Molecular mechanism of mitochondrial calcium uptake

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• 作者：Lele Wang (1)
  Xue Yang (1)
  Yuequan Shen (1) (2) (3)
  
  1. State Key Laboratory of Medicinal Chemical Biology ; Nankai University ; 94 Weijin Road ; Tianjin ; 300071 ; China
  2. College of Life Sciences ; Nankai University ; 94 Weijin Road ; Tianjin ; 300071 ; China
  3. Collaborative Innovation Center of Chemical Science and Engineering (Tianjin) ; Tianjin ; 300072 ; China
  
• 关键词：Calcium signaling ; Calcium channel ; VDAC ; MCU ; MICU ; EMRE ; MCUR1
• 刊名：Cellular and Molecular Life Sciences (CMLS)
• 出版年：2015
• 出版时间：April 2015
• 年：2015
• 卷：72
• 期：8
• 页码：1489-1498
• 全文大小：1,023 KB
• 参考文献：1. Rizzuto, R, Stefani, D, Raffaello, A, Mammucari, C (2012) Mitochondria as sensors and regulators of calcium signalling. Nat Rev Mol Cell Biol 13: pp. 566-578 412" target="_blank" title="It opens in new window">CrossRef
  2. Chandel, NS (2014) Mitochondria as signaling organelles. BMC Biol 12: pp. 34 41-7007-12-34" target="_blank" title="It opens in new window">CrossRef
  3. Pagliarini, DJ, Rutter, J (2013) Hallmarks of a new era in mitochondrial biochemistry. Genes Dev 27: pp. 2615-2627 4.113" target="_blank" title="It opens in new window">CrossRef
  4. Clapham, DE (2007) Calcium signaling. Cell 131: pp. 1047-1058 CrossRef
  5. Carafoli, E (2010) The fateful encounter of mitochondria with calcium: how did it happen?. Biochim Biophys Acta 1797: pp. 595-606 4" target="_blank" title="It opens in new window">CrossRef
  6. Graier, WF, Frieden, M, Malli, R (2007) Mitochondria and Ca(2+) signaling: old guests, new functions. Pflugers Arch 455: pp. 375-396 424-007-0296-1" target="_blank" title="It opens in new window">CrossRef
  7. Duchen, MR (2000) Mitochondria and calcium: from cell signalling to cell death. J Physiol 529: pp. 57-68 469-7793.2000.00057.x" target="_blank" title="It opens in new window">CrossRef
  8. Feske, S, Skolnik, EY, Prakriya, M (2012) Ion channels and transporters in lymphocyte function and immunity. Nat Rev Immunol 12: pp. 532-547 CrossRef
  9. Rowland, AA, Voeltz, GK (2012) Endoplasmic reticulum-mitochondria contacts: function of the junction. Nat Rev Mol Cell Biol 13: pp. 607-625 440" target="_blank" title="It opens in new window">CrossRef
  10. Herrington, J, Park, YB, Babcock, DF, Hille, B (1996) Dominant role of mitochondria in clearance of large Ca2+ loads from rat adrenal chromaffin cells. Neuron 16: pp. 219-228 CrossRef
  11. Babcock, DF, Herrington, J, Goodwin, PC, Park, YB, Hille, B (1997) Mitochondrial participation in the intracellular Ca2+ network. J Cell Biol 136: pp. 833-844 4.833" target="_blank" title="It opens in new window">CrossRef
  12. Jouaville, LS, Ichas, F, Holmuhamedov, EL, Camacho, P, Lechleiter, JD (1995) Synchronization of calcium waves by mitochondrial substrates in Xenopus laevis oocytes. Nature 377: pp. 438-441 438a0" target="_blank" title="It opens in new window">CrossRef
  13. Boitier, E, Rea, R, Duchen, MR (1999) Mitochondria exert a negative feedback on the propagation of intracellular Ca2+ waves in rat cortical astrocytes. J Cell Biol 145: pp. 795-808 45.4.795" target="_blank" title="It opens in new window">CrossRef
  14. Denton, RM, McCormack, JG (1980) The role of calcium in the regulation of mitochondrial metabolism. Biochem Soc Trans 8: pp. 266-268
  15. McCormack, JG, Denton, RM (1979) The effects of calcium ions and adenine nucleotides on the activity of pig heart 2-oxoglutarate dehydrogenase complex. Biochem J 180: pp. 533-544
  16. Jouaville, LS, Pinton, P, Bastianutto, C, Rutter, GA, Rizzuto, R (1999) Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming. Proc Natl Acad Sci USA 96: pp. 13807-13812 4.13807" target="_blank" title="It opens in new window">CrossRef
  17. Orrenius, S, Zhivotovsky, B, Nicotera, P (2003) Regulation of cell death: the calcium-apoptosis link. Nat Rev Mol Cell Biol 4: pp. 552-565 CrossRef
  18. Hajnoczky, G, Csordas, G, Madesh, M, Pacher, P (2000) Control of apoptosis by IP(3) and ryanodine receptor driven calcium signals. Cell Calcium 28: pp. 349-363 4/ceca.2000.0169" target="_blank" title="It opens in new window">CrossRef
  19. Szalai, G, Krishnamurthy, R, Hajnoczky, G (1999) Apoptosis driven by IP(3)-linked mitochondrial calcium signals. EMBO J 18: pp. 6349-6361 49" target="_blank" title="It opens in new window">CrossRef
  20. Pinton, P, Ferrari, D, Rapizzi, E, Virgilio, F, Pozzan, T, Rizzuto, R (2001) The Ca2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: significance for the molecular mechanism of Bcl-2 action. EMBO J 20: pp. 2690-2701 CrossRef
  21. Scorrano, L, Oakes, SA, Opferman, JT, Cheng, EH, Sorcinelli, MD, Pozzan, T, Korsmeyer, SJ (2003) BAX and BAK regulation of endoplasmic reticulum Ca2+: a control point for apoptosis. Science 300: pp. 135-139 CrossRef
  22. Deluca, HF, Engstrom, GW (1961) Calcium uptake by rat kidney mitochondria. Proc Natl Acad Sci USA 47: pp. 1744-1750 47.11.1744" target="_blank" title="It opens in new window">CrossRef
  23. Vasington, FD, Murphy, JV (1962) Ca ion uptake by rat kidney mitochondria and its dependence on respiration and phosphorylation. J Biol Chem 237: pp. 2670-2677
  24. Brand, MD, Chen, CH, Lehninger, AL (1976) Stoichiometry of H+ ejection during respiration-dependent accumulation of Ca2+ by rat liver mitochondria. J Biol Chem 251: pp. 968-974
  25. Kirichok, Y, Krapivinsky, G, Clapham, DE (2004) The mitochondrial calcium uniporter is a highly selective ion channel. Nature 427: pp. 360-364 46" target="_blank" title="It opens in new window">CrossRef
  26. Rottenberg, H, Scarpa, A (1974) Calcium uptake and membrane potential in mitochondria. Biochemistry 13: pp. 4811-4817 CrossRef
  27. Drago, I, Pizzo, P, Pozzan, T (2011) After half a century mitochondrial calcium in- and efflux machineries reveal themselves. EMBO J 30: pp. 4119-4125 CrossRef
  28. Rizzuto, R, Pozzan, T (2006) Microdomains of intracellular Ca2+: molecular determinants and functional consequences. Physiol Rev 86: pp. 369-408 4.2005" target="_blank" title="It opens in new window">CrossRef
  29. Rizzuto, R, Pinton, P, Carrington, W, Fay, FS, Fogarty, KE, Lifshitz, LM, Tuft, RA, Pozzan, T (1998) Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses. Science 280: pp. 1763-1766 CrossRef
  30. Csordas, G, Thomas, AP, Hajnoczky, G (1999) Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria. EMBO J 18: pp. 96-108 CrossRef
  31. Shoshan-Barmatz, V, Ben-Hail, D (2012) VDAC, a multi-functional mitochondrial protein as a pharmacological target. Mitochondrion 12: pp. 24-34 4.001" target="_blank" title="It opens in new window">CrossRef
  32. Bathori, G, Csordas, G, Garcia-Perez, C, Davies, E, Hajnoczky, G (2006) Ca2+-dependent control of the permeability properties of the mitochondrial outer membrane and voltage-dependent anion-selective channel (VDAC). J Biol Chem 281: pp. 17347-17358 4/jbc.M600906200" target="_blank" title="It opens in new window">CrossRef
  33. Shoshan-Barmatz, V, Israelson, A, Brdiczka, D, Sheu, SS (2006) The voltage-dependent anion channel (VDAC): function in intracellular signalling, cell life and cell death. Curr Pharm Des 12: pp. 2249-2270 4/138161206777585111" target="_blank" title="It opens in new window">CrossRef
  34. Hodge, T, Colombini, M (1997) Regulation of metabolite flux through voltage-gating of VDAC channels. J Membr Biol 157: pp. 271-279 CrossRef
  35. Shoshan-Barmatz, V, Pinto, V, Zweckstetter, M, Raviv, Z, Keinan, N, Arbel, N (2010) VDAC, a multi-functional mitochondrial protein regulating cell life and death. Mol Aspects Med 31: pp. 227-285 CrossRef
  36. Stefani, D, Bononi, A, Romagnoli, A, Messina, A, Pinto, V, Pinton, P, Rizzuto, R (2012) VDAC1 selectively transfers apoptotic Ca2+ signals to mitochondria. Cell Death Differ 19: pp. 267-273 CrossRef
  37. Gincel, D, Zaid, H, Shoshan-Barmatz, V (2001) Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function. Biochem J 358: pp. 147-155 42/0264-6021:3580147" target="_blank" title="It opens in new window">CrossRef
  38. Tsai, MF, Jiang, D, Zhao, L, Clapham, D, Miller, C (2014) Functional reconstitution of the mitochondrial Ca2+/H+ antiporter Letm1. J Gen Physiol 143: pp. 67-73 CrossRef
  39. Bayrhuber, M, Meins, T, Habeck, M, Becker, S, Giller, K, Villinger, S, Vonrhein, C, Griesinger, C, Zweckstetter, M, Zeth, K (2008) Structure of the human voltage-dependent anion channel. Proc Natl Acad Sci USA 105: pp. 15370-15375 CrossRef
  40. Ujwal, R, Cascio, D, Colletier, JP, Faham, S, Zhang, J, Toro, L, Ping, P, Abramson, J (2008) The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating. Proc Natl Acad Sci USA 105: pp. 17742-17747 4105" target="_blank" title="It opens in new window">CrossRef
  41. Hiller, S, Garces, RG, Malia, TJ, Orekhov, VY, Colombini, M, Wagner, G (2008) Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science 321: pp. 1206-1210 CrossRef
  42. Abu-Hamad, S, Arbel, N, Calo, D, Arzoine, L, Israelson, A, Keinan, N, Ben-Romano, R, Friedman, O, Shoshan-Barmatz, V (2009) The VDAC1N-terminus is essential both for apoptosis and the protective effect of anti-apoptotic proteins. J Cell Sci 122: pp. 1906-1916 42/jcs.040188" target="_blank" title="It opens in new window">CrossRef
  43. Zheng, L, Stathopulos, PB, Li, GY, Ikura, M (2008) Biophysical characterization of the EF-hand and SAM domain containing Ca2+ sensory region of STIM1 and STIM2. Biochem Biophys Res Commun 369: pp. 240-246 CrossRef
  44. Joiner, ML, Koval, OM, Li, J, He, BJ, Allamargot, C, Gao, Z, Luczak, ED, Hall, DD, Fink, BD, Chen, B (2012) CaMKII determines mitochondrial stress responses in heart. Nature 491: pp. 269-273 444" target="_blank" title="It opens in new window">CrossRef
  45. Israelson, A, Abu-Hamad, S, Zaid, H, Nahon, E, Shoshan-Barmatz, V (2007) Localization of the voltage-dependent anion channel-1 Ca2+-binding sites. Cell Calcium 41: pp. 235-244 CrossRef
  46. Israelson, A, Zaid, H, Abu-Hamad, S, Nahon, E, Shoshan-Barmatz, V (2008) Mapping the ruthenium red-binding site of the voltage-dependent anion channel-1. Cell Calcium 43: pp. 196-204 CrossRef
  47. Perocchi, F, Gohil, VM, Girgis, HS, Bao, XR, McCombs, JE, Palmer, AE, Mootha, VK (2010) MICU1 encodes a mitochondrial EF hand protein required for Ca(2+) uptake. Nature 467: pp. 291-296 CrossRef
  48. Collins, S, Meyer, T (2010) Cell biology: a sensor for calcium uptake. Nature 467: pp. 283 467283a" target="_blank" title="It opens in new window">CrossRef
  49. Sancak, Y, Markhard, AL, Kitami, T, Kovacs-Bogdan, E, Kamer, KJ, Udeshi, ND, Carr, SA, Chaudhuri, D, Clapham, DE, Li, AA (2013) EMRE is an essential component of the mitochondrial calcium uniporter complex. Science 342: pp. 1379-1382 42993" target="_blank" title="It opens in new window">CrossRef
  50. Hajnoczky, G, Csordas, G (2010) Calcium signalling: fishing out molecules of mitochondrial calcium transport. Curr Biol 20: pp. R888-R891 CrossRef
  51. Bick, AG, Calvo, SE, Mootha, VK (2012) Evolutionary diversity of the mitochondrial calcium uniporter. Science 336: pp. 886 4977" target="_blank" title="It opens in new window">CrossRef
  52. Baughman, JM, Perocchi, F, Girgis, HS, Plovanich, M, Belcher-Timme, CA, Sancak, Y, Bao, XR, Strittmatter, L, Goldberger, O, Bogorad, RL (2011) Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter. Nature 476: pp. 341-345 4" target="_blank" title="It opens in new window">CrossRef
  53. Mallilankaraman, K, Doonan, P, Cardenas, C, Chandramoorthy, HC, Muller, M, Miller, R, Hoffman, NE, Gandhirajan, RK, Molgo, J, Birnbaum, MJ (2012) MICU1 is an essential gatekeeper for MCU-mediated mitochondrial Ca(2+) uptake that regulates cell survival. Cell 151: pp. 630-644 CrossRef
  54. Hoffman, NE, Chandramoorthy, HC, Shamugapriya, S, Zhang, X, Rajan, S, Mallilankaraman, K, Gandhirajan, RK, Vagnozzi, RJ, Ferrer, LM, Sreekrishnanilayam, K (2013) MICU1 motifs define mitochondrial calcium uniporter binding and activity. Cell Rep 5: pp. 1576-1588 CrossRef
  55. Wang, L, Yang, X, Li, S, Wang, Z, Liu, Y, Feng, J, Zhu, Y, Shen, Y (2014) Structural and mechanistic insights into MICU1 regulation of mitochondrial calcium uptake. EMBO J 33: pp. 594-604 CrossRef
  56. Csordas, G, Golenar, T, Seifert, EL, Kamer, KJ, Sancak, Y, Perocchi, F, Moffat, C, Weaver, D, Perez, SDLF, Bogorad, R (2013) MICU1 controls both the threshold and cooperative activation of the mitochondrial Ca2+ uniporter. Cell Metab 17: pp. 976-987 4.020" target="_blank" title="It opens in new window">CrossRef
  57. Patron, M, Checchetto, V, Raffaello, A, Teardo, E, Vecellio Reane, D, Mantoan, M, Granatiero, V, Szabo, I, Stefani, D, Rizzuto, R (2014) MICU1 and MICU2 finely tune the mitochondrial Ca2+ uniporter by exerting opposite effects on MCU activity. Mol Cell 53: pp. 726-737 4.01.013" target="_blank" title="It opens in new window">CrossRef
  58. Hung, V, Zou, P, Rhee, HW, Udeshi, ND, Cracan, V, Svinkina, T, Carr, SA, Mootha, VK, Ting, AY (2014) Proteomic mapping of the human mitochondrial intermembrane space in live cells via ratiometric APEX tagging. Mol Cell 55: pp. 332-341 4.06.003" target="_blank" title="It opens in new window">CrossRef
  59. Kamer, KJ, Mootha, VK (2014) MICU1 and MICU2 play nonredundant roles in the regulation of the mitochondrial calcium uniporter. EMBO Rep 15: pp. 299-307 46" target="_blank" title="It opens in new window">CrossRef
  60. Plovanich, M, Bogorad, RL, Sancak, Y, Kamer, KJ, Strittmatter, L, Li, AA, Girgis, HS, Kuchimanchi, S, Groot, J, Speciner, L (2013) MICU2, a paralog of MICU1, resides within the mitochondrial uniporter complex to regulate calcium handling. PLoS ONE 8: pp. e55785 CrossRef
  61. Ahuja, M, Muallem, S (2014) The gatekeepers of mitochondrial calcium influx: mICU1 and MICU2. EMBO Rep 15: pp. 205-206 438446" target="_blank" title="It opens in new window">CrossRef
  62. Stefani, D, Raffaello, A, Teardo, E, Szabo, I, Rizzuto, R (2011) A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter. Nature 476: pp. 336-340 CrossRef
  63. Raffaello, A, Stefani, D, Sabbadin, D, Teardo, E, Merli, G, Picard, A, Checchetto, V, Moro, S, Szabo, I, Rizzuto, R (2013) The mitochondrial calcium uniporter is a multimer that can include a dominant-negative pore-forming subunit. EMBO J 32: pp. 2362-2376 CrossRef
  64. Martell, JD, Deerinck, TJ, Sancak, Y, Poulos, TL, Mootha, VK, Sosinsky, GE, Ellisman, MH, Ting, AY (2012) Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy. Nat Biotechnol 30: pp. 1143-1148 CrossRef
  65. Marchi, S, Lupini, L, Patergnani, S, Rimessi, A, Missiroli, S, Bonora, M, Bononi, A, Corra, F, Giorgi, C, Marchi, E (2013) Downregulation of the mitochondrial calcium uniporter by cancer-related miR-25. Curr Biol 23: pp. 58-63 CrossRef
  66. Kovacs-Bogdan, E, Sancak, Y, Kamer, KJ, Plovanich, M, Jambhekar, A, Huber, RJ, Myre, MA, Blower, MD, Mootha, VK (2014) Reconstitution of the mitochondrial calcium uniporter in yeast. Proc Natl Acad Sci USA 111: pp. 8985-8990 400514111" target="_blank" title="It opens in new window">CrossRef
  67. Herzig, S, Maundrell, K, Martinou, JC (2013) Life without the mitochondrial calcium uniporter. Nat Cell Biol 15: pp. 1398-1400 CrossRef
  68. Pan, X, Liu, J, Nguyen, T, Liu, C, Sun, J, Teng, Y, Fergusson, MM, Rovira, II, Allen, M, Springer, DA (2013) The physiological role of mitochondrial calcium revealed by mice lacking the mitochondrial calcium uniporter. Nat Cell Biol 15: pp. 1464-1472 CrossRef
  69. Bondarenko, AI, Jean-Quartier, C, Malli, R, Graier, WF (2013) Characterization of distinct single-channel properties of Ca(2+) inward currents in mitochondria. Pflugers Arch 465: pp. 997-1010 424-013-1224-1" target="_blank" title="It opens in new window">CrossRef
  70. Pendin, D, Greotti, E, Pozzan, T (2014) The elusive importance of being a mitochondrial Ca(2+) uniporter. Cell Calcium 55: pp. 139-145 4.02.008" target="_blank" title="It opens in new window">CrossRef
  71. Marchi, S, Pinton, P (2014) The mitochondrial calcium uniporter complex: molecular components, structure and physiopathological implications. J Physiol 592: pp. 829-839 CrossRef
  72. Mallilankaraman, K, Cardenas, C, Doonan, PJ, Chandramoorthy, HC, Irrinki, KM, Golenar, T, Csordas, G, Madireddi, P, Yang, J, Muller, M (2012) MCUR1 is an essential component of mitochondrial Ca2+ uptake that regulates cellular metabolism. Nat Cell Biol 14: pp. 1336-1343 CrossRef
  73. Hoffman, NE, Chandramoorthy, HC, Shanmughapriya, S, Zhang, XQ, Vallem, S, Doonan, PJ, Malliankaraman, K, Guo, S, Rajan, S, Elrod, JW (2014) SLC25A23 augments mitochondrial Ca(2)(+) uptake, interacts with MCU, and induces oxidative stress-mediated cell death. Mol Biol Cell 25: pp. 936-947 CrossRef
  74. Dedkova, EN, Blatter, LA (2013) Calcium signaling in cardiac mitochondria. J Mol Cell Cardiol 58: pp. 125-133 CrossRef
  75. Feng, S, Li, H, Tai, Y, Huang, J, Su, Y, Abramowitz, J, Zhu, MX, Birnbaumer, L, Wang, Y (2013) Canonical transient receptor potential 3 channels regulate mitochondrial calcium uptake. Proc Natl Acad Sci USA 110: pp. 11011-11016 CrossRef
  76. Ryu, SY, Beutner, G, Dirksen, RT, Kinnally, KW, Sheu, SS (2010) Mitochondrial ryanodine receptors and other mitochondrial Ca2+ permeable channels. FEBS Lett 584: pp. 1948-1955 CrossRef
  77. Beutner, G, Sharma, VK, Giovannucci, DR, Yule, DI, Sheu, SS (2001) Identification of a ryanodine receptor in rat heart mitochondria. J Biol Chem 276: pp. 21482-21488 4/jbc.M101486200" target="_blank" title="It opens in new window">CrossRef
  78. Jakob, R, Beutner, G, Sharma, VK, Duan, Y, Gross, RA, Hurst, S, Jhun, BS, O-Uchi, J, Sheu, SS (2014) Molecular and functional identification of a mitochondrial ryanodine receptor in neurons. Neurosci Lett 575: pp. 7-12 4.05.026" target="_blank" title="It opens in new window">CrossRef
  79. Beutner, G, Sharma, VK, Lin, L, Ryu, SY, Dirksen, RT, Sheu, SS (2005) Type 1 ryanodine receptor in cardiac mitochondria: transducer of excitation-metabolism coupling. Biochim Biophys Acta 1717: pp. 1-10 CrossRef
  80. Altschafl, BA, Beutner, G, Sharma, VK, Sheu, SS, Valdivia, HH (2007) The mitochondrial ryanodine receptor in rat heart: a pharmaco-kinetic profile. Biochim Biophys Acta 1768: pp. 1784-1795 4.011" target="_blank" title="It opens in new window">CrossRef
  81. Ryu, SY, Beutner, G, Kinnally, KW, Dirksen, RT, Sheu, SS (2011) Single channel characterization of the mitochondrial ryanodine receptor in heart mitoplasts. J Biol Chem 286: pp. 21324-21329 4/jbc.C111.245597" target="_blank" title="It opens in new window">CrossRef
  82. Stuart, JA, Cadenas, S, Jekabsons, MB, Roussel, D, Brand, MD (2001) Mitochondrial proton leak and the uncoupling protein 1 homologues. Biochim Biophys Acta 1504: pp. 144-158 43-7" target="_blank" title="It opens in new window">CrossRef
  83. Trenker, M, Malli, R, Fertschai, I, Levak-Frank, S, Graier, WF (2007) Uncoupling proteins 2 and 3 are fundamental for mitochondrial Ca2+ uniport. Nat Cell Biol 9: pp. 445-452 CrossRef
  84. Berardi, MJ, Shih, WM, Harrison, SC, Chou, JJ (2011) Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching. Nature 476: pp. 109-113 CrossRef
  85. Hashimi, H, McDonald, L, Stribrna, E, Lukes, J (2013) Trypanosome Letm1 protein is essential for mitochondrial potassium homeostasis. J Biol Chem 288: pp. 26914-26925 4/jbc.M113.495119" target="_blank" title="It opens in new window">CrossRef
  86. Nowikovsky, K, Bernardi, P (2014) LETM1 in mitochondrial cation transport. Front Physiol 5: pp. 83 4.00083" target="_blank" title="It opens in new window">CrossRef
  87. Nowikovsky, K, Froschauer, EM, Zsurka, G, Samaj, J, Reipert, S, Kolisek, M, Wiesenberger, G, Schweyen, RJ (2004) The LETM1/YOL027 gene family encodes a factor of the mitochondrial K+ homeostasis with a potential role in the Wolf鈥揌irschhorn syndrome. J Biol Chem 279: pp. 30307-30315 4/jbc.M403607200" target="_blank" title="It opens in new window">CrossRef
  88. Dimmer, KS, Navoni, F, Casarin, A, Trevisson, E, Endele, S, Winterpacht, A, Salviati, L, Scorrano, L (2008) LETM1, deleted in Wolf鈥揌irschhorn syndrome is required for normal mitochondrial morphology and cellular viability. Hum Mol Genet 17: pp. 201-214 CrossRef
  89. Jiang, D, Zhao, L, Clapham, DE (2009) Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+ antiporter. Science 326: pp. 144-147 45" target="_blank" title="It opens in new window">CrossRef
  90. Sparagna, GC, Gunter, KK, Sheu, SS, Gunter, TE (1995) Mitochondrial calcium uptake from physiological-type pulses of calcium. A description of the rapid uptake mode. J Biol Chem 270: pp. 27510-27515 4/jbc.270.46.27510" target="_blank" title="It opens in new window">CrossRef
  91. Michels, G, Khan, IF, Endres-Becker, J, Rottlaender, D, Herzig, S, Ruhparwar, A, Wahlers, T, Hoppe, UC (2009) Regulation of the human cardiac mitochondrial Ca2+ uptake by 2 different voltage-gated Ca2+ channels. Circulation 119: pp. 2435-2443 CrossRef
  92. Bogeski, I, Gulaboski, R, Kappl, R, Mirceski, V, Stefova, M, Petreska, J, Hoth, M (2011) Calcium binding and transport by coenzyme Q. J Am Chem Soc 133: pp. 9293-9303 CrossRef
  93. Beech, DJ, Bahnasi, YM, Dedman, AM, Al-Shawaf, E (2009) TRPC channel lipid specificity and mechanisms of lipid regulation. Cell Calcium 45: pp. 583-588 CrossRef
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Cell Biology
  Biomedicine
  Life Sciences
  Biochemistry
  
• 出版者：Birkh盲user Basel
• ISSN：1420-9071

文摘

Mitochondrial calcium uptake plays a critical role in various cellular functions. After half a century of extensive studies, the molecular components and important regulators of the mitochondrial calcium uptake complex have been identified. However, the mechanism by which these protein molecules interact with one another and coordinate to regulate calcium passage through mitochondrial membranes remains elusive. Here, we summarize recent progress in the structural and functional characterization of these important protein molecules, which are involved in mitochondrial calcium uptake. In particular, we focus on the current understanding of the molecular mechanism underlying calcium through two mitochondrial membranes. Additionally, we provide a new perspective for future directions in investigation and molecular intervention.