Z., Kim, A., Kang, H., & Lu, B. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1721136115 · Cited by 233 · see citing works
Nrf2 as a regulator of mitochondrial function: Energy metabolism and beyond
Esteras, N., & Abramov, A. Y. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.07.013 · Cited by 214 · see citing works
Mitochondria-associated membranes as hubs for neurodegeneration
Krols, M., Isterdael, G. V., Asselbergh, B., Kremer, A., Lippens, S., Timmerman, V., & Janssens, S. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1528-7 · Cited by 200 · see citing works
Constriction 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 Transfer in Cancer: A Comprehensive Review
Zampieri, L. X., Silva‐Almeida, C., Rondeau, J. D., & Sonveaux, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063245 · Cited by 173 · see citing works
Lewis, T. L., Turi, G. F., Kwon, S., Losonczy, A., & Polleux, F. (2016) · Current Biology · doi:10.1016/j.cub.2016.07.064 · Cited by 167 · see citing works
Filadi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., & Pizzo, P. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.013 · Cited by 170 · see citing works
Genetically Encoded Fluorescent Indicators for Organellar Calcium Imaging
Suzuki, J., Kanemaru, K., & Iino, M. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.04.054 · Cited by 151 · see citing works
New insights into the role of mitochondrial calcium homeostasis in cell migration
Paupe, V., & Prudent, J. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.05.039 · Cited by 142 · see citing works
ROS Control Mitochondrial Motility through p38 and the Motor Adaptor Miro/Trak
Debattisti, V., Gerencser, A. A., Saotome, M., Das, S., & Hajnóczky, G. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.060 · Cited by 132 · see citing works
Deacetylation of Miro1 by HDAC6 blocks mitochondrial transport and mediates axon growth inhibition
Kalinski, A. L., Kar, A. N., Craver, J., Tosolini, A. P., Sleigh, J. N., Lee, S. J., Hawthorne, A. L., Brito‐Vargas, P., Miller-Randolph, S., Passino, R., et al. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201702187 · Cited by 119 · see citing works
Miro-1 Links Mitochondria and Microtubule Dynein Motors To Control Lymphocyte Migration and Polarity
Morlino, G., Barreiro, O., Baixauli, F., Robles‐Valero, J., González, J. M., Villa‐Bellosta, R., Cuenca-Alba, J., Sorzano, C. Ó. S., Veiga, E., Martin-Cofreces, N. B., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01177-13 · Cited by 117 · see citing works
Mitochondrial trafficking in neurons and the role of the Miro family of GTPase proteins
Birsa, N., Norkett, R., Higgs, N., López‐Doménech, G., & Kittler, J. T. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130234 · Cited by 111 · see citing works
The Role of Impaired Mitochondrial Dynamics in MFN2-Mediated Pathology
Zaman, M., & Shutt, T. E. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.858286 · Cited by 113 · see citing works
The Role of Mitochondrial Calcium Homeostasis in Alzheimer’s and Related Diseases
Ryan, K. C., Ashkavand, Z., & Norman, K. R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239153 · Cited by 107 · see citing works
Suzuki, M., Danilchanka, O., & Mekalanos, J. J. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.09.015 · Cited by 104 · see citing works
Mesenchymal stem cell-mediated transfer of mitochondria: mechanisms and functional impact
Velarde, F., Ezquerra, S., Delbruyere, X., Caicedo, A., Hidalgo, Y., & Khoury, M. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04207-3 · Cited by 99 · see citing works
Su, B., Ji, Y.-S., Sun, X., Liu, X., & Chen, Z.-Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.526129 · Cited by 99 · see citing works
Jadiya, P., Garbincius, J. F., & Elrod, J. W. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01224-4 · Cited by 94 · see citing works
Wang, J., Li, H., Yao, Y., Zhao, T., Chen, Y., Shen, Y., Wang, L., & Zhu, Y. (2018) · Stem Cell Research & Therapy · doi:10.1186/s13287-018-0832-2 · Cited by 92 · see citing works
The ER-mitochondria interface, where Ca2+ and cell death meet
de Ridder, I., Kerkhofs, M., Lemos, F. O., Loncke, J., Bultynck, G., & Parys, J. B. (2023) · Cell Calcium · doi:10.1016/j.ceca.2023.102743 · Cited by 97 · see citing works
Cheng, H., Gang, X., He, G., Liu, Y., Wang, Y., Zhao, X. Y., & Wang, G. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.592129 · Cited by 88 · see citing works
Obashi, K., & Okabe, S. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12263 · Cited by 88 · see citing works
Großmann, D., Berenguer-Escuder, C., Bellet, M. E., Scheibner, D., Bohler, J., Massart, F., Rapaport, D., Skupin, A., d’Hérouël, A. F., Sharma, M., et al. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7718 · Cited by 84 · see citing works
Gómez-Valadés, A. G., Pozo, M., Varela, L., Boudjadja, M. B., Ramírez, S., Chivite, Í., Eyre, E., Haddad-Tóvolli, R., Obri, A., Milà‐Guasch, M., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.07.008 · Cited by 83 · see citing works
Role of Calcium Modulation in the Pathophysiology and Treatment of Alzheimer’s Disease
Baracaldo-Santamaría, D., Avendaño-Lopez, S. S., Ariza-Salamanca, D. F., Rodríguez-Giraldo, M., Calderón‐Ospina, C., González-Reyes, R. E., & Nava-Mesa, M. O. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24109067 · Cited by 85 · see citing works
Mitochondrial dynamics and their impact on T cell function
Quintana, A., & Hoth, M. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.02.005 · Cited by 82 · see citing works
Mitochondrial calcium at the synapse
Datta, S., & Jaiswal, M. (2021) · Mitochondrion · doi:10.1016/j.mito.2021.04.006 · Cited by 73 · see citing works
Mitochondrial Dynamics and Motility Inside Living Vascular Endothelial Cells: Role of Bioenergetics
Giedt, R. J., Pfeiffer, D. R., Anastasios Matzavinos, A., Kao, C., & Alevriadou, B. R. (2012) · Annals of Biomedical Engineering · doi:10.1007/s10439-012-0568-6 · Cited by 71 · see citing works
Sundar, I. K., Maremanda, K. P., & Rahman, I. (2019) · Toxicology Letters · doi:10.1016/j.toxlet.2019.09.022 · Cited by 68 · see citing works
Mitochondria: key players in the neurotoxic effects of amphetamines
Barbosa, D. J., Capela, J. P., Feio‐Azevedo, R., Gomes, A., Bastos, M. D. L., & Carvalho, F. D. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1478-9 · Cited by 69 · see citing works
Zheng, Y., Zhang, X., & Chen, Z. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13122 · Cited by 69 · see citing works
Liiv, M., Vaarmann, A., Safiulina, D., Choubey, V., Gupta, R., Kuum, M., Janickova, L., Hodurova, Z., Cagalinec, M., Zeb, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50502-x · Cited by 68 · see citing works
Mechanics of mitochondrial motility in neurons
Barnhart, E. L. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.02.022 · Cited by 68 · see citing works
Miro sculpts mitochondrial dynamics in neuronal health and disease
Devine, M. J., Birsa, N., & Kittler, J. T. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.12.008 · Cited by 67 · see citing works
The mitochondrial permeability transition pore in Ca2+ homeostasis
Carraro, M., & Bernardi, P. (2023) · Cell Calcium · doi:10.1016/j.ceca.2023.102719 · Cited by 64 · see citing works
Li, L., Nadanaciva, S., Berger, Z., Shen, W., Paumier, K. L., Schwartz, J. W., Mou, K., Loos, P., Milici, A. J., Dunlop, J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0085815 · Cited by 64 · see citing works
Altered synapses in a Drosophila model of Alzheimer's disease
Mhatre, S. D., Satyasi, V., Killen, M., Paddock, B. E., Moir, R. D., Saunders, A. J., & Marenda, D. R. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.012104 · Cited by 62 · see citing works
MCU Interacts with Miro1 to Modulate Mitochondrial Functions in Neurons
Niescier, R. F., Hong, K., Park, D., & Min, K. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0504-18.2018 · Cited by 60 · see citing works
Self-citationMacVicar, T., Mannack, L., Lees, R. M., & Lane, J. D. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160613356 · Cited by 56 · see citing works
Berenguer-Escuder, C., Großmann, D., Antony, P. M. A., Arena, G., Wasner, K., Massart, F., Jarazo, J., Walter, J., Schwamborn, J. C., Grünewald, A., et al. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa066 · Cited by 57 · see citing works
Live cell imaging of signaling and metabolic activities
Depaoli, M. R., Bischof, H., Eroğlu, E., Burgstaller, S., Ramadani‐Muja, J., Rauter, T., Schinagl, M., Waldeck‐Weiermair, M., Hay, J., Graier, W. F., et al. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.06.003 · Cited by 52 · see citing works
Berenguer-Escuder, C., Großmann, D., Massart, F., Antony, P. M. A., Burbulla, L. F., Glaab, E., Imhoff, S., Trinh, J., Seibler, P., Grünewald, A., et al. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8122226 · Cited by 52 · see citing works
Jørgensen, C., & Khoury, M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.606781 · Cited by 50 · see citing works
Geng, Z., Guan, S., Wang, S., Yu, Z., Liu, T., Du, S., & Zhu, C. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14344 · Cited by 48 · see citing works
Osteocyte mitochondria inhibit tumor development via STING-dependent antitumor immunity
Zhou, H., Zhang, W., Li, H., Xu, F., Yinwang, E., Xue, Y., Chen, T., Wang, S., Wang, Z., Sun, H., et al. (2024) · Science Advances · doi:10.1126/sciadv.adi4298 · Cited by 51 · see citing works
Singh, B., Modica-Napolitano, J. S., & Singh, K. K. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.05.004 · Cited by 49 · see citing works
The Emerging Role of RHOT1/Miro1 in the Pathogenesis of Parkinson's Disease
Großmann, D., Berenguer-Escuder, C., Chemla, A., Arena, G., & Krüger, R. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.00587 · Cited by 48 · see citing works
The myriad roles of Miro in the nervous system: axonal transport of mitochondria and beyond
Lee, K.-S., & Lu, B.-W. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00330 · Cited by 46 · see citing works
Understanding Miro GTPases: Implications in the Treatment of Neurodegenerative Disorders
Kay, L., Pienaar, I., Cooray, R., Black, G., & Soundararajan, M. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0927-x · Cited by 40 · see citing works
White, C. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00171 · Cited by 41 · see citing works
Do, J., Zwick, D. B., Kenyon, J. D., Zhong, F., Askew, D., Huang, A. Y.-C., Hof, W. V., Finney, M. R., & Laughlin, M. J. (2021) · Scientific Reports · doi:10.1038/s41598-021-90115-8 · Cited by 41 · see citing works
Miro proteins and their role in mitochondrial transfer in cancer and beyond
Nahácka, Z., Novák, J., Zobalová, R., & Neužil, J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.937753 · Cited by 41 · see citing works
Dynamics of Mitochondrial Transport in Axons
Niescier, R. F., Kwak, S. K., Joo, S. H., Chang, K. T., & Min, K. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00123 · Cited by 40 · see citing works
Self-citationZheng, X. F. S., Chen, M., Meng, X., Chu, X., Cai, C., & Zou, F. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.03.019 · Cited by 39 · see citing works
Shaw, J. L., & Chang, K. T. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003792 · Cited by 38 · see citing works
Self-citationOrchestrating mitochondria in neurons: Cytoskeleton as the conductor
Cardanho‐Ramos, C., Faria‐Pereira, A., & Morais, V. A. (2019) · Cytoskeleton · doi:10.1002/cm.21585 · Cited by 37 · see citing works
Regulation of Ca2+ exchanges and signaling in mitochondria
Carvalho, E. J., Stathopulos, P. B., & Madesh, M. (2020) · Current Opinion in Physiology · doi:10.1016/j.cophys.2020.08.010 · Cited by 37 · see citing works
Zhang, L., Liu, Q., Hu, H., Zhao, L., & Zhu, K. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113482 · Cited by 35 · see citing works
Tang, J., Duan, W., Deng, P., Li, H., Liu, C., Duan, Y., Feng, M., & Xu, S. (2021) · Toxicology · doi:10.1016/j.tox.2021.152726 · Cited by 36 · see citing works
Huntington, T. E., & Srinivasan, R. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102383 · Cited by 31 · see citing works
Jadiya, P., Cohen, H. M., Kolmetzky, D. W., Kadam, A. A., Tomar, D., & Elrod, J. W. (2023) · iScience · doi:10.1016/j.isci.2023.106296 · Cited by 34 · see citing works
Organelle biogenesis and interorganellar connections
Daniele, T., & Schiaffino, M. V. (2014) · Communicative & Integrative Biology · doi:10.4161/cib.29587 · Cited by 34 · see citing works
Cisplatin induces mitochondrial deficits in Drosophila larval segmental nerve
Podratz, J. L., Lee, H. B., Knorr, P., Koehler, S. V., Forsythe, S. D., Lambrecht, K., Arias‐Mejias, S. M., Schmidt, K., Steinhoff, G., Yudintsev, G., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.10.003 · Cited by 34 · see citing works
Mitochondria Change Dynamics and Morphology during Grapevine Leaf Senescence
Ruberti, C., Barizza, E., Bodner, M., Rocca, N. L., Michele, R. D., Carimi, F., Schiavo, F. L., & Zottini, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102012 · Cited by 33 · see citing works
Miro, MCU, and calcium: bridging our understanding of mitochondrial movement in axons
Niescier, R. F., Chang, K. T., & Min, K. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00148 · Cited by 33 · see citing works
Self-citationThe evolution of the axonal transport toolkit
Surana, S., Villarroel‐Campos, D., Lazo, O. M., Moretto, E., Tosolini, A. P., Rhymes, E. R., Richter, S., Sleigh, J. N., & Schiavo, G. (2019) · Traffic · doi:10.1111/tra.12710 · Cited by 30 · see citing works
Interaction between the mitochondrial adaptor MIRO and the motor adaptor TRAK
Baltrusaitis, E. E., Ravitch, E. E., Fenton, A. R., Perez, T. A., Holzbaur, E. L. F., & Domínguez, R. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105441 · Cited by 31 · see citing works
Hutto, R. A., Bisbach, C. M., Abbas, F. H., Brock, D. C., Cleghorn, W. M., Parker, E. D., Bauer, B. H., Ge, W., Vinberg, F., Hurley, J. B., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0398-2 · Cited by 31 · see citing works
Cristae junction as a fundamental switchboard for mitochondrial ion signaling and bioenergetics
Gottschalk, B., Madreiter‐Sokolowski, C. T., & Graier, W. F. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102517 · Cited by 30 · see citing works
Zaninello, M., & Bean, C. (2023) · Biomolecules · doi:10.3390/biom13060938 · Cited by 30 · see citing works
The mitochondrial Ras-related GTPase Miro: views from inside and outside the metazoan kingdom
Yamaoka, S., & Hara‐Nishimura, I. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00350 · Cited by 30 · see citing works
Mitochondrial roles of the psychiatric disease risk factor DISC1
Norkett, R., Modi, S., & Kittler, J. T. (2017) · Schizophrenia Research · doi:10.1016/j.schres.2016.12.025 · Cited by 29 · see citing works
Mitochondrial Calcium Signaling as a Therapeutic Target for Alzheimer’s Disease
Wu, A. J., Tong, B. C., Huang, S., Li, M., & Cheung, K. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666191210091302 · Cited by 29 · see citing works
Miro proteins connect mitochondrial function and intercellular transport
Nahácka, Z., Zobalová, R., Dubisova, M., Rohlena, J., & Neužil, J. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2021.1925216 · Cited by 28 · see citing works
Insight into human Miro1/2 domain organization based on the structure of its N-terminal GTPase
Smith, K. P., Focia, P. J., Chakravarthy, S., Landahl, E. C., Klosowiak, J. L., Rice, S. E., & Freymann, D. M. (2019) · Journal of Structural Biology · doi:10.1016/j.jsb.2020.107656 · Cited by 27 · see citing works
Guo, M., Liu, R., Zhang, F., Qu, J., Yang, Y., & Li, X. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107409 · Cited by 28 · see citing works
Guo, Y., Fu, T., Cheng, Y., Li, Y., Zhang, R.-C., Ma, Q.-T., Wang, G., Ning, W., Fan, W., Yang, J., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02287-9 · Cited by 26 · see citing works
Photochemical Targeting of Mitochondria to Overcome Chemoresistance in Ovarian Cancer †
Rickard, B. P., Overchuk, M., Obaid, G., Ruhi, M. K., Demirci, U., Fenton, S. E., Santos, J. H., Kessel, D. H., & Rizvi, I. (2022) · Photochemistry and Photobiology · doi:10.1111/php.13723 · Cited by 26 · see citing works
Devine, M. J., Szulc, B. R., Howden, J. H., López‐Doménech, G., Ruiz, A. J., & Kittler, J. T. (2022) · Journal of Cell Science · doi:10.1242/jcs.259823 · Cited by 26 · see citing works
Synaptic mitochondria: A crucial factor in the aged hippocampus
Cicali, K. A., & Tapia‐Rojas, C. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102524 · Cited by 26 · see citing works
Choi, S. Y., Kim, J. Y., Kim, H., Cho, B., Cho, H. M., Oppenheim, R. W., Kim, H., Rhyu, I. J., & Sun, W. (2012) · The FASEB Journal · doi:10.1096/fj.12-211920 · Cited by 25 · see citing works
Kuk, M. U., Lee, Y. H., Kim, J., Hwang, S. Y., Park, J. T., & Park, S. C. (2021) · Cells · doi:10.3390/cells10020420 · Cited by 22 · see citing works
Intermitochondrial signaling regulates the uniform distribution of stationary mitochondria in axons
Matsumoto, N., Hori, I., Kajita, M., Murase, T., Nakamura, W., Tsuji, T., Miyake, S., Inatani, M., & Konishi, Y. (2022) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2022.103704 · Cited by 22 · see citing works
Mitochondrial Miro GTPases coordinate mitochondrial and peroxisomal dynamics
Zinsmaier, K. E. (2020) · Small GTPases · doi:10.1080/21541248.2020.1843957 · Cited by 21 · see citing works
Mitochondrial fission and fusion in neurodegenerative diseases:Ca2+ signalling
Liu, X., Li, T., Tu, X., Xu, M., & Wang, J. (2025) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2025.103992 · Cited by 21 · see citing works
Yokota, S., Takihara, Y., Arimura, S., Miyake, S., Takamura, Y., Yoshimura, N., & Inatani, M. (2015) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.15-17876 · Cited by 19 · see citing works
Schwarz, L., Sharma, K., Dodi, L. D., Rieder, L.-S., Fallier‐Becker, P., Casadei, N., & Fitzgerald, J. C. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.966209 · Cited by 17 · see citing works
Imaging of neuronal mitochondria in situ
Plucińska, G., & Misgeld, T. (2016) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2016.06.006 · Cited by 17 · see citing works
Costa, F. P., Wiedenmann, B. J., Schöll, E., & Tuszyński, J. A. (2024) · Frontiers in Network Physiology · doi:10.3389/fnetp.2024.1483401 · Cited by 17 · see citing works
Guan, Y., Wang, D., Ying, S., & Feng, M. (2016) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2016.05.005 · Cited by 15 · see citing works
- Authors
- Chang, K. T., Niescier, R. F., & Min, K.-T.
- Affiliations
- University of Southern California (US)
- Indiana University Bloomington (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2011-08-29
- Volume
- 108
- Issue
- 37
- Pages
- 15456-15461
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3174631
- OpenAlex
- W1998654006
- Cited by
- 153
- References
- 33
- Citations by year
- 2026: 9 · 2025: 15 · 2024: 13 · 2023: 11 · 2022: 13 · 2021: 14 · 2020: 10 · 2019: 12 · 2018: 8 · 2017: 7 · 2016: 10 · 2015: 5 · 2014: 12 · 2013: 6 · 2012: 8
- FWCI
- 3.37
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Scholarworks@UNIST (Ulsan National Institute of Science and Technology) (submittedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (K99NS052524, NS052524, R00NS052524)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- mitochondrial motility, axons, mitochondrial matrix calcium, mitochondrial calcium uniporter, calcium uptake, Miro1, mitochondrial transport, calcium buffering, neuronal energy metabolism, calcium-dependent enzyme activity
- MeSH terms
- Animals, Axons, Calcium, Humans, Mitochondria, Movement, Mutation, Calcium Channels, Calcium Signaling, EF Hand Motifs, Mitochondrial Proteins, Mice
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