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Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Open accessAbstract
Changes in mitochondrial morphology that occur during cell cycle, differentiation, and death are tightly regulated by the balance between fusion and fission processes. Excessive fragmentation can be caused by inhibition of the fusion machinery and is a common consequence of dysfunction of the organelle. Here, we show a role for calcineurin-dependent translocation of the profission dynamin related protein 1 (Drp1) to mitochondria in dysfunction-induced fragmentation. When mitochondrial depolarization is associated with sustained cytosolic Ca 2+ rise, it activates the cytosolic phosphatase calcineurin that normally interacts with Drp1. Calcineurin-dependent dephosphorylation of Drp1, and in particular of its conserved serine 637, regulates its translocation to mitochondria as substantiated by site directed mutagenesis. Thus, fragmentation of depolarized mitochondria depends on a loop involving sustained Ca 2+ rise, activation of calcineurin, and dephosphorylation of Drp1 and its translocation to the organelle.
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“Interestingly, the downstream ROCK target calcineurin can dephosphorylate Drp1 and cause mitochondrial fission [135,136].”
From RhoA Signaling in Neurodegenerative Diseases (2022) · cites this paper as [135]
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“The activation of cAMP/PKA upon nutrient starvation leads to phosphorylation of Drp1, preventing its stable docking on the mitochondrial surface and therefore mitochondrial fission (Cereghetti et al, 2008) (Fig 2A).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Cereghetti et al, 2008
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Cites
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
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion
Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673
Self-citationMitochondrial Transport of Cations: Channels, Exchangers, and Permeability Transition
Bernardi, P. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1127 · Cited by 1,546
Self-citationBAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis
Scorrano, L., Oakes, S. A., Opferman, J. T., Cheng, E. H. Y., Sorcinelli, M. D., Pozzan, T., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1081208 · Cited by 1,387
Self-citationMitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission.
Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., & Mihara, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607279200 · Cited by 1,226
Organelle isolation: functional mitochondria from mouse liver, muscle and cultured filroblasts
Frezza, C., Cipolat, S., & Scorrano, L. (2007) · Nature Protocols · doi:10.1038/nprot.2006.478 · Cited by 1,188
Self-citationCribbs, J. T., & Strack, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401062 · Cited by 1,061
Chang, C., & Blackstone, C. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700083200 · Cited by 824
Self-citationCipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K., Metzger, K., Frezza, C., Annaert, W. G., D'adamio, L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.021 · Cited by 756
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Abdullah, M. O., Zeng, R. X., Margerum, C. L., Papadopoli, D. J., Monnin, C., Punter, K. B., Chu, C., Al-Rofaidi, M., Al‐Tannak, N. F., Berardi, D., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111198 · Cited by 46
Romani, P., Benedetti, G., Cusan, M., Arboit, M., Cirillo, C., Wu, X., Rouni, G., Kostourou, V., Aragona, M., Giampietro, C., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01527-3 · Cited by 47
RetractedCalcium-mediated regulation of mitophagy: implications in neurodegenerative diseases
Borbolis, F., Ploumi, C., & Palikaras, K. (2025) · npj Metabolic Health and Disease · doi:10.1038/s44324-025-00049-2 · Cited by 50
Tagashira, H., Zhang, C., Lu, Y., Hasegawa, H., Kanai, H., Han, F., & Fukunaga, K. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.12.029 · Cited by 51
Schauss, A. C., Huang, H., Choi, S., Xu, L., Soubeyrand, S., Bilodeau, P. S., Zunino, R., Rippstein, P. U., Frohman, M. A., & McBride, H. M. (2010) · BMC Biology · doi:10.1186/1741-7007-8-100 · Cited by 47
Kim, K. Y., Hwang, S., Park, S. Y., Kim, M. J., Jun, D. Y., & Kim, Y. H. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.07.018 · Cited by 47
Sarkar, S., Jun, S., & Simpkins, J. W. (2015) · Brain Research · doi:10.1016/j.brainres.2015.04.059 · Cited by 47
Cho, Y., & Kim, Y. K. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103212 · Cited by 48
Merrill, R. A., Slupe, A. M., & Strack, S. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08631.x · Cited by 48
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Hung, C. H.-L., Ho, J. Y. S., & Chang, R. C. (2010) · Ageing Research Reviews · doi:10.1016/j.arr.2010.05.003 · Cited by 46
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Chao, T. H., Wang, H., & Ho, P. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00473 · Cited by 47
Valenti, D., Rossi, L., Marzulli, D., Bellomo, F., Rasmo, D. D., Signorile, A., & Vacca, R. A. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.014 · Cited by 48
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Burdyga, A., Surdo, N. C., Monterisi, S., Benedetto, G. D., Grisan, F., Penna, E., Pellegrini, L., Zaccolo, M., Bortolozzi, M., Swietach, P., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1806318115 · Cited by 46
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Li, Y., Xie, Z., Song, Q., & Li, J.-Y. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-00864-z · Cited by 49
Oliveira, J. M. A., & Gonçalves, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807459200 · Cited by 45
Li, S., Fell, S. M., Surova, O. V., Smedler, E., Wallis, K., Chen, Z. X., Hellman, U., Johnsen, J. I., Martinsson, T., Kenchappa, R. S., et al. (2016) · Developmental Cell · doi:10.1016/j.devcel.2015.12.029 · Cited by 41
Wang, L., Ye, X., Zhao, Q., Zhou, Z., Dan, J., Zhu, Y., Chen, Q., & Liu, L. (2014) · Stem Cells and Development · doi:10.1089/scd.2014.0059 · Cited by 46
Wang, W., Fernández‐Sanz, C., & Sheu, S. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.004 · Cited by 46
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Liu, X., Wang, Y., Yu, X., Li, D., & Li, G. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3255 · Cited by 45
Quintana, D. D., Garcia, J. A., Sarkar, S. N., Jun, S., Engler-Chiurazzi, E. B., Russell, A. E., Cavendish, J. Z., & Simpkins, J. W. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.12.004 · Cited by 46
Seo, S. U., Woo, S. M., Kim, M. W., Lee, H., Kim, S. H., Kang, S. C., Lee, E., Min, K., & Kwon, T. K. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101422 · Cited by 45
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Ježek, J., Cooper, K. F., & Strich, R. (2021) · Biology · doi:10.3390/biology10010033 · Cited by 47
Machine learning-based classification of mitochondrial morphology in primary neurons and brain
Fogo, G. M., Anzell, A. R., Maheras, K. J., Raghunayakula, S., Wider, J. M., Emaus, K. J., Bryson, T. D., Bukowski, M. J., Neumar, R. W., Przyklenk, K., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-84528-8 · Cited by 44
Mitochondrial Ca2+ as a Key Regulator of Mitochondrial Activities
Calí, T., Ottolini, D., & Brini, M. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_3 · Cited by 44
SanMartín, C. D., Paula-Lima, A. C., GarcÃa, A., Veloso, P., Härtel, S., NÃoñez, M. T., & Hidalgo, C. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00013 · Cited by 43
Chen, S., Lin, T., Yang, D., Lee, S.-Y., Shaw, F.-Z., Liou, C., & Chuang, Y. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.03.045 · Cited by 44
Aung, L. H. H., Jumbo, J. C. C., Wang, Y., & Li, P. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.06.006 · Cited by 45
Li, G., Xu, K., Xing, W., Yang, H., Li, Y., Wang, X., Zhou, J., An, J., Dong, L., Zhang, X., et al. (2022) · Hypertension · doi:10.1161/hypertensionaha.122.19126 · Cited by 44
Biogenesis of Mitochondrial Proteins
Herrmann, J. M., Longen, S., Weckbecker, D., & Depuydt, M. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_3 · Cited by 44
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Nagdas, S., & Kashatus, D. F. (2017) · Antioxidants · doi:10.3390/antiox6020033 · Cited by 46
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Wang, H., Yi, J., Li, X., Xiao, Y., Dhakal, K. R., & Zhou, J. (2017) · Bone · doi:10.1016/j.bone.2017.10.010 · Cited by 43
Yu, X., Jia, L., Yu, W., & Du, H. (2019) · Brain Research · doi:10.1016/j.brainres.2019.01.018 · Cited by 43
Ruiz, A., Quintela‐López, T., Sánchez‐Gómez, M. V., Gaminde‐Blasco, A., Alberdi, E. M., & Matute, C. (2020) · Glia · doi:10.1002/glia.23802 · Cited by 43
Shi, Y., Zhang, Z., Yin, Q., Fu, C. S., Barszczyk, A., Zhang, X., Wang, J., & Yang, D. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16544 · Cited by 43
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Rasmo, D. D., Cormio, A., Cormio, G., & Signorile, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021224 · Cited by 44
Bertolin, G., Jacoupy, M., Traver, S., Ferrando-Miguel, R., Georges, T. S., Grenier, K., Ardila-Osorio, H., Mp, M., Takahashi, H., Lees, A. J., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2014.224 · Cited by 45
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Zhou, Y., Suo, W., Zhang, X., Liang, J., Zhao, W., Wang, Y., Li, H., & Ni, Q. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115669 · Cited by 43
Pekson, R., Liang, F. G., Axelrod, J. L., Lee, J., Qin, D., Wittig, A. J. H., Paulino, V. M., Zheng, M., Peixoto, P. M. V., & Kitsis, R. N. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2303713120 · Cited by 42
Park, S. J., Lee, H., Jo, D. S., Jo, Y. K., Shin, J. H., Kim, H. B., Seo, H. M., Rubinsztein, D. C., Koh, J., Lee, E. K., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.10.017 · Cited by 42
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Choudhary, V., Kaddour‐Djebbar, I., Lakshmikanthan, V., Ghazaly, T., Thangjam, G. S., Sreekumar, A., Lewis, R. W., Mills, I. G., Bollag, W. B., & Kumar, M. V. (2011) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-10-0445 · Cited by 41
Pan, R., Kaur, N., & Hu, J. (2014) · The Plant Journal · doi:10.1111/tpj.12532 · Cited by 42
Karam, C. N., Yi, J., Xiao, Y., Dhakal, K. R., Zhang, L., Li, X., Manno, C. D., Xu, J., Li, K., Cheng, H., et al. (2017) · Skeletal Muscle · doi:10.1186/s13395-017-0123-0 · Cited by 42
Xu, M., Hua, Y., Qi, Y., Meng, G., & Yang, S. (2019) · Experimental Dermatology · doi:10.1111/exd.13930 · Cited by 42
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Giovarelli, M., Zecchini, S., Martini, E., Garrè, M., Barozzi, S., Ripolone, M., Napoli, L., Coazzoli, M., Vantaggiato, C., Roux-Biejat, P., et al. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-020-0510-7 · Cited by 41
White, C. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00171 · Cited by 42
Michels, S., Ganjam, G. K., Martins, H. C., Schratt, G. M., Wöhr, M., Schwarting, R. K. W., & Culmsee, C. (2018) · Cell Death Discovery · doi:10.1038/s41420-018-0061-6 · Cited by 43
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Zaninello, M., Palikaras, K., Sotiriou, A., Tavernarakis, N., & Scorrano, L. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00847-3 · Cited by 40
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Rasmo, D. D., Micelli, L., Santeramo, A., Signorile, A., Lattanzio, P., & Papa, S. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.01.006 · Cited by 40
Huang, H., Xiong, Q., Wang, N., Chen, R., Ren, H., Siwko, S. K., Han, H., Liu, M., Qian, M., & Du, B. (2018) · Science Advances · doi:10.1126/sciadv.aas9784 · Cited by 38
Chen, Y., Guo, S., Tang, Y., Mou, C., Hu, X., Shao, F., Yan, W. X., & Wu, Q. (2020) · Medical Science Monitor · doi:10.12659/msm.928651 · Cited by 42
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Ye, F., Li, X., Li, F., Li, J., Chang, W., Yuan, J., & Chen, J. (2016) · NeuroToxicology · doi:10.1016/j.neuro.2016.10.004 · Cited by 41
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Qi, Z., Shi, W., Zhao, Y., Ji, X., & Liu, K. J. (2019) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2019.114601 · Cited by 39
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Kabra, U. D., & Jastroch, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813782 · Cited by 40
Uzhachenko, R. V., Ivanov, S. V., Yarbrough, W. G., Shanker, A., Medzhitov, R. M., & Ivanova, A. V. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5437 · Cited by 38
Hwang, R., Wiemerslage, L., LaBreck, C. J., Khan, M. H., Kannan, K., Wang, X., Zhu, X., Lee, D., & Fridell, Y.-W. C. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.05.032 · Cited by 38
Lavie, J., Serrat, R., Bellancé, N., Courtand, G., Dupuy, J., Tesson, C., Coupry, I., Brice, A., Lacombe, D., Dürr, A., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw425 · Cited by 39
Borgmann, K., & Ghorpade, A. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9812-z · Cited by 38
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Martinvalet, D. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/9165214 · Cited by 40
Aung, L. H. H., Chen, X., Jumbo, J. C. C., Li, Z., Wang, S., Zhao, C., Liu, Z., Wang, Y., & Li, P. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.08.006 · Cited by 37
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Bretón‐Romero, R., Acín‐Pérez, R., Rodríguez‐Pascual, F., Molledo, M. M., Brandes, R. P., Rial, E., Enríquez, J. A., & Lamas, S. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.07.003 · Cited by 39
Cho, M.-H., Kim, D., Choi, J., Chang, E., & Seung-YongYoon (2012) · Brain Research · doi:10.1016/j.brainres.2012.03.010 · Cited by 39
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Mammucari, C., Patrón, M., Granatiero, V., & Rizzuto, R. (2011) · BioFactors · doi:10.1002/biof.160 · Cited by 37
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Tseng, H., Lin, C., Hsiao, L., & Yang, C. (2019) · Journal of Lipid Research · doi:10.1194/jlr.ra119000141 · Cited by 37
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Das, R., Kamal, I. M., Das, S., Chakrabarti, S., & Chakrabarti, O. (2021) · Journal of Cell Science · doi:10.1242/jcs.257808 · Cited by 38
Tan, A. R., Cai, A. Y., Deheshi, S., & Rintoul, G. L. (2011) · Cell Calcium · doi:10.1016/j.ceca.2010.12.002 · Cited by 37
Galindo, M. F., Solesio, M. E., Atienzar‐Aroca, S., Zamora, M. J., & Jordán, J. (2012) · Parkinson s Disease · doi:10.1155/2012/131058 · Cited by 37
Linkermann, A., Konstantinidis, K., & Kitsis, R. N. (2016) · Cell Death & Differentiation · doi:10.1038/cdd.2015.151 · Cited by 36
Scarpelli, P. H., Tessarin‐Almeida, G., Viçoso, K. L., Lima, W. R., Borges‐Pereira, L., Meissner, K. A., Wrenger, C., Raffaello, A., Rizzuto, R., Pozzan, T., et al. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12484 · Cited by 36
Zheng, F., Jia, B., Dong, F., Liu, L., Rasul, F., He, J., & Fu, C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010185 · Cited by 33
Lovy, A., Ahumada-Castro, U., Bustos, G., Farías, P., González-Billault, C. E., Molgó, J., & Cárdenas, C. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00378 · Cited by 37
Loh, J., Lin, C., Yang, M., Chou, C., Chen, W.-S., Hong, M., Cho, C.-L., Hsu, C., Cheng, J., Chou, A., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.04.013 · Cited by 39
Self-citationCho, S.-G., Xiao, X., Wang, S., Gao, H., Rafikov, R., Black, S. M., Huang, S., Ding, H., Yoon, Y., Kirken, R. A., et al. (2019) · Journal of the American Society of Nephrology · doi:10.1681/asn.2018111117 · Cited by 35
Mitochondrial fission – changing perspectives for future progress
Kamerkar, S. C., Liu, A., & Higgs, H. N. (2025) · Journal of Cell Science · doi:10.1242/jcs.263640 · Cited by 43
Darwesh, A. M., Jamieson, K. L., Wang, C., Samokhvalov, V., & Seubert, J. M. (2018) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2018-0480 · Cited by 35
A novel class of cardioprotective small-molecule PTP inhibitors
Antonucci, S., Sante, M. D., Šileikytė, J., Devereaux, J., Bauer, T. M., Bround, M. J., Menabò, R., Paillard, M., Alánová, P., Carraro, M., et al. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104548 · Cited by 34
Self-citationThe Protective Effects of Calcineurin on Pancreatitis in Mice Depend on the Cellular Source
Wen, L., Javed, T. A., Dobbs, A. K., Brown, R., Niu, M., Li, L., Khalid, A., Barakat, M. T., Xiao, X., Yimlamai, D., et al. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.05.051 · Cited by 36
Tang, F.-L., Wang, J., Itokazu, Y., & Yu, R. K. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15137 · Cited by 30
Lee, D. G., Nam, B. R., Huh, J., & Lee, D. (2020) · Inflammation · doi:10.1007/s10753-020-01370-2 · Cited by 37
Switch from ER-mitochondrial to SR-mitochondrial calcium coupling during muscle differentiation
Yi, M., Weaver, D., Eisner, V., Várnai, P., Hunyady, L., Ma, J., Csordás, G., & Hajnóczky, G. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.05.012 · Cited by 35
Signaling at the gate: Phosphorylation of the mitochondrial protein import machinery
Rao, S., Gerbeth, C., Harbauer, A. B., Mikropoulou, D., Meisinger, C., & Schmidt, O. (2011) · Cell Cycle · doi:10.4161/cc.10.13.16054 · Cited by 34
Metadata
- Authors
- Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L.
- Affiliations
- Veneto Institute of Molecular Medicine (IT)
- *Dulbecco-Telethon Institute;
- National Institutes of Health (US)
- University of Padua (IT)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2008-10-14
- Volume
- 105
- Issue
- 41
- Pages
- 15803-15808
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2572940
- OpenAlex
- W2023283007
- Cited by
- 1,129
- References
- 35
- Citations by year
- 2026: 40 · 2025: 51 · 2024: 54 · 2023: 79 · 2022: 67 · 2021: 79 · 2020: 92 · 2019: 60 · 2018: 86 · 2017: 78 · 2016: 80 · 2015: 59 · 2014: 68 · 2013: 58 · 2012: 54
- FWCI
- 16.44
- 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)
- Archive ouverte UNIGE (University of Geneva) (acceptedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Padua Research Archive (University of Padova) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- calcineurin, Drp1, mitochondrial fission, mitochondrial depolarization, mitochondrial fragmentation, intracellular calcium, mitochondrial morphology, mitochondrial fusion
- MeSH terms
- Calcium, HeLa Cells, Humans, Microtubule-Associated Proteins, Mitochondria, Phosphorylation, Serine, Mutagenesis, Site-Directed, Calcineurin, GTP Phosphohydrolases, Protein Transport, Mitochondrial Proteins, Dynamins, Membrane Potential, Mitochondrial
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