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Mitochondria: The Hub of Cellular Ca2+Signaling

Szabadkai, György, Duchen, Michael R.·2008·Physiology

DOI 10.1152/physiol.00046.2007

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Abstract

Mitochondria couple cellular metabolic state with Ca 2+transport processes. They therefore control not only their own intra-organelle [Ca 2+], but they also influence the entire cellular network of cellular Ca 2+signaling, including the endoplasmic reticulum, the plasma membrane, and the nucleus. Through the detailed study of mitochondrial roles in Ca 2+signaling, a remarkable picture of inter-organelle communication has emerged. We here review the ways in which this system provides integrity and flexibility for the cell to cope with the countless demands throughout its life cycle and discuss briefly the mechanisms through which it can also drive cell death.

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The versatility and universality of calcium signalling
Berridge, M. J., Lipp, P., & Bootman, M. D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036035 · Cited by 5,701
The Pathophysiology of Mitochondrial Cell Death
Green, D. R., & Kroemer, G. (2004) · Science · doi:10.1126/science.1099320 · Cited by 3,418
Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280
Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257
Peroxisome Proliferator-Activated Receptor-γ Coactivator 1α (PGC-1α): Transcriptional Coactivator and Metabolic Regulator
Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076
Sigma-1 Receptor Chaperones at the ER- Mitochondrion Interface Regulate Ca2+ Signaling and Cell Survival
Hayashi, T., & Su, T.-P. (2007) · Cell · doi:10.1016/j.cell.2007.08.036 · Cited by 1,826
Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T., & Tsujimoto, Y. (2005) · Nature · doi:10.1038/nature03317 · Cited by 1,635 · cited 1×
“the permeability transition (5, 62, 74), allowing as well”
Background
Mitochondrial Transport of Cations: Channels, Exchangers, and Permeability Transition
Bernardi, P. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1127 · Cited by 1,535
Translocation of Proteins into Mitochondria
Neupert, W., & Herrmann, J. M. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.163409 · Cited by 1,481
Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413
Self-citation
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
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 · cited 1×
“ply of reducing equivalents [NAD(P)H+] (67, 84, 86).”
Background
Structural and functional features and significance of the physical linkage between ER and mitochondria
Csordás, G., Renken, C., Várnai, P., Walter, L., Weaver, D., Buttle, K. F., Balla, T., Mannella, C. A., & Hajnóczky, G. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604016 · Cited by 1,373
Mitochondria and calcium: from cell signalling to cell death
Duchen, M. R. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.00057.x · Cited by 1,259
Self-citation
Microdomains with High Ca 2+ Close to IP 3 -Sensitive Channels that Are Sensed by Neighboring Mitochondria
Rizzuto, R., Brini, M., Murgia, M., & Pozzan, T. (1993) · Science · doi:10.1126/science.8235595 · Cited by 1,205
Phospholipid synthesis in a membrane fraction associated with mitochondria.
Vance, J. E. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39106-9 · Cited by 1,150
Advances in Male Contraception
Page, S. T., Amory, J. K., & Bremner, W. J. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0041 · Cited by 1,134
Decoding of cytosolic calcium oscillations in the mitochondria
Hajnóczky, G., Robb-Gaspers, L. D., Seitz, M. B., & Thomas, A. P. (1995) · Cell · doi:10.1016/0092-8674(95)90430-1 · Cited by 1,108
Peroxisome Proliferator-Activated Receptor γ Coactivator 1 Coactivators, Energy Homeostasis, and Metabolism
Handschin, C., & Spiegelman, B. M. (2006) · Endocrine Reviews · doi:10.1210/er.2006-0037 · Cited by 1,090
The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
Kokoszka, J. E., Waymire, K. G., Levy, S. E., Sligh, J. E., Cai, J., Jones, D. P., MacGregor, G. R., & Wallace, D. C. (2004) · Nature · doi:10.1038/nature02229 · Cited by 1,086
Reversible phosphorylation of Drp1 by cyclic AMP‐dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
Cribbs, J. T., & Strack, S. (2007) · The EMBO Reports · doi:10.1038/sj.embor.7401062 · Cited by 1,020
Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
Baines, C. P., Kaiser, R. A., Sheiko, T., Craigen, W. J., & Molkentin, J. D. (2007) · Nature Cell Biology · doi:10.1038/ncb1575 · Cited by 971
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 815
Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D
Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A., & Bernardi, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500089200 · Cited by 808 · cited 1×
“the permeability transition (5, 62, 74), allowing as well”
Background
The Machines that Divide and Fuse Mitochondria
Hoppins, S., Lackner, L., & Nunnari, J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.071905.090048 · Cited by 790
Mitochondria Are Excitable Organelles Capable of Generating and Conveying Electrical and Calcium Signals
Ichas, F., Jouaville, L. S., & Mazat, J.-P. (1997) · Cell · doi:10.1016/s0092-8674(00)80301-3 · Cited by 748
Mitochondrial retrograde signaling
Liu, Z., & Butow, R. A. (2006) · Annual Review of Genetics · doi:10.1146/annurev.genet.40.110405.090613 · Cited by 680
Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis
Deniaud, A., Sharaf el dein, O., Maillier, E., Poncet, D., Kroemer, G., Lemaire, C., & Brenner, C. (2008) · Oncogene · doi:10.1038/sj.onc.1210638 · Cited by 586
Mitochondrial-nuclear communications
Ryan, M. T., & Hoogenraad, N. J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052305.091720 · Cited by 575
Mitochondria as all‐round players of the calcium game
Rizzuto, R., Bernardi, P., & Pozzan, T. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.00037.x · Cited by 560
Capsaicin-induced ion fluxes in dorsal root ganglion cells in culture
Wood, J., Winter, J., James, I., Rang, H., Yeats, J., & Bevan, S. (1988) · The Journal of Neuroscience · doi:10.1523/jneurosci.08-09-03208.1988 · Cited by 559
Mitochondrial Participation in the Intracellular Ca2+ Network
Babcock, D. F., Herrington, J., Goodwin, P. C., Park, Y. B., & Hille, B. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.4.833 · Cited by 548
Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria
Csordas, G. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.96 · Cited by 540
Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
Breckenridge, D. G., Stojanovic, M., Marcellus, R. C., & Shore, G. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200212059 · Cited by 534
Mitochondrial Regulation of Store-operated Calcium Signaling in T Lymphocytes
Hoth, M., Fanger, C. M., & Lewis, R. S. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.3.633 · Cited by 506
Control of mitochondrial motility and distribution by the calcium signal
Yi, M., Weaver, D., & Hajnóczky, G. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406038 · Cited by 476
Drp-1-Dependent Division of the Mitochondrial Network Blocks Intraorganellar Ca2+ Waves and Protects against Ca2+-Mediated Apoptosis
Szabadkai, G., Simoni, A. M., Chami, M., Wieckowski, M. R., Youle, R. J., & Rizzuto, R. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.026 · Cited by 475
Self-citation
Chromaffin-cell stimulation triggers fast millimolar mitochondrial Ca2+ transients that modulate secretion
Montero, M., Alonso, M. T., Carnicero, E., Cuchillo-Ibáñez, I., Albillos, A., García, A. G., García-Sancho, J., & Alvarez, J. (2000) · Nature Cell Biology · doi:10.1038/35000001 · Cited by 471
The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking
Fransson, Å., Ruusala, A., & Aspenström, P. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.163 · Cited by 464
Recombinant expression of the voltage-dependent anion channel enhances the transfer of Ca2+ microdomains to mitochondria
Rapizzi, E., Pinton, P., Szabadkai, G., Wieckowski, M. R., Vandecasteele, G., Baird, G., Tuft, R. A., Fogarty, K. E., & Rizzuto, R. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205091 · Cited by 452
Self-citation
Mitochondrial Involvement in Post-Tetanic Potentiation of Synaptic Transmission
Tang, Y.-G., & Zucker, R. S. (1997) · Neuron · doi:10.1016/s0896-6273(00)81248-9 · Cited by 441
Stoichiometry of Respiratory Stimulation, Accumulation of Ca++ and Phosphate, and Oxidative Phosphorylation in Rat Liver Mitochondria
Rossi, C. S., & Lehninger, A. L. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91230-5 · Cited by 441
Inositol 1,4,5-Trisphosphate Receptors as Signal Integrators
Patterson, R. L., Boehning, D., & Snyder, S. H. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.071403.161303 · Cited by 441
Regulated and unregulated mitochondrial permeability transition pores: a new paradigm of pore structure and function?
He, L., & Lemasters, J. J. (2002) · FEBS Letters · doi:10.1016/s0014-5793(01)03314-2 · Cited by 434
Synchronization of calcium waves by mitochondrial substrates in Xenopus laevis oocytes
Jouaville, L. S., Ichas, F., Holmuhamedov, E. L., Camacho, P., & Lechleiter, J. D. (1995) · Nature · doi:10.1038/377438a0 · Cited by 427
Calcium and mitochondria
Gunter, T. E., Yule, D. I., Gunter, K. K., Eliseev, R. A., & Salter, J. D. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.03.071 · Cited by 407
Regulation of the intracellular free calcium concentration in single rat dorsal root ganglion neurones in vitro.
Thayer, S. A., & Miller, R. J. (1990) · The Journal of Physiology · doi:10.1113/jphysiol.1990.sp018094 · Cited by 403
IP3 receptor/Ca2+ channel: from discovery to new signaling concepts
Mikoshiba, K. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04825.x · Cited by 397
The Relationship between Free and Total Calcium Concentrations in the Matrix of Liver and Brain Mitochondria
Chalmers, S., & Nicholls, D. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212661200 · Cited by 389
Mitochondrial calcium transport: mechanisms and functions
Gunter, T. E., Buntinas, L., Sparagna, G., Eliseev, R., & Gunter, K. (2000) · Cell Calcium · doi:10.1054/ceca.2000.0168 · Cited by 378
The regulation of extramitochondrial free calcium ion concentration by rat liver mitochondria
Nicholls, D. G. (1978) · Biochemical Journal · doi:10.1042/bj1760463 · Cited by 373
Subtype-Specific and ER Lumenal Environment-Dependent Regulation of Inositol 1,4,5-Trisphosphate Receptor Type 1 by ERp44
Higo, T., Hattori, M., Nakamura, T., Natsume, T., Michikawa, T., & Mikoshiba, K. (2005) · Cell · doi:10.1016/j.cell.2004.11.048 · Cited by 373
Integrating cytosolic calcium signals into mitochondrial metabolic responses
Robb-Gaspers, L. D. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.4987 · Cited by 370
Why Do We Still Have a Maternally Inherited Mitochondrial DNA? Insights from Evolutionary Medicine
Wallace, D. C. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.081205.150955 · Cited by 363
Active mitochondria surrounding the pancreatic acinar granule region prevent spreading of inositol trisphosphate-evoked local cytosolic Ca2+ signals
Tinel, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.18.4999 · Cited by 361
Mitochondria and calcium signaling
Nicholls, D. G. (2005) · Cell Calcium · doi:10.1016/j.ceca.2005.06.011 · Cited by 349
Ca2+-dependent changes in the mitochondrial energetics in single dissociated mouse sensory neurons
Duchen, M. R. (1992) · Biochemical Journal · doi:10.1042/bj2830041 · Cited by 338
Self-citation
Uncoupling proteins 2 and 3 are fundamental for mitochondrial Ca2+ uniport
Trenker, M., Malli, R., Fertschai, I., Levak-Frank, S., & Graier, W. F. (2007) · Nature Cell Biology · doi:10.1038/ncb1556 · Cited by 333
Perinuclear, perigranular and sub-plasmalemmal mitochondria have distinct functions in the regulation of cellular calcium transport
Park, M. K. (2001) · The EMBO Journal · doi:10.1093/emboj/20.8.1863 · Cited by 319
Mitochondrial Ion Channels
O’Rourke, B. (2007) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.031905.163804 · Cited by 310
Mitochondrial Calcium Uptake from Physiological-type Pulses of Calcium
Sparagna, G. C., Gunter, K. K., Sheu, S.-S., & Gunter, T. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.46.27510 · Cited by 309
Increased longevity and refractoriness to Ca2+-dependent neurodegeneration in Surf1 knockout mice
Dell'Agnello, C., Leo, S., Agostino, A., Szabadkai, G., Tiveron, C., Zulian, A., Prelle, A., Roubertoux, P., Rizzuto, R., & Zeviani, M. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddl477 · Cited by 308
Self-citation
Mitochondrial calcium transport
Nicholls, D. G., & Crompton, M. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)80806-4 · Cited by 306
The voltage-dependent anion channel-1 modulates apoptotic cell death
Zaid, H., Abu-Hamad, S., Israelson, A., Nathan, I., & Shoshan-Barmatz, V (2005) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401599 · Cited by 300
Mitochondria Exert a Negative Feedback on the Propagation of Intracellular Ca2+ Waves in Rat Cortical Astrocytes
Boitier, E., Rea, R., & Duchen, M. R. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.4.795 · Cited by 298
Self-citation
VDAC closure increases calcium ion flux
Tan, W., & Colombini, M. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.06.002 · Cited by 281
Mitochondria Suppress Local Feedback Activation of Inositol 1,4,5-Trisphosphate Receptors by Ca2+
Hajnóczky, G., Hager, R., & Thomas, A. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.14157 · Cited by 263
Mitochondrial intermembrane junctional complexes and their involvement in cell death
Crompton, M., Barksby, E., Johnson, N., & Capano, M. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01368-8 · Cited by 258
Cytoplasmic dynein regulates the subcellular distribution of mitochondria by controlling the recruitment of the fission factor dynamin-related protein-1
Varadi, A., Johnson-Cadwell, L. I., Cirulli, V., Yoon, Y., Allan, V. J., & Rutter, G. A. (2004) · Journal of Cell Science · doi:10.1242/jcs.01299 · Cited by 242
[17] Imaging mitochondrial function in intact cells
Duchen, M. R., Surin, A., & Jacobson, J. (2003) · Methods in Enzymology · doi:10.1016/s0076-6879(03)61019-0 · Cited by 237
Self-citation
Sperm-triggered [Ca2+] oscillations and Ca2+homeostasis in the mouse egg have an absolute requirement for mitochondrial ATP production
Dumollard, R., Marangos, P., Fitzharris, G., Swann, K., Duchen, M., & Carroll, J. (2004) · Development · doi:10.1242/dev.01181 · Cited by 233
Self-citation
Respiring mitochondria determine the pattern of activation and inactivation of the store-operated Ca2+ current ICRAC
Gilabert, J. A. (2000) · The EMBO Journal · doi:10.1093/emboj/19.23.6401 · Cited by 231
Modulating sarco(endo)plasmic reticulum Ca2+ ATPase 2 (SERCA2) activity: Cell biological implications
Vangheluwe, P., Raeymaekers, L., Dode, L., & Wuytack, F. (2005) · Cell Calcium · doi:10.1016/j.ceca.2005.06.033 · Cited by 226
Ca2+-dependent Control of the Permeability Properties of the Mitochondrial Outer Membrane and Voltage-dependent Anion-selective Channel (VDAC)
Báthori, G., Csordás, G., Garcia-Perez, C., Davies, E., & Hajnóczky, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600906200 · Cited by 224
Mitochondrial protein-import machinery: correlating structure with function
Baker, M. J., Frazier, A. E., Gulbis, J. M., & Ryan, M. T. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.07.010 · Cited by 213
Cardiac adenoviral S100A1 gene delivery rescues failing myocardium
Most, P., Pleger, S. T., Völkers, M., Heidt, B., Boerries, M., Weichenhan, D., Löffler, E., Janssen, P. M. L., Eckhart, A. D., Martini, J., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200421454 · Cited by 213
A fundamental system of cellular energy homeostasis regulated by PGC-1α
Rohas, L. M., St-Pierre, J., Uldry, M., Jäger, S., Handschin, C., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702683104 · Cited by 208
Mitochondrial dynamics and Ca2+ signaling
Szabadkai, G., Simoni, A. M., Bianchi, K., De Stefani, D., Leo, S., Wieckowski, M. R., & Rizzuto, R. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.04.002 · Cited by 204
Self-citation
Ca2+ Homeostasis during Mitochondrial Fragmentation and Perinuclear Clustering Induced by hFis1
Frieden, M., James, D., Castelbou, C., Danckaert, A., Martinou, J.-C., & Demaurex, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312366200 · Cited by 203
A Role for Calcium Influx in the Regulation of Mitochondrial Calcium in Endothelial Cells
Lawrie, A. M., Rizzuto, R., Pozzan, T., & Simpson, A. W. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.18.10753 · Cited by 186
Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca 2+ release channels
Yang, J., McBride, S., Mak, D.-O. D., Vardi, N., Palczewski, K., Haeseleer, F., & Foskett, J. K. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.102006299 · Cited by 186
Ca2+ Homeostasis in the Agonist-sensitive Internal Store: Functional Interactions Between Mitochondria and the ER Measured In Situ in Intact Cells
Landolfi, B., Curci, S., Debellis, L., Pozzan, T., & Hofer, A. M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.5.1235 · Cited by 185
Mitochondrial signaling pathways: A receiver/integrator organelle
Goldenthal, M. J., & Marín-García, J. (2004) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000038228.85494.3b · Cited by 184
Sustained Ca2+ Transfer across Mitochondria Is Essential for Mitochondrial Ca2+ Buffering, Store-operated Ca2+ Entry, and Ca2+ Store Refilling
Malli, R., Frieden, M., Osibow, K., Zoratti, C., Mayer, M., Demaurex, N., & Graier, W. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302511200 · Cited by 175
Evidence that mitochondria buffer physiological Ca2+ loads in lizard motor nerve terminals
David, G., Barrett, J. N., & Barrett, E. F. (1998) · The Journal of Physiology · doi:10.1111/j.1469-7793.1998.059bo.x · Cited by 168
Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis
LI, Y., JOHNSON, N., CAPANO, M., EDWARDS, M., & CROMPTON, M. (2004) · Biochemical Journal · doi:10.1042/bj20040669 · Cited by 162
The Integration of Mitochondrial Calcium Transport and Storage
Nicholls, D. G., & Chalmers, S. (2004) · Journal of Bioenergetics and Biomembranes · doi:10.1023/b:jobb.0000041753.52832.f3 · Cited by 162
A historical review of cellular calcium handling, with emphasis on mitochondria
Saris, N.-E. L., & Carafoli, E. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0100-9 · Cited by 159
The rapid mode of calcium uptake into heart mitochondria (RaM): comparison to RaM in liver mitochondria
Buntinas, L., Gunter, K. K., Sparagna, G. C., & Gunter, T. E. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00254-1 · Cited by 149
The Role of Mitochondria for Ca2+ Refilling of the Endoplasmic Reticulum
Malli, R., Frieden, M., Trenker, M., & Graier, W. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409353200 · Cited by 147
Kinetics of calcium(2+) ion carrier in rat liver mitochondria
Bragadin, M., Pozzan, T., & AZZONE, G. F. (1979) · Biochemistry · doi:10.1021/bi00593a033 · Cited by 147
The Sodium-Calcium Antiport of Heart Mitochondria Is Not Electroneutral
Jung, D. W., Baysal, K., & Brierley, G. P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.672 · Cited by 146
Mitochondria-to-nucleus stress signaling in mammalian cells: Nature of nuclear gene targets, transcription regulation, and induced resistance to apoptosis
Biswas, G., Guha, M., & Avadhani, N. G. (2005) · Gene · doi:10.1016/j.gene.2005.03.028 · Cited by 144
Mitochondrial permeability transition in apoptosis and necrosis
Zamzami, N., Larochette, N., & Kroemer, G. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401682 · Cited by 137
Calcium and mitochondria: mechanisms and functions of a troubled relationship
Bianchi, K., Rimessi, A., Prandini, A., Szabadkai, G., & Rizzuto, R. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.015 · Cited by 134
Self-citation
Biphasic Regulation of Mitochondrial Ca2+ Uptake by Cytosolic Ca2+ Concentration
Moreau, B., Nelson, C., & Parekh, A. B. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.059 · Cited by 132
The Role of Phosphate in the Regulation of the Independent Calcium‐Efflux Pathway of Liver Mitochondria
Zoccarato, F., & Nicholls, D. G. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06875.x · Cited by 125
Pyridine nucleotide redox state parallels production of aldosterone in potassium-stimulated adrenal glomerulosa cells.
Pralong, W. F., Hunyady, L., Várnai, P., Wollheim, C. B., & Spät, A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.1.132 · Cited by 104
Cytopathic effects of the cytomegalovirus-encoded apoptosis inhibitory protein vMIA
Poncet, D., Pauleau, A., Szabadkai, G., Vozza, A., Scholz, S. R., Bras, M. L., Brière, J.-J., Jalil, A., Moigne, R. L., Brenner, C., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604069 · Cited by 104
Self-citation
HSP70 Binds to the Fast-twitch Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA1a) and Prevents Thermal Inactivation
Tupling, A. R., Gramolini, A. O., Duhamel, T. A., Kondo, H., Asahi, M., Tsuchiya, S. C., Borrelli, M. J., Lepock, J. R., Otsu, K., Hori, M., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409336200 · Cited by 96
Mitochondria respond to Ca2+ already in the submicromolar range: correlation with redox state
Pitter, J. G., Maechler, P., Wollheim, C. B., & Spät, A. (2002) · Cell Calcium · doi:10.1054/ceca.2001.0264 · Cited by 95
Mitochondrial Ca2+-induced Ca2+Release Mediated by the Ca2+Uniporter
Montero, M., Alonso, M. T., Albillos, A., García-Sancho, J., & Álvarez, J. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.1.63 · Cited by 91
tcBid promotes Ca2+ signal propagation to the mitochondria: control of Ca2+ permeation through the outer mitochondrial membrane
Csordás, G., Madesh, M., Antonsson, B. E., & Hajnóczky, G. (2002) · The EMBO Journal · doi:10.1093/emboj/21.9.2198 · Cited by 83
Heat Shock Suppresses the Permeability Transition in Rat Liver Mitochondria
He, L., & Lemasters, J. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300153200 · Cited by 82
Mitochondrial Regulation of Intracellular Ca2+ Signaling: More Than Just Simple Ca2+ Buffers
Parekh, A. B. (2003) · Physiology · doi:10.1152/nips.01458.2003 · Cited by 82
EGTA inhibits reverse uniport-dependent Ca2+ release from uncoupled mitochondria. Possible regulation of the Ca2+ uniporter by a Ca2+ binding site on the cytoplasmic side of the inner membrane.
Igbavboa, U., & Pfeiffer, D. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57318-5 · Cited by 81
Inhibition of Ca2+ Sparks by Ruthenium Red in Permeabilized Rat Ventricular Myocytes
Lukyanenko, V. I., Györke, I., Subramanian, S., et al. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76381-8 · Cited by 76
Subplasmalemmal Mitochondria Modulate the Activity of Plasma Membrane Ca2+-ATPases
Frieden, M., Arnaudeau, S., Castelbou, C., & Demaurex, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510279200 · Cited by 74
The stoichiometry of the exchange catalysed by the mitochondrial calcium/sodium antiporter
Brand, M. D. (1985) · Biochemical Journal · doi:10.1042/bj2290161 · Cited by 73
CIB1, a Ubiquitously Expressed Ca2+-binding Protein Ligand of the InsP3 Receptor Ca2+ Release Channel
White, C., Yang, J., Monteiro, M. J., & Foskett, J. K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602175200 · Cited by 61
Regulation of Ca2+ signalling and Ca2+-mediated cell death by the transcriptional coactivator PGC-1α
Bianchi, K., Vandecasteele, G., Carli, C., Romagnoli, A., Szabadkai, G., & Rizzuto, R. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401784 · Cited by 60
Self-citation
Mitochondrial Ca2+ Dynamics Reveals Limited Intramitochondrial Ca2+ Diffusion
Gerencser, A. A., & Ádám‐Vizi, V. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.050062 · Cited by 58
Activation of a Novel Calcineurin-mediated Insulin-like Growth Factor-1 Receptor Pathway, Altered Metabolism, and Tumor Cell Invasion in Cells Subjected to Mitochondrial Respiratory Stress
Guha, M., Srinivasan, S., Biswas, G., & Avadhani, N. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611693200 · Cited by 54
Erratum to “Probing neural circuits in the zebrafish: a suite of optical techniques” [Methods 30 (2003) 49–63]
O’Malley, D. M., Zhou, Q., & Gahtan, E. (2003) · Methods · doi:10.1016/s1046-2023(03)00130-0 · Cited by 50
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
Mitochondrial Calcium in Relaxed and Tetanized Myocardium
Horikawa, Y., Goel, A., Somlyo, A. P., & Somlyo, A. V. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77869-5 · Cited by 43
Participation of p38 MAPK and a novel-type protein kinase C in the control of mitochondrial Ca2+ uptake
Szanda, G., Koncz, P., Rajki, A., & Spät, A. (2007) · Cell Calcium · doi:10.1016/j.ceca.2007.05.013 · Cited by 41
Functional analysis of the promoter of the mitochondrial phosphate carrier human gene: identification of activator and repressor elements and their transcription factors
Iacobazzi, V., Infantino, V., Costanzo, P., Izzo, P., & Palmieri, F. (2005) · Biochemical Journal · doi:10.1042/bj20050776 · Cited by 38
‘What nourishes me, destroys me’: towards a new mitochondrial biology
Jacobson, J., & Duchen, M. R. (2001) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400911 · Cited by 18
Self-citation

A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
De Stefani, D., Raffaello, A., Teardo, E., Szabò, I., & Rizzuto, R. (2011) · Nature · doi:10.1038/nature10230 · Cited by 1,915
Physiology of Astroglia
Verkhratsky, A., & Nedergaard, M. (2018) · Physiological Reviews · doi:10.1152/physrev.00042.2016 · Cited by 1,678
Essential Regulation of Cell Bioenergetics by Constitutive InsP3 Receptor Ca2+ Transfer to Mitochondria
Cárdenas, C., Miller, R. A., Smith, I., Bui, T., Molgó, J., Müller, M., Vais, H., Cheung, K.-H., Yang, J., Parker, I., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.007 · Cited by 1,026
Mitochondrial dysfunction and oxidative stress in heart disease
Peoples, J. N., Saraf, A., Ghazal, N., Pham, T. T., & Kwong, J. Q. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0355-7 · Cited by 950
MAM: more than just a housekeeper
Hayashi, T., Rizzuto, R., Hajnoczky, G., & Su, T.-P. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.12.002 · Cited by 787

See all 403

Authors: Szabadkai, G., & Duchen, M. R.
Venue: Physiology
Publisher: American Physiological Society
Published: 2008-04
Volume: 23
Issue: 2
Pages: 84-94
ISSN: 0886-1714 (ISSN-L)
1548-9213
1548-9221
DOI: 10.1152/physiol.00046.2007
OpenAlex: W2033673006
Cited by: 403
References: 119
FWCI: 12.78
Type: journal article
Language: en
Open access: closed

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Mitochondria: The Hub of Cellular Ca2+Signaling

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