Mitochondrial calcium exchange in physiology and disease

LETM Proteins Play a Role in the Accumulation of Mitochondrially Encoded Proteins in Arabidopsis thaliana and AtLETM2 Displays Parent of Origin Effects

Zhang, B., Carrie, C., Ivanova, A., Narsai, R., Murcha, M. W., Duncan, O., Wang, Y., Law, S. R., Albrecht, V., Pogson, B. J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.383836 · Cited by 68

Inositol 1,4,5-trisphosphate-mediated sarcoplasmic reticulum–mitochondrial crosstalk influences adenosine triphosphate production via mitochondrial Ca2+uptake through the mitochondrial ryanodine receptor in cardiac myocytes

Seidlmayer, L. K., Kühn, J., Berbner, A., Arias-Loza, P.-A., Williams, T., Kaspar, M., Czolbe, M., Kwong, J. Q., Molkentin, J. D., Heinze, K. G., et al. (2016) · Cardiovascular Research · doi:10.1093/cvr/cvw185 · Cited by 68

Strategic Positioning and Biased Activity of the Mitochondrial Calcium Uniporter in Cardiac Muscle

de la Fuente, S., Fernández‐Sanz, C., Vail, C., Agra, E. J., Holmström, K. M., Sun, J., Mishra, J., Williams, D., Finkel, T., Murphy, E., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.755496 · Cited by 68

Ion and inhibitor binding of the double-ring ion selectivity filter of the mitochondrial calcium uniporter

Cao, C., Wang, S., Cui, T., Su, X., & Chou, J. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620316114 · Cited by 67

Mitochondrial Ca2+ uniporter and CaMKII in heart

Fieni, F., Johnson, D. E., Hudmon, A., & Kirichok, Y. (2014) · Nature · doi:10.1038/nature13626 · Cited by 66

Structural dependency of the inhibitory action of benzodiazepines and related compounds on the mitochondrial Na+-Ca2+ exchanger

Chiesi, M., Schwaller, R., & Eichenberger, K. (1988) · Biochemical Pharmacology · doi:10.1016/0006-2952(88)90623-5 · Cited by 66

Ribosome-binding Proteins Mdm38 and Mba1 Display Overlapping Functions for Regulation of Mitochondrial Translation

Bauerschmitt, H., Mick, D. U., Deckers, M., Vollmer, C., Funes, S., Kehrein, K., Ott, M., Rehling, P., & Herrmann, J. M. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-02-0101 · Cited by 66

Inverse correlation between expression of the Wolfs Hirschhorn candidate gene Letm1 and mitochondrial volume in C. elegans and in mammalian cells

Hasegawa, A., & van der Bliek, A. M. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm154 · Cited by 66

Cooperative Interactions in Energy-dependent Accumulation of Ca2+ by Isolated Rat Liver Mitochondria

Bygrave, F. L., Reed, K. C., & Spencer, T. L. (1971) · Nature New Biology · doi:10.1038/newbio230089a0 · Cited by 65

Mitochondrial pathobiology in ALS

Martin, L. J. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9395-y · Cited by 65

EMRE is essential for mitochondrial calcium uniporter activity in a mouse model

Liu, J. C., Syder, N. C., Ghorashi, N. S., Willingham, T. B., Parks, R. J., Sun, J., Fergusson, M. M., Liu, J., Holmström, K. M., Menazza, S., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.134063 · Cited by 65

Cardiovascular homeostasis dependence on MICU2, a regulatory subunit of the mitochondrial calcium uniporter

Bick, A. G., Wakimoto, H., Kamer, K. J., Sancak, Y., Goldberger, O., Raja, A. A., DeLaughter, D. M., Gorham, J., Mootha, V. K., Seidman, J. G., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1711303114 · Cited by 64

The Pathophysiology of LETM1

Nowikovsky, K., Pozzan, T., Rizzuto, R., Scorrano, L., & Bernardi, P. (2012) · The Journal of General Physiology · doi:10.1085/jgp.201110757 · Cited by 64

Selective mitochondrial Ca 2+ uptake deficit in disease endstage vulnerable motoneurons of the SOD1 G93A mouse model of amyotrophic lateral sclerosis

Fuchs, A., Kutterer, S., Mühling, T., Duda, J., Schütz, B., Liss, B., Keller, B. U., & Roeper, J. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2012.247981 · Cited by 63

Suppression of Arrhythmia by Enhancing Mitochondrial Ca2+ Uptake in Catecholaminergic Ventricular Tachycardia Models

Schweitzer, M. K., Wilting, F., Sedej, S., Dreizehnter, L., Dupper, N. J., Tian, X. Y., Moretti, A., My, I., Kwon, O., Priori, S. G., et al. (2017) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2017.06.008 · Cited by 63

Reduced mitochondrial Ca2+ transients stimulate autophagy in human fibroblasts carrying the 13514A>G mutation of the ND5 subunit of NADH dehydrogenase

Granatiero, V., Giorgio, V., Calí, T., Patrón, M., Brini, M., Bernardi, P., Tiranti, V., Zeviani, M., Pallafacchina, G., Stefani, D. D., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.84 · Cited by 62

Inhibitory Properties of Ruthenium Amine Complexes on Mitochondrial Calcium Uptake

Zazueta, C., Torres, M. E. S., Correa, F., & Garza‐Ortiz, A. (1999) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005464927366 · Cited by 61

Endoplasmic reticulum potassium–hydrogen exchanger and small conductance calcium-activated potassium channel activities are essential for ER calcium uptake in neurons and cardiomyocytes

Kuum, M., Veksler, V., Liiv, J., Ventura‐Clapier, R., & Kaasik, A. (2012) · Journal of Cell Science · doi:10.1242/jcs.090126 · Cited by 61

Mitochondrial calcium uniporter inhibition provides cardioprotection in pressure overload-induced heart failure through autophagy enhancement

Yu, Z., Chen, R., Li, M., Yu, Y. Q., Liang, Y., Han, F., Qin, S., Chen, X., Su, Y., & Ge, J. (2018) · International Journal of Cardiology · doi:10.1016/j.ijcard.2018.05.054 · Cited by 61

Mitochondrial control of epigenetics

Naviaux, R. K. (2008) · Cancer Biology & Therapy · doi:10.4161/cbt.7.8.6741 · Cited by 60

Trypanosome Letm1 Protein Is Essential for Mitochondrial Potassium Homeostasis

Hashimi, H., McDonald, L., Stříbrná, E., & Lukeš, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.495119 · Cited by 60

A Middle Eastern Founder Mutation Expands the Genotypic and Phenotypic Spectrum of Mitochondrial MICU1 Deficiency: A Report of 13 Patients

Musa, S. O., Eyaid, W., Kamer, K. J., Ali, R., Al‐Mureikhi, M., Shahbeck, N., Al‐Mesaifri, F., Makhseed, N., Zakkiriah, M., Al‐Shehhi, W., et al. (2018) · JIMD Reports · doi:10.1007/8904_2018_107 · Cited by 60

Structures reveal gatekeeping of the mitochondrial Ca2+ uniporter by MICU1-MICU2

Wang, C., Jacewicz, A., Delgado, B. D., Baradaran, R., & Long, S. B. (2020) · eLife · doi:10.7554/elife.59991 · Cited by 60

Coupled transmembrane mechanisms control MCU-mediated mitochondrial Ca 2+ uptake

Vais, H., Payne, R. J., Paudel, U., Li, C., & Foskett, J. K. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2005976117 · Cited by 60

Mitochondrial matrix pH controls oxidative phosphorylation and metabolism‐secretion coupling in INS‐1E clonal β cells

Akhmedov, D., Braun, M., Mataki, C., Park, K., Pozzan, T., Schoonjans, K., Rorsman, P., Wollheim, C. B., & Wiederkehr, A. (2010) · The FASEB Journal · doi:10.1096/fj.10-162222 · Cited by 59

Single Channel Characterization of the Mitochondrial Ryanodine Receptor in Heart Mitoplasts

Ryu, S.-Y., Beutner, G., Kinnally, K. W., Dirksen, R. T., & Sheu, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.c111.245597 · Cited by 59

Targeted siRNA Screens Identify ER-to-Mitochondrial Calcium Exchange in Autophagy and Mitophagy Responses in RPE1 Cells

MacVicar, T., Mannack, L., Lees, R. M., & Lane, J. D. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160613356 · Cited by 59

Analysis of the structure and function of EMRE in a yeast expression system

Yamamoto, T., Yamagoshi, R., Harada, K., Kawano, M., Minami, N., Ido, Y., Kuwahara, K., Fujita, A., Ozono, M., Watanabe, A., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.019 · Cited by 59

Comprehensive Genetic Characterization of Mitochondrial Ca2+ Uniporter Components Reveals Their Different Physiological Requirements In Vivo

Tufi, R., Gleeson, T. P., von Stockum, S., Hewitt, V. L., Lee, J. J., Terriente-Félix, A., Sánchez-Martínez, Á., Ziviani, E., & Whitworth, A. J. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.033 · Cited by 59

Inorganic polyphosphate is required for sustained free mitochondrial calcium elevation, following calcium uptake

Solesio, M. E., del Molino, L. C. G., Elustondo, P. A., Diao, C. T. M., Chang, J., & Pavlov, E. V. (2019) · Cell Calcium · doi:10.1016/j.ceca.2019.102127 · Cited by 59

Voltage-Dependent Anion Channel Transports Calcium Ions through Biomimetic Membranes

Deniaud, A., Rossi, C., Berquand, A., et al. (2007) · Langmuir · doi:10.1021/la063105+ · Cited by 58

G37R SOD1 mutant alters mitochondrial complex I activity, Ca2+ uptake and ATP production

Coussée, E., Smet, P. D., Bogaert, E., Elens, I., Damme, P. V., Willems, P. H. G. M., Koopman, W. J. H., Bosch, L. V. D., & Callewaert, G. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.02.004 · Cited by 58

Pathological consequences of MICU1 mutations on mitochondrial calcium signalling and bioenergetics

Bhosale, G., Sharpe, J. A., Koh, A., Kouli, A., Szabadkai, G., & Duchen, M. R. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.01.015 · Cited by 58

MICU1 protects against myocardial ischemia/reperfusion injury and its control by the importer receptor Tom70

Xue, Q., Pei, H.-F., Liu, Q.-S., Zhao, M.-J., Sun, J., Gao, E., Ma, X.-L., & Tao, L. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.280 · Cited by 58

Tamoxifen-induced knockdown of the mitochondrial calcium uniporter in Thy1-expressing neurons protects mice from hypoxic/ischemic brain injury

Nichols, M. T., Pavlov, E. V., & Robertson, G. S. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0607-9 · Cited by 58

Rearrangement of MICU1 multimers for activation of MCU is solely controlled by cytosolic Ca2+

Waldeck‐Weiermair, M., Malli, R., Parichatikanond, W., et al. (2015) · Scientific Reports · doi:10.1038/srep15602 · Cited by 56

Inhibiting the Mitochondrial Calcium Uniporter during Development Impairs Memory in Adult Drosophila

Drago, I., & Davis, R. L. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.017 · Cited by 56

A novel 4p16.3 microduplication distal to WHSC1 and WHSC2 characterized by oligonucleotide array with new phenotypic features

Cyr, A. B., Nimmakayalu, M. A., Longmuir, S. Q., Patil, S. R., Keppler‐Noreuil, K. M., & Shchelochkov, O. A. (2011) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.34120 · Cited by 55

Polarization of Calcium Signaling and Fluid Secretion in Salivary Gland Cells

Ambudkar, I. S. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712804143321 · Cited by 55

Functional roles of MICU1 and MICU2 in mitochondrial Ca 2+ uptake

Matesanz-Isabel, J., Arias-del-Val, J., Álvarez-Illera, P., Fonteríz, R. I., Montero, M., & Álvarez, J. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.02.022 · Cited by 55

The role of the mitochondrial calcium uniporter in cerebral ischemia/reperfusion injury in rats involves regulation of mitochondrial energy metabolism

Zhao, Q., Wang, S., Li, Y., Wang, P., Li, S., Guo, Y., & Yao, R. (2013) · Molecular Medicine Reports · doi:10.3892/mmr.2013.1321 · Cited by 54

Association of Mitochondrial Letm1 with Epileptic Seizures

Zhang, X., Chen, G., Lü, Y., Liu, J., Fang, M., Luo, J., Cao, Q., & Wang, X. (2013) · Cerebral Cortex · doi:10.1093/cercor/bht118 · Cited by 54

Ca2+uptake in mitochondria occurs via the reverse action of the Na+/Ca2+exchanger in metabolically inhibited MDCK cells

Smets, I., Caplanusi, A., Despa, S. I., Molnár, Z., Radu, M., vandeVen, M., Ameloot, M. M., & Steels, P. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00284.2003 · Cited by 53

Mitochondrial calcium uniporter complex modulation in cancerogenesis

Marchi, S., Vitto, V. A. M., Danese, A., Wieckowski, M. R., Giorgi, C., & Pinton, P. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1612698 · Cited by 53

Studying mitochondrial Ca2+ uptake – A revisit

Jean-Quartier, C., Bondarenko, A. I., Alam, M. R., Trenker, M., Waldeck‐Weiermair, M., Malli, R., & Graier, W. F. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.10.033 · Cited by 52

Molecular and functional identification of a mitochondrial ryanodine receptor in neurons

Jakob, R., Beutner, G., Sharma, V. K., Duan, Y., Gross, R. A., Hurst, S., Jhun, B. S., O‐Uchi, J., & Sheu, S. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.05.026 · Cited by 52

Mitochondrial cardiomyopathies feature increased uptake and diminished efflux of mitochondrial calcium

Sommakia, S., Houlihan, P. R., Deane, S., Simcox, J., Torres, N. S., Jeong, M.-Y., Winge, D. R., Villanueva, C. J., & Chaudhuri, D. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2017.09.009 · Cited by 52

The mitochondrial inner membrane protein LETM1 modulates cristae organization through its LETM domain

Nakamura, S., Matsui, A., Akabane, S., Tamura, Y., Hatano, A., Miyano, Y., Omote, H., Kajikawa, M., Maenaka, K., Moriyama, Y., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-0832-5 · Cited by 52

Glucagon Regulation of Oxidative Phosphorylation Requires an Increase in Matrix Adenine Nucleotide Content through Ca2+ Activation of the Mitochondrial ATP-Mg/Pi Carrier SCaMC-3

Amigo, I., Traba, J., González‐Barroso, M. M., Rueda, C. B., Fernández, M., Rial, E., Sánchez, A., Satrústegui, J., & del Arco, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.409144 · Cited by 51

A null mutation in MICU2 causes abnormal mitochondrial calcium homeostasis and a severe neurodevelopmental disorder

Shamseldin, H. E., AlAsmari, A. M., Salih, M. A., Samman, M. M., Mian, S. A., Alshidi, T. A., Ibrahim, N., Hashem, M., Faqeih, E., Al-Mohanna, F. A., et al. (2017) · Brain · doi:10.1093/brain/awx237 · Cited by 51

Parkin-dependent regulation of the MCU complex component MICU1

Matteucci, A., Patrón, M., Reane, D. V., Gastaldello, S., Amoroso, S., Rizzuto, R., Brini, M., Raffaello, A., & Calí, T. (2018) · Scientific Reports · doi:10.1038/s41598-018-32551-7 · Cited by 51

The structure of the MICU1‐MICU2 complex unveils the regulation of the mitochondrial calcium uniporter

Wu, W., Shen, Q., Zhang, R., Qiu, Z., Wang, Y., Zheng, J., & Jia, Z. (2020) · The EMBO Journal · doi:10.15252/embj.2019104285 · Cited by 51

Mitochondrial calcium uniporter in Drosophila transfers calcium between the endoplasmic reticulum and mitochondria in oxidative stress-induced cell death

Choi, S., Quan, X., Bang, S., Yoo, H., Kim, J., Park, J., Park, K., & Chung, J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.765578 · Cited by 50

NCLX prevents cell death during adrenergic activation of the brown adipose tissue

Assali, E. A., Jones, A. E., Veliova, M., Acín‐Pérez, R., Taha, M., Miller, N., Shum, M., de Oliveira, M. F., Las, G., Liesa, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16572-3 · Cited by 50

Overexpression of human mutated G93A SOD1 changes dynamics of the ER mitochondria calcium cycle specifically in mouse embryonic motor neurons

Lautenschläger, J., Prell, T., Ruhmer, J., Weidemann, L., Witte, O. W., & Großkreutz, J. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.03.027 · Cited by 49

Crystal structure of MICU2 and comparison with MICU1 reveal insights into the uniporter gating mechanism

Kamer, K. J., Jiang, W., Kaushik, V. K., Mootha, V. K., & Grabarek, Z. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1817759116 · Cited by 49

The mitochondrial peptidase, neurolysin, regulates respiratory chain supercomplex formation and is necessary for AML viability

Mirali, S., Botham, A. D., Voisin, V., Xu, C., St‐Germain, J. R., Sharon, D. M., Hoff, F. W., Qiu, Y., Hurren, R., Gronda, M., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aaz8264 · Cited by 49

Inhibition of L-type Ca2+ channel by mitochondrial Na+–Ca2+ exchange inhibitor CGP-37157 in rat atrial myocytes

Thư, L. T. A., Ahn, J. R., & Woo, S. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.09.013 · Cited by 48

A membrane potential‐modulated pathway for Ca2+ efflux in rat liver mitochondria

Bernardi, P., & AZZONE, G. F. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)80476-6 · Cited by 48

Targeting EZH2 regulates tumor growth and apoptosis through modulating mitochondria dependent cell-death pathway in HNSCC

Zhou, X., Ren, Y., Kong, L., Cai, G., Sun, S., Song, W., Wang, Y., Jin, R., Qi, L., Mei, M., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5606 · Cited by 48

CaMKII does not control mitochondrial Ca2+ uptake in cardiac myocytes

Nickel, A. G., Kohlhaas, M., Bertero, E., Wilhelm, D., Wagner, M., Sequeira, V., Kreußer, M. M., Dewenter, M., Kappl, R., Hoth, M., et al. (2019) · The Journal of Physiology · doi:10.1113/jp276766 · Cited by 48

Deletions involving genes WHSC1 and LETM1 may be necessary, but are not sufficient to cause Wolf–Hirschhorn Syndrome

Andersen, E., Carey, J. C., Earl, D., Corzo, D., Suttie, M., Hammond, P., & South, S. T. (2013) · European Journal of Human Genetics · doi:10.1038/ejhg.2013.192 · Cited by 46

Reversal of mitochondrial Na/Ca exchange during metabolic inhibition in rat cardiomyocytes

Griffiths, E. J. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00726-7 · Cited by 45

Frataxin deficiency in neonatal rat ventricular myocytes targets mitochondria and lipid metabolism

Òbis, È., Irazusta, V. P., Sanchís, D., Ros, J., & Tamarit, J. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.016 · Cited by 45

CGP-37157 Inhibits the Sarcoplasmic Reticulum Ca2+ ATPase and Activates Ryanodine Receptor Channels in Striated Muscle

Neumann, J. T., Díaz‐Sylvester, P., Fleischer, S., & Copello, J. A. (2010) · Molecular Pharmacology · doi:10.1124/mol.110.067165 · Cited by 45

Pharmacological modulation of mitochondrial calcium homeostasis

Arduíno, D. M., & Perocchi, F. (2018) · The Journal of Physiology · doi:10.1113/jp274959 · Cited by 45

LETM1 couples mitochondrial DNA metabolism and nutrient preference

Durigon, R., Mitchell, A., Jones, A. W. E., Manole, A., Mennuni, M., Hirst, E. M. A., Houlden, H., Maragni, G., Lattante, S., Doronzio, P. N., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708550 · Cited by 45

MICU1 and MICU2 Play an Essential Role in Mitochondrial Ca 2+ Uptake, Growth, and Infectivity of the Human Pathogen Trypanosoma cruzi

Bertolini, M. S., Chiurillo, M. Á., Lander, N., Vercesi, A. E., & Docampo, R. (2019) · mBio · doi:10.1128/mbio.00348-19 · Cited by 45

Important mitochondrial proteins in human omental adipose tissue show reduced expression in obesity

Lindinger, P. W., Christe, M., Eberlé, A. N., Kern, B. E., Peterli, R., Peters, T. T. A., Jayawardene, K. J. I., Fearnley, I. M., & Walker, J. E. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.03.037 · Cited by 45

Mitochondrial Ca2+ concentrations in live cells: quantification methods and discrepancies

Fernández‐Sanz, C., de la Fuente, S., & Sheu, S. (2019) · FEBS Letters · doi:10.1002/1873-3468.13427 · Cited by 44

The debate continues – What is the role of MCU and mitochondrial calcium uptake in the heart?

Garbincius, J. F., Luongo, T. S., & Elrod, J. W. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.04.029 · Cited by 44

Transport of Ca2+ and Ca2+-dependent permeability transition in heart mitochondria in the early stages of Duchenne muscular dystrophy

Dubinin, M. V., Talanov, E. Y., Tenkov, K. S., Starinets, V. S., Mikheeva, I. B., & Belosludtsev, K. N. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148250 · Cited by 44

MicroRNA‐195 controls MICU1 expression and tumor growth in ovarian cancer

Rao, G., Dwivedi, S. K. D., Zhang, Y., Dey, A., Shameer, K., Karthik, R., Srikantan, S., Hossen, M. N., Wren, J. D., Madesh, M., et al. (2020) · EMBO Reports · doi:10.15252/embr.201948483 · Cited by 44

Calcium influx through the mitochondrial calcium uniporter holocomplex, MCUcx

Boyman, L., Greiser, M., & Lederer, W. J. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.10.015 · Cited by 44

Elemental Analysis of Neurofibrillary Tangles in Alzheimer's Disease Using Proton‐Induced X‐ray Analysis

Murray, F. E. S., Landsberg, J. P., Williams, R. J. P., Esiri, M. M., & Watt, F. (2007) · Novartis Foundation symposium · doi:10.1002/9780470514306.ch12 · Cited by 42

Regulation of OPA1-mediated mitochondrial fusion by leucine zipper/EF-hand-containing transmembrane protein-1 plays a role in apoptosis

Piao, L., Li, Y., Kim, S. J., Sohn, K., Yang, K., Park, K. A., Byun, H. S., Won, M., Hong, J. H., Hur, G. M., et al. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.01.020 · Cited by 42

Overexpression of ryanodine receptor type 1 enhances mitochondrial fragmentation and Ca 2+ -induced ATP production in cardiac H9c2 myoblasts

O‐Uchi, J., Jhun, B. S., Hurst, S., Bisetto, S., Gross, P., Chen, M., Kettlewell, S., Park, J., Oyamada, H., Smith, G. L., et al. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00094.2013 · Cited by 42

Impaired translocation and activation of mitochondrial Akt1 mitigated mitochondrial oxidative phosphorylation Complex V activity in diabetic myocardium

Yang, J.-Y., Deng, W., Chen, Y., Fan, W., Baldwin, K. M., Jope, R. S., Wallace, D. C., & Wang, P. H. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.02.016 · Cited by 41

FOXD1-dependent MICU1 expression regulates mitochondrial activity and cell differentiation

Shanmughapriya, S., Tomar, D., Dong, Z., Slovik, K. J., Nemani, N., Natarajaseenivasan, K., Carvalho, E. J., Lu, C., Corrigan, K., Garikipati, V. N. S., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05856-4 · Cited by 41

Exploring the In Vivo Role of the Mitochondrial Calcium Uniporter in Brown Fat Bioenergetics

Flicker, D., Sancak, Y., Mick, E., Goldberger, O., & Mootha, V. K. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.013 · Cited by 41

A strong role for nature in face recognition

McKone, E., & Palermo, R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000567107 · Cited by 40

Pivotal role of mitochondrial Na+–Ca2+ exchange in antigen receptor mediated Ca2+ signalling in DT40 and A20 B lymphocytes

Kim, B., Takeuchi, A., Koga, O., Hikida, M., & Matsuoka, S. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.222927 · Cited by 40

The basal flux of Akt in the mitochondria is mediated by heat shock protein 90

Barksdale, K. A., & Bijur, G. N. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05878.x · Cited by 39

Characterization of distinct single-channel properties of Ca2+ inward currents in mitochondria

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Single-Channel Currents of the Permeability Transition Pore from the Inner Mitochondrial Membrane of Rat Liver and of a Human Hepatoma Cell Line

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Privileged crosstalk between TRPV1 channels and mitochondrial calcium shuttling machinery controls nociception

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Mitochondrial pore opening and loss of Ca2+ exchanger NCLX levels occur after frataxin depletion

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A putative mitochondrial calcium uniporter in A. fumigatus contributes to mitochondrial Ca2+ homeostasis and stress responses

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Suppression of Lung Tumorigenesis by Leucine Zipper/EF Hand–Containing Transmembrane-1

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MICU1 Confers Protection from MCU-Dependent Manganese Toxicity

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Skeletal muscle excitation-metabolism coupling

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Effect of micromolar Ca2+ on NADH inhibition of bovine kidney ?-ketoglutarate dehydrogenase complex and possible role of Ca2+ in signal amplification

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Increasing Ca2+ in photoreceptor mitochondria alters metabolites, accelerates photoresponse recovery, and reveals adaptations to mitochondrial stress

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 34

Computational analysis of Ca 2+ dynamics in isolated cardiac mitochondria predicts two distinct modes of Ca 2+ uptake

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Mitochondrial Ca2+ uniporter (MCU)-dependent and MCU-independent Ca2+ channels coexist in the inner mitochondrial membrane

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Suppression of LETM1 by siRNA inhibits cell proliferation and invasion of bladder cancer cells

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Characterization of MCU-Binding Proteins MCUR1 and CCDC90B — Representatives of a Protein Family Conserved in Prokaryotes and Eukaryotic Organelles

Adlakha, J., Karamichali, I., Sangwallek, J., Deiss, S., Bär, K., Coles, M. P., Hartmann, M. D., Lupas, A. N., & Alvarez, B. H. (2019) · Structure · doi:10.1016/j.str.2018.11.004 · Cited by 33

Cardiac-specific deficiency of the mitochondrial calcium uniporter augments fatty acid oxidation and functional reserve

Altamimi, T., Karwi, Q. G., Uddin, G. M., Fukushima, A., Kwong, J. Q., Molkentin, J. D., & Lopaschuk, G. D. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2018.12.019 · Cited by 33

Structure of the MICU1–MICU2 heterodimer provides insights into the gatekeeping threshold shift

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Nuclear-mitochondrial communication involving miR-181c plays an important role in cardiac dysfunction during obesity

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Yeast homologs of human MCUR1 regulate mitochondrial proline metabolism

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Coiled-coil domain containing 109B is a HIF1α-regulated gene critical for progression of human gliomas

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The Mitochondrial Ca 2+ Uniporter Complex (MCUC) of Trypanosoma brucei Is a Hetero-oligomer That Contains Novel Subunits Essential for Ca 2+ Uptake

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Functional analysis and importance for host cell infection of the Ca2+-conducting subunits of the mitochondrial calcium uniporter ofTrypanosoma cruzi

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Importance of mitochondrial calcium uniporter in high glucose–induced endothelial cell dysfunction

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Identification of LETM1 as a marker of cancer stem-like cells and predictor of poor prognosis in esophageal squamous cell carcinoma

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Mitochondrial calcium dysfunction contributes to autophagic cell death induced by MPP+ via AMPK pathway

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Transport of Ca2+ and Ca2+-Dependent Permeability Transition in Rat Liver Mitochondria under the Streptozotocin-Induced Type I Diabetes

Belosludtsev, K. N., Talanov, E. Y., Starinets, V. S., Agafonov, A. V., Dubinin, M. V., & Belosludtseva, N. V. (2019) · Cells · doi:10.3390/cells8091014 · Cited by 31

Mg2+ differentially regulates two modes of mitochondrial Ca2+ uptake in isolated cardiac mitochondria: implications for mitochondrial Ca2+ sequestration

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The gain-of-function enhancement of IP3-receptor channel gating by familial Alzheimer's disease-linked presenilin mutants increases the open probability of mitochondrial permeability transition pore

Toglia, P. T., & Ullah, G. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.05.002 · Cited by 30

LETM1 is a potential cancer stem-like cell marker and predicts poor prognosis in colorectal adenocarcinoma

Piao, L., Feng, Y., Yang, Z., Qi, W., Li, H., Han, H., & Xuan, Y. (2019) · Pathology - Research and Practice · doi:10.1016/j.prp.2019.152437 · Cited by 30

The Valosin-Containing Protein Protects the Heart Against Pathological Ca2+ Overload by Modulating Ca2+ Uptake Proteins

Stoll, S., Xi, J., Ma, B., Leimena, C., Behringer, E. J., Qin, G., & Qiu, H. (2019) · Toxicological Sciences · doi:10.1093/toxsci/kfz164 · Cited by 30

Discovery of EMRE in fungi resolves the true evolutionary history of the mitochondrial calcium uniporter

Pittis, A. A., Goh, V., Cebrian-Serrano, A., Wettmarshausen, J., Perocchi, F., & Gabaldón, T. (2020) · Nature Communications · doi:10.1038/s41467-020-17705-4 · Cited by 29

Mitochondrial calcium transport in trypanosomes

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Single α-Domain Constructs of the Na+/Ca2+Exchanger, NCLX, Oligomerize To Form a Functional Exchanger

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LETM1 haploinsufficiency causes mitochondrial defects in Wolf-Hirschhorn syndrome patient cells: implications for dissecting underlying pathomechanisms in this condition

Hart, L., Rauch, A. M., Carr, A. M., et al. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.014464 · Cited by 29

Inhibitory Interaction of the Plasma Membrane Na+/Ca2+ Exchangers with the 14-3-3 Proteins

Pulina, M. V., Rizzuto, R., Brini, M., & Carafoli, E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602033200 · Cited by 28

Identification of residues that control Li + versus Na + dependent Ca 2+ exchange at the transport site of the mitochondrial NCLX

Roy, S., Dey, K., Hershfinkel, M., Ohana, E., & Sekler, I. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.01.011 · Cited by 28

Slow activation of fast mitochondrial Ca2+ uptake by cytosolic Ca2+

Basso, E., Rigotto, G., Zucchetti, A. E., & Pozzan, T. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002332 · Cited by 28

The crystal structure of MICU2 provides insight into Ca2+ binding and MICU1‐MICU2 heterodimer formation

Wu, W., Shen, Q., Lei, Z., Qiu, Z., Li, D., Pei, H., Zheng, J., & Jia, Z. (2019) · EMBO Reports · doi:10.15252/embr.201847488 · Cited by 28

Variable Assembly of EMRE and MCU Creates Functional Channels with Distinct Gatekeeping Profiles

Payne, R. J., Li, C., & Foskett, J. K. (2020) · iScience · doi:10.1016/j.isci.2020.101037 · Cited by 28

TPP+ inhibits Na+-stimulated Ca2+ efflux from brain mitochondria

Karadjov, J. S., Kudzina, L. Y., & Зинченко, В. П. (1986) · Cell Calcium · doi:10.1016/0143-4160(86)90014-x · Cited by 27

Calpain-Inhibitors Protect Frataxin-Deficient Dorsal Root Ganglia Neurons from Loss of Mitochondrial Na+/Ca2+ Exchanger, NCLX, and Apoptosis

Britti, E., Delaspre, F., Tamarit, J., & Ros, J. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03020-3 · Cited by 27

Total Matrix Ca2+ Modulates Ca2+ Efflux via the Ca2+/H+ Exchanger in Cardiac Mitochondria

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MICU3 Plays an Important Role in Cardiovascular Function

Puente, B. N., Sun, J., Parks, R. J., Fergusson, M. M., Liu, C., Springer, D., Aponte, A. M., Liu, J. C., & Murphy, E. (2020) · Circulation Research · doi:10.1161/circresaha.120.317177 · Cited by 27

Developmental brain abnormalities and acute encephalopathy in a patient with myopathy with extrapyramidal signs secondary to pathogenic variants in MICU1

Wilton, K. M., Morales‐Rosado, J. A., Selcen, D., Muthusamy, K., Ewing, S., Agre, K. E., Nickels, K. C., Klee, E. W., Ho, M., & Morava, É. (2020) · JIMD Reports · doi:10.1002/jmd2.12114 · Cited by 26

Molecular signatures and functional analysis of beige adipocytes induced from in vivo intra-abdominal adipocytes

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The mRNA Decay Factor CAR-1/LSM14 Regulates Axon Regeneration via Mitochondrial Calcium Dynamics

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Roles of the mitochondrial Na+-Ca2+ exchanger, NCLX, in B lymphocyte chemotaxis

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MCUB and mitochondrial calcium uptake – modeling, function, and therapeutic potential

Lambert, J. P., Murray, E. K., & Elrod, J. W. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1732926 · Cited by 24

New players in high fat diet-induced obesity: LETM1 and CTMP

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SMDT1-driven change in mitochondrial dynamics mediate cell apoptosis in PDAC

Xie, K., Guo, D., & Luo, X. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.02.043 · Cited by 23

Dual Effect of Phosphate Transport on Mitochondrial Ca2+ Dynamics

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Elevated mRNA-levels of distinct mitochondrial and plasma membrane Ca2+ transporters in individual hypoglossal motor neurons of endstage SOD1 transgenic mice

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Gestation age-associated dynamics of mitochondrial calcium uniporter subunits expression in feto-maternal complex at term and preterm delivery

Vishnyakova, P., Tarasova, N. V., Volodina, M. A., Tsvirkun, D., Sukhanova, I. A., Kurchakova, T. A., Кан, Н. Е., Medzidova, M. K., Sukhikh, G. T., & Vysokikh, M. Y. (2019) · Scientific Reports · doi:10.1038/s41598-019-41996-3 · Cited by 22

Metabolite regulation of the mitochondrial calcium uniporter channel

Tomar, D., & Elrod, J. W. (2020) · Cell Calcium · doi:10.1016/j.ceca.2020.102288 · Cited by 22

Co-delivery of LETM1 and CTMP synergistically inhibits tumor growth in H-ras12V liver cancer model mice

Shin, J.-Y., Chung, Y.-S., Kang, B., Jiang, H., Yu, D., Han, K., Chae, C., Moon, J.-H., Jang, G., & Cho, M.-H. (2013) · Cancer Gene Therapy · doi:10.1038/cgt.2013.6 · Cited by 21

LETM1 overexpression is correlated with the clinical features and survival outcome of breast cancer.

Li, N., Zheng, Y., Xuan, C., Lin, Z., Piao, L., & Liu, S. (2015) · PubMed · Cited by 20

The NCLX-type Na+/Ca2+ Exchanger NCX-9 Is Required for Patterning of Neural Circuits in Caenorhabditis elegans

Sharma, V., Roy, S., Sekler, I., & O’Halloran, D. M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.758953 · Cited by 20

LETM1 is a potential biomarker that predicts poor prognosis in gastric adenocarcinoma

Li, H., Piao, L., Xu, D., & Xuan, Y. (2019) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2019.104333 · Cited by 20

The mitochondrial calcium uniporter contributes to morphine tolerance through pCREB and CPEB1 in rat spinal cord dorsal horn

Takahashi, K., Yi, H., Gu, J., Ikegami, D., Liu, S., Iida, T., Kashiwagi, Y., Dong, C., Kunisawa, T., & Hao, S. (2019) · British Journal of Anaesthesia · doi:10.1016/j.bja.2019.05.027 · Cited by 19

Is MCU dispensable for normal heart function?

Liu, J. C. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.04.028 · Cited by 19

Mitochondrial Carriers Regulating Insulin Secretion Profiled in Human Islets upon Metabolic Stress

Jiménez‐Sánchez, C., Brun, T., & Maechler, P. (2020) · Biomolecules · doi:10.3390/biom10111543 · Cited by 19

Oxygen Glucose Deprivation Induced Prosurvival Autophagy Is Insufficient to Rescue Endothelial Function

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Electrical recordings of the mitochondrial calcium uniporter in Xenopus oocytes

Tsai, C.-W., & Tsai, M.-F. (2018) · The Journal of General Physiology · doi:10.1085/jgp.201812015 · Cited by 16

Structure-dynamic and functional relationships in a Li+-transporting sodium‑calcium exchanger mutant

Giladi, M., Lee, S. Y., Refaeli, B., Hiller, R., Chung, K. Y., & Khananshvili, D. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.11.015 · Cited by 16

Investigation of mitochondrial calcium uniporter role in embryonic and adult motor neurons from G93AhSOD1 mice

Tadić, V., Adam, A., Goldhammer, N., Lautenschläger, J., Oberstadt, M., Malci, A., Le, T. T., Sengupta, S., Stubendorff, B., Keiner, S., et al. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.11.019 · Cited by 16

Reporting a rare form of myopathy, myopathy with extrapyramidal signs, in an Iranian family using next generation sequencing: a case report

Mojbafan, M., Nojehdeh, S. T., Rahiminejad, F., Nilipour, Y., Tonekaboni, S. H., & Zeinali, S. (2020) · BMC Medical Genetics · doi:10.1186/s12881-020-01016-y · Cited by 16

LETM1 Promotes Gastric Cancer Cell Proliferation, Migration, and Invasion via the PI3K/Akt Signaling Pathway

Zhang, Y., Chen, L., Cao, Y., Chen, S., Xu, C., Xing, J., & Zhang, K. (2020) · Journal of the Korean Gastric Cancer Association · doi:10.5230/jgc.2020.20.e12 · Cited by 15

Leucine Zipper-EF-Hand Containing Transmembrane Protein 1 Is a Potential Prognostic Biomarker and Promotes Cell Progression in Prostate Cancer

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Coupling of LETM1 up-regulation with oxidative phosphorylation and platelet-derived growth factor receptor signaling via YAP1 transactivation

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In vitro synthesis of the human calcium transporter Letm1 within cell-sized liposomes and investigation of its lipid dependency

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A swarm intelligence-based hybrid approach for identifying network modules

Atay, Y., Aslan, M. S., & Kodaz, H. (2017) · Journal of Computational Science · doi:10.1016/j.jocs.2017.10.011 · Cited by 4

Mitochondria: It is all about energy

Casanova, A., Wevers, A., Navarro-Ledesma, S., & Pruimboom, L. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1114231 · Cited by 303

Calcium Overload and Mitochondrial Metabolism

Walkon, L. L., Strubbe-Rivera, J. O., & Bazil, J. N. (2022) · Biomolecules · doi:10.3390/biom12121891 · Cited by 187

The roles of mitochondria in global and local intracellular calcium signalling

Cartes-Saavedra, B., Ghosh, A., & Hajnóczky, G. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00820-1 · Cited by 126

Mitochondrial calcium cycling in neuronal function and neurodegeneration

Walters, G. C., & Usachev, Y. M. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1094356 · Cited by 105

Mitochondria‐associated endoplasmic reticulum membrane: Overview and inextricable link with cancer

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