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Volumn 13, Issue 2, 2013, Pages 252-265

The role of calcium stores in apoptosis and autophagy

Author keywords

Apoptosis; Autophagy; Calcium signaling; Calcium stores; Endoplasmic reticulum; Lysosomes; Mitochondria

Indexed keywords


EID: 84874904524     PISSN: 15665240     EISSN: 18755666     Source Type: Journal    
DOI: 10.2174/1566524011313020003     Document Type: Review
Times cited : (97)

References (202)
  • 1
    • 34548188741 scopus 로고    scopus 로고
    • Self-eating and self-killing: Crosstalk between autophagy and apoptosis
    • Maiuri MC, Zalckvar E, Kimchi A, Kroemer G. Self-eating and self-killing: crosstalk between autophagy and apoptosis. Nat Rev Mol Cell Biol 2007; 8(9): 741-752.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.9 , pp. 741-752
    • Maiuri, M.C.1    Zalckvar, E.2    Kimchi, A.3    Kroemer, G.4
  • 2
    • 56749170677 scopus 로고    scopus 로고
    • Autophagic cell death: The story of a misnomer
    • Kroemer G, Levine B. Autophagic cell death: the story of a misnomer. Nat Rev Mol Cell Biol 2008; 9(12): 1004-1010.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , Issue.12 , pp. 1004-1010
    • Kroemer, G.1    Levine, B.2
  • 3
    • 0034304906 scopus 로고    scopus 로고
    • The versatility and universality of calcium signalling
    • Berridge MJ, Lipp P, Bootman MD. The versatility and universality of calcium signalling. Nat Rev Mol Cell Biol 2000; 1(1): 11-21.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , Issue.1 , pp. 11-21
    • Berridge, M.J.1    Lipp, P.2    Bootman, M.D.3
  • 4
    • 80051936634 scopus 로고    scopus 로고
    • A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
    • De Stefani D, Raffaello A, Teardo E, Szabò I, Rizzuto R. A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter. Nature 2011; 476: 336-340.
    • (2011) Nature , vol.476 , pp. 336-340
    • de Stefani, D.1    Raffaello, A.2    Teardo, E.3    Szabò, I.4    Rizzuto, R.5
  • 5
    • 80051946060 scopus 로고    scopus 로고
    • Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter
    • Baughman JM, Perocchi F, Girgis HS, et al. Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter. Nature 2011; 476: 341-345
    • (2011) Nature , vol.476 , pp. 341-345
    • Baughman, J.M.1    Perocchi, F.2    Girgis, H.S.3
  • 6
    • 0032511112 scopus 로고    scopus 로고
    • Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses
    • Rizzuto R, Pinton P, Carrington W, et al. Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses. Science 1998; 280(5370): 1763-1766.
    • (1998) Science , vol.280 , Issue.5370 , pp. 1763-1766
    • Rizzuto, R.1    Pinton, P.2    Carrington, W.3
  • 7
    • 0021213009 scopus 로고
    • Potentiation of oxidative cell injury in hepatocytes which have accumulated Ca2+
    • Thor H, Hartzell P, Orrenius S. Potentiation of oxidative cell injury in hepatocytes which have accumulated Ca2+. J Biol Chem 1984; 259(10): 6612-6615.
    • (1984) J Biol Chem , vol.259 , Issue.10 , pp. 6612-6615
    • Thor, H.1    Hartzell, P.2    Orrenius, S.3
  • 8
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok Y, Krapivinsky G, Clapham DE. The mitochondrial calcium uniporter is a highly selective ion channel. Nature 2004; 427(6972): 360-364.
    • (2004) Nature , vol.427 , Issue.6972 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 10
    • 0029143569 scopus 로고
    • Decoding of cytosolic calcium oscillations in the mitochondria
    • Hajnóczky G, Robb-Gaspers LD, Seitz MB, Thomas AP. Decoding of cytosolic calcium oscillations in the mitochondria. Cell 1995; 82(3): 415-424.
    • (1995) Cell , vol.82 , Issue.3 , pp. 415-424
    • Hajnóczky, G.1    Robb-Gaspers, L.D.2    Seitz, M.B.3    Thomas, A.P.4
  • 11
    • 0033118649 scopus 로고    scopus 로고
    • Contributions of mitochondria to animal physiology: From homeostatic sensor to calcium signalling and cell death
    • Duchen MR. Contributions of mitochondria to animal physiology: from homeostatic sensor to calcium signalling and cell death. J Physiol 1999; 516 (Pt 1): 1-17.
    • (1999) J Physiol , vol.516 , Issue.Pt 1 , pp. 1-17
    • Duchen, M.R.1
  • 12
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: Channels, exchangers, and permeability transition
    • Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol Rev 1999; 79(4): 1127-1155.
    • (1999) Physiol Rev , vol.79 , Issue.4 , pp. 1127-1155
    • Bernardi, P.1
  • 13
    • 0031587822 scopus 로고    scopus 로고
    • Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals
    • Ichas F, Jouaville LS, Mazat JP. Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals. Cell 1997; 89(7): 1145-1153.
    • (1997) Cell , vol.89 , Issue.7 , pp. 1145-1153
    • Ichas, F.1    Jouaville, L.S.2    Mazat, J.P.3
  • 14
    • 0032701640 scopus 로고    scopus 로고
    • Permeability transition pore regulates both mitochondrial membrane potential and agonist-evoked Ca2+ signals in oligodendrocyte progenitors
    • Smaili SS, Russell JT. Permeability transition pore regulates both mitochondrial membrane potential and agonist-evoked Ca2+ signals in oligodendrocyte progenitors. Cell Calcium 1999; 26(3-4): 121-130.
    • (1999) Cell Calcium , vol.26 , Issue.3-4 , pp. 121-130
    • Smaili, S.S.1    Russell, J.T.2
  • 15
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G, Galluzzi L, Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 2007; 87(1): 99-163.
    • (2007) Physiol Rev , vol.87 , Issue.1 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 17
    • 33751513394 scopus 로고    scopus 로고
    • Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies
    • Kim H, Rafiuddin-Shah M, Tu HC, et al. Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies. Nat Cell Biol 2006; 8(12): 1348-1358.
    • (2006) Nat Cell Biol , vol.8 , Issue.12 , pp. 1348-1358
    • Kim, H.1    Rafiuddin-Shah, M.2    Tu, H.C.3
  • 18
    • 77956220629 scopus 로고    scopus 로고
    • Neuronal calcium signaling, mitochondrial dysfunction, and Alzheimer's disease
    • Supnet C, Bezprozvanny I. Neuronal calcium signaling, mitochondrial dysfunction, and Alzheimer's disease. J Alzheimers Dis 2010; 20 (Suppl 2): S487-S498.
    • (2010) J Alzheimers Dis , vol.20 , Issue.SUPPL. 2
    • Supnet, C.1    Bezprozvanny, I.2
  • 19
    • 0036272650 scopus 로고    scopus 로고
    • Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • Casley CS, Canevari L, Land JM, Clark JB, Sharpe MA. Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J Neurochem 2002; 80(1): 91-100.
    • (2002) J Neurochem , vol.80 , Issue.1 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 20
    • 39149122810 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer's disease
    • Reddy PH, Beal MF. Amyloid beta, mitochondrial dysfunction and synaptic damage: implications for cognitive decline in aging and Alzheimer's disease. Trends Mol Med 2008; 14(2): 45-53.
    • (2008) Trends Mol Med , vol.14 , Issue.2 , pp. 45-53
    • Reddy, P.H.1    Beal, M.F.2
  • 21
    • 79959236620 scopus 로고    scopus 로고
    • Modulation of mitochondrial calcium as a pharmacological target for Alzheimer's disease
    • Hung CH, Ho YS, Chang RC. Modulation of mitochondrial calcium as a pharmacological target for Alzheimer's disease. Ageing Res Rev 2010; 9(4): 447-456.
    • (2010) Ageing Res Rev , vol.9 , Issue.4 , pp. 447-456
    • Hung, C.H.1    Ho, Y.S.2    Chang, R.C.3
  • 22
    • 33745246534 scopus 로고    scopus 로고
    • Intracellular nucleotides act as critical prosurvival factors by binding to cytochrome C and inhibiting apoptosome
    • Chandra D, Bratton SB, Person MD, et al. Intracellular nucleotides act as critical prosurvival factors by binding to cytochrome C and inhibiting apoptosome. Cell 2006; 125(7): 1333-1346.
    • (2006) Cell , vol.125 , Issue.7 , pp. 1333-1346
    • Chandra, D.1    Bratton, S.B.2    Person, M.D.3
  • 24
    • 0032504574 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: The role of cytochrome c
    • Cai J, Yang J, Jones DP. Mitochondrial control of apoptosis: the role of cytochrome c. Biochim Biophys Acta 1998; 1366(1-2): 139-149.
    • (1998) Biochim Biophys Acta , vol.1366 , Issue.1-2 , pp. 139-149
    • Cai, J.1    Yang, J.2    Jones, D.P.3
  • 25
    • 0035967169 scopus 로고    scopus 로고
    • Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death
    • Joza N, Susin SA, Daugas E, et al. Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death. Nature 2001; 410(6828): 549-554.
    • (2001) Nature , vol.410 , Issue.6828 , pp. 549-554
    • Joza, N.1    Susin, S.A.2    Daugas, E.3
  • 26
    • 2942532135 scopus 로고    scopus 로고
    • Analysis of the composition, assembly kinetics and activity of native Apaf-1 apoptosomes
    • Hill MM, Adrain C, Duriez PJ, Creagh EM, Martin SJ. Analysis of the composition, assembly kinetics and activity of native Apaf-1 apoptosomes. EMBO J 2004; 23(10): 2134-2145.
    • (2004) EMBO J , vol.23 , Issue.10 , pp. 2134-2145
    • Hill, M.M.1    Adrain, C.2    Duriez, P.J.3    Creagh, E.M.4    Martin, S.J.5
  • 27
  • 28
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A, Nagata S. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 1998; 391(6662): 43-50.
    • (1998) Nature , vol.391 , Issue.6662 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 29
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li LY, Luo X, Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 2001; 412(6842): 95-9.
    • (2001) Nature , vol.412 , Issue.6842 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 30
    • 39049149816 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Jeong SY, Seol DW. The role of mitochondria in apoptosis. BMB Rep 2008; 41(1): 11-22.
    • (2008) BMB Rep , vol.41 , Issue.1 , pp. 11-22
    • Jeong, S.Y.1    Seol, D.W.2
  • 32
    • 77958130220 scopus 로고    scopus 로고
    • The interplay between BCL-2 family proteins and mitochondrial morphology in the regulation of apoptosis
    • Soriano DE, Scorrano L. The interplay between BCL-2 family proteins and mitochondrial morphology in the regulation of apoptosis. Adv Exp Med Biol 2010; 687: 97-114.
    • (2010) Adv Exp Med Biol , vol.687 , pp. 97-114
    • Soriano, D.E.1    Scorrano, L.2
  • 33
    • 0037044737 scopus 로고    scopus 로고
    • Effect of Bcl-2 overexpression on mitochondrial structure and function
    • Kowaltowski AJ, Cosso RG, Campos CB, Fiskum G. Effect of Bcl-2 overexpression on mitochondrial structure and function. J Biol Chem 2002; 277(45): 42802-7.
    • (2002) J Biol Chem , vol.277 , Issue.45 , pp. 42802-42807
    • Kowaltowski, A.J.1    Cosso, R.G.2    Campos, C.B.3    Fiskum, G.4
  • 34
    • 0037035807 scopus 로고    scopus 로고
    • Bax-mediated Ca2+ mobilization promotes cytochrome c release during apoptosis
    • Nutt LK, Chandra J, Pataer A, et al. Bax-mediated Ca2+ mobilization promotes cytochrome c release during apoptosis. J Biol Chem 2002; 277(23): 20301-8.
    • (2002) J Biol Chem , vol.277 , Issue.23 , pp. 20301-20308
    • Nutt, L.K.1    Chandra, J.2    Pataer, A.3
  • 36
    • 0037175393 scopus 로고    scopus 로고
    • Recombinant expression of the voltage-dependent anion channel enhances the transfer of Ca2+ microdomains to mitochondria
    • Rapizzi E, Pinton P, Szabadkai G, et al. Recombinant expression of the voltage-dependent anion channel enhances the transfer of Ca2+ microdomains to mitochondria. J Cell Biol 2002; 159(4): 613-24.
    • (2002) J Cell Biol , vol.159 , Issue.4 , pp. 613-624
    • Rapizzi, E.1    Pinton, P.2    Szabadkai, G.3
  • 37
    • 64849113485 scopus 로고    scopus 로고
    • Control of mitochondrial apoptosis by the Bcl-2 family
    • Brunelle JK, Letai A. Control of mitochondrial apoptosis by the Bcl-2 family. J Cell Sci 2009; 122(Pt 4): 437-41.
    • (2009) J Cell Sci , vol.122 , Issue.Pt 4 , pp. 437-441
    • Brunelle, J.K.1    Letai, A.2
  • 38
    • 0036791637 scopus 로고    scopus 로고
    • The roles of Bid
    • Esposti MD. The roles of Bid. Apoptosis 2002; 7(5): 433-40.
    • (2002) Apoptosis , vol.7 , Issue.5 , pp. 433-440
    • Esposti, M.D.1
  • 39
    • 0035842896 scopus 로고    scopus 로고
    • VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release
    • Madesh M, Hajnóczky G. VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release. J Cell Biol 2001; 155(6): 1003-15.
    • (2001) J Cell Biol , vol.155 , Issue.6 , pp. 1003-1015
    • Madesh, M.1    Hajnóczky, G.2
  • 40
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher S, Osen-Sand A, Nichols A, et al. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol 1999; 144(5): 891-901.
    • (1999) J Cell Biol , vol.144 , Issue.5 , pp. 891-901
    • Desagher, S.1    Osen-Sand, A.2    Nichols, A.3
  • 41
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R, Desagher S, Antonsson B, Martinou JC. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol 2000; 20(3): 929-35.
    • (2000) Mol Cell Biol , vol.20 , Issue.3 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 42
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei MC, Zong WX, Cheng EH, et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 2001; 292(5517): 727-30.
    • (2001) Science , vol.292 , Issue.5517 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3
  • 44
    • 34250864795 scopus 로고    scopus 로고
    • Protein turnover via autophagy: Implications for metabolism
    • Mizushima N, Klionsky DJ. Protein turnover via autophagy: implications for metabolism. Annu Rev Nutr 2007; 27: 19-40.
    • (2007) Annu Rev Nutr , vol.27 , pp. 19-40
    • Mizushima, N.1    Klionsky, D.J.2
  • 46
    • 25144506835 scopus 로고    scopus 로고
    • Autophagy in cell death: An innocent convict?
    • Levine B, Yuan J. Autophagy in cell death: an innocent convict? J Clin Invest 2005; 115(10): 2679-88.
    • (2005) J Clin Invest , vol.115 , Issue.10 , pp. 2679-2688
    • Levine, B.1    Yuan, J.2
  • 48
    • 53549132786 scopus 로고    scopus 로고
    • Beclin 1 bridges autophagy, apoptosis and differentiation
    • Wang J. Beclin 1 bridges autophagy, apoptosis and differentiation. Autophagy 2008; 4(7): 947-8.
    • (2008) Autophagy , vol.4 , Issue.7 , pp. 947-948
    • Wang, J.1
  • 49
    • 0017816161 scopus 로고
    • Inhibition by insulin of the formation of autophagic vacuoles in rat liver. A morphometric approach to the kinetics of intracellular degradation by autophagy
    • Pfeifer U. Inhibition by insulin of the formation of autophagic vacuoles in rat liver. A morphometric approach to the kinetics of intracellular degradation by autophagy. J Cell Biol 1978; 78(1): 152-67.
    • (1978) J Cell Biol , vol.78 , Issue.1 , pp. 152-167
    • Pfeifer, U.1
  • 50
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondriaanchored receptor Atg32 mediates degradation of mitochondria via selective autophagy
    • Okamoto K, Kondo-Okamoto N, Ohsumi Y. Mitochondriaanchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. Dev Cell 2009; 17(1): 87-97.
    • (2009) Dev Cell , vol.17 , Issue.1 , pp. 87-97
    • Okamoto, K.1    Kondo-Okamoto, N.2    Ohsumi, Y.3
  • 51
    • 79955623510 scopus 로고    scopus 로고
    • During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
    • Gomes LC, Di Benedetto G, Scorrano L. During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat Cell Biol 2011; 13(5): 589-98.
    • (2011) Nat Cell Biol , vol.13 , Issue.5 , pp. 589-598
    • Gomes, L.C.1    Di Benedetto, G.2    Scorrano, L.3
  • 52
    • 77649282583 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and mitophagy activation in blood mononuclear cells of fibromyalgia patients: Implications in the pathogenesis of the disease
    • Cordero MD, De Miguel M, Moreno Fernández AM, et al. Mitochondrial dysfunction and mitophagy activation in blood mononuclear cells of fibromyalgia patients: implications in the pathogenesis of the disease. Arthritis Res Ther 2010; 12(1): R17.
    • (2010) Arthritis Res Ther , vol.12 , Issue.1
    • Cordero, M.D.1    de Miguel, M.2    Moreno Fernández, A.M.3
  • 53
    • 4644273585 scopus 로고    scopus 로고
    • Uth1p is involved in the autophagic degradation of mitochondria
    • Kissová I, Deffieu M, Manon S, Camougrand N. Uth1p is involved in the autophagic degradation of mitochondria. J Biol Chem 2004; 279(37): 39068-74.
    • (2004) J Biol Chem , vol.279 , Issue.37 , pp. 39068-39074
    • Kissová, I.1    Deffieu, M.2    Manon, S.3    Camougrand, N.4
  • 54
    • 78349275317 scopus 로고    scopus 로고
    • Mitophagy in yeast: Actors and physiological roles
    • Bhatia-Kissová I, Camougrand N. Mitophagy in yeast: actors and physiological roles. FEMS Yeast Res 2010; 10(8): 1023-34.
    • (2010) FEMS Yeast Res , vol.10 , Issue.8 , pp. 1023-1034
    • Bhatia-Kissová, I.1    Camougrand, N.2
  • 55
  • 56
    • 5444236546 scopus 로고    scopus 로고
    • Uth1p: A yeast mitochondrial protein at the crossroads of stress, degradation and cell death
    • Camougrand N, Kissová I, Velours G, Manon S. Uth1p: a yeast mitochondrial protein at the crossroads of stress, degradation and cell death. FEMS Yeast Res 2004; 5(2): 133-40.
    • (2004) FEMS Yeast Res , vol.5 , Issue.2 , pp. 133-140
    • Camougrand, N.1    Kissová, I.2    Velours, G.3    Manon, S.4
  • 57
    • 34250796793 scopus 로고    scopus 로고
    • Selective and non-selective autophagic degradation of mitochondria in yeast
    • Kissová I, Salin B, Schaeffer J, Bhatia S, Manon S, Camougrand N. Selective and non-selective autophagic degradation of mitochondria in yeast. Autophagy 2007; 3(4): 329-36.
    • (2007) Autophagy , vol.3 , Issue.4 , pp. 329-336
    • Kissová, I.1    Salin, B.2    Schaeffer, J.3    Bhatia, S.4    Manon, S.5    Camougrand, N.6
  • 59
    • 16844366524 scopus 로고    scopus 로고
    • Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging
    • Lemasters JJ. Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging. Rejuvenation Res 2005; 8(1): 3-5.
    • (2005) Rejuvenation Res , vol.8 , Issue.1 , pp. 3-5
    • Lemasters, J.J.1
  • 60
    • 0037238512 scopus 로고    scopus 로고
    • The product of the UTH1 gene, required for Bax-induced cell death in yeast, is involved in the response to rapamycin
    • Camougrand N, Grelaud-Coq A, Marza E, Priault M, Bessoule JJ, Manon S. The product of the UTH1 gene, required for Bax-induced cell death in yeast, is involved in the response to rapamycin. Mol Microbiol 2003; 47(2): 495-506.
    • (2003) Mol Microbiol , vol.47 , Issue.2 , pp. 495-506
    • Camougrand, N.1    Grelaud-Coq, A.2    Marza, E.3    Priault, M.4    Bessoule, J.J.5    Manon, S.6
  • 61
    • 57049186623 scopus 로고    scopus 로고
    • How to live long and prosper: Autophagy, mitochondria, and aging
    • Yen WL, Klionsky DJ. How to live long and prosper: autophagy, mitochondria, and aging. Physiology (Bethesda) 2008; 23: 248-62.
    • (2008) Physiology (Bethesda) , vol.23 , pp. 248-262
    • Yen, W.L.1    Klionsky, D.J.2
  • 62
    • 0042707790 scopus 로고    scopus 로고
    • Mitochondrial recycling and aging of cardiac myocytes: The role of autophagocytosis
    • Terman A, Dalen H, Eaton JW, Neuzil J, Brunk UT. Mitochondrial recycling and aging of cardiac myocytes: the role of autophagocytosis. Exp Gerontol 2003; 38(8): 863-76.
    • (2003) Exp Gerontol , vol.38 , Issue.8 , pp. 863-876
    • Terman, A.1    Dalen, H.2    Eaton, J.W.3    Neuzil, J.4    Brunk, U.T.5
  • 63
    • 73449095225 scopus 로고    scopus 로고
    • Atg32 is a tag for mitochondria degradation in yeast
    • Kanki T, Klionsky DJ. Atg32 is a tag for mitochondria degradation in yeast. Autophagy 2009; 5(8): 1201-2.
    • (2009) Autophagy , vol.5 , Issue.8 , pp. 1201-1202
    • Kanki, T.1    Klionsky, D.J.2
  • 64
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T, Asakawa S, Hattori N, et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 1998; 392(6676): 605-8.
    • (1998) Nature , vol.392 , Issue.6676 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3
  • 65
    • 58149339635 scopus 로고    scopus 로고
    • Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity
    • Hung LW, Ciccotosto GD, Giannakis E, et al. Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity. J Neurosci 2008; 28(46): 11950-8.
    • (2008) J Neurosci , vol.28 , Issue.46 , pp. 11950-11958
    • Hung, L.W.1    Ciccotosto, G.D.2    Giannakis, E.3
  • 66
    • 68149103297 scopus 로고    scopus 로고
    • Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion
    • Song Z, Ghochani M, McCaffery JM, Frey TG, Chan DC. Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion. Mol Biol Cell 2009; 20(15): 3525-32.
    • (2009) Mol Biol Cell , vol.20 , Issue.15 , pp. 3525-3532
    • Song, Z.1    Ghochani, M.2    McCaffery, J.M.3    Frey, T.G.4    Chan, D.C.5
  • 67
    • 78650017514 scopus 로고    scopus 로고
    • Mitochondrial dynamics, cell death and the pathogenesis of Parkinson's disease
    • Büeler H. Mitochondrial dynamics, cell death and the pathogenesis of Parkinson's disease. Apoptosis 2010; 15(11): 1336-53.
    • (2010) Apoptosis , vol.15 , Issue.11 , pp. 1336-1353
    • Büeler, H.1
  • 68
    • 75949104449 scopus 로고    scopus 로고
    • Mitochondria get a Parkin' ticket
    • Wild P, Dikic I. Mitochondria get a Parkin' ticket. Nat Cell Biol 2010; 12(2): 104-6.
    • (2010) Nat Cell Biol , vol.12 , Issue.2 , pp. 104-106
    • Wild, P.1    Dikic, I.2
  • 69
    • 78049368074 scopus 로고    scopus 로고
    • Parkinsonrelated parkin reduces α-Synuclein phosphorylation in a gene transfer model
    • Khandelwal PJ, Dumanis SB, Feng LR, et al. Parkinsonrelated parkin reduces α-Synuclein phosphorylation in a gene transfer model. Mol Neurodegener 2010; 5: 47.
    • (2010) Ol Neurodegener , vol.5 , pp. 47
    • Khandelwal, P.J.1    Dumanis, S.B.2    Feng, L.R.3
  • 71
    • 33751159209 scopus 로고    scopus 로고
    • Intracellular signaling by the unfolded protein response
    • Bernales S, Papa FR, Walter P. Intracellular signaling by the unfolded protein response. Annu Rev Cell Dev Biol 2006; 22: 487-508.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 487-508
    • Bernales, S.1    Papa, F.R.2    Walter, P.3
  • 72
    • 33646267694 scopus 로고    scopus 로고
    • Conformational diseases and ER stress-mediated cell death: Apoptotic cell death and autophagic cell death
    • Momoi T. Conformational diseases and ER stress-mediated cell death: apoptotic cell death and autophagic cell death. Curr Mol Med 2006; 6(1): 111-8.
    • (2006) Curr Mol Med , vol.6 , Issue.1 , pp. 111-118
    • Momoi, T.1
  • 73
    • 0037418861 scopus 로고    scopus 로고
    • Cell biology. Apoptosis--the calcium connection
    • Demaurex N, Distelhorst C. Cell biology. Apoptosis--the calcium connection. Science 2003; 300(5616): 65-7.
    • (2003) Science , vol.300 , Issue.5616 , pp. 65-67
    • Demaurex, N.1    Distelhorst, C.2
  • 74
    • 33644847375 scopus 로고    scopus 로고
    • Microdomains of intracellular Ca2+: Molecular determinants and functional consequences
    • Rizzuto R, Pozzan T. Microdomains of intracellular Ca2+: molecular determinants and functional consequences. Physiol Rev 2006; 86(1): 369-408.
    • (2006) Physiol Rev , vol.86 , Issue.1 , pp. 369-408
    • Rizzuto, R.1    Pozzan, T.2
  • 75
    • 0031594742 scopus 로고    scopus 로고
    • The endoplasmic reticulum Ca2+ store: A view from the lumen
    • Meldolesi J, Pozzan T. The endoplasmic reticulum Ca2+ store: a view from the lumen. Trends Biochem Sci 1998; 23(1): 10-4.
    • (1998) Trends Biochem Sci , vol.23 , Issue.1 , pp. 10-14
    • Meldolesi, J.1    Pozzan, T.2
  • 76
    • 7444240833 scopus 로고    scopus 로고
    • The ER function BiP is a master regulator of ER function
    • Hendershot LM. The ER function BiP is a master regulator of ER function. Mt Sinai J Med 2004; 71(5): 289-97.
    • (2004) Mt Sinai J Med , vol.71 , Issue.5 , pp. 289-297
    • Hendershot, L.M.1
  • 77
    • 33645156429 scopus 로고    scopus 로고
    • From acute ER stress to physiological roles of the Unfolded Protein Response
    • Wu J, Kaufman RJ. From acute ER stress to physiological roles of the Unfolded Protein Response. Cell Death Differ 2006; 13(3): 374-84.
    • (2006) Cell Death Differ , vol.13 , Issue.3 , pp. 374-384
    • Wu, J.1    Kaufman, R.J.2
  • 78
    • 70349479191 scopus 로고    scopus 로고
    • Calcium and cell death signaling in neurodegeneration and aging
    • Smaili S, Hirata H, Ureshino R, et al. Calcium and cell death signaling in neurodegeneration and aging. An Acad Bras Cienc 2009; 81(3): 467-75.
    • (2009) An Acad Bras Cienc , vol.81 , Issue.3 , pp. 467-475
    • Smaili, S.1    Hirata, H.2    Ureshino, R.3
  • 79
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, Walter P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 2000; 101(3): 249-58.
    • (2000) Cell , vol.101 , Issue.3 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 80
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: The unfolded protein response in yeast and mammals
    • Patil C, Walter P. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol 2001; 13(3): 349-55.
    • (2001) Curr Opin Cell Biol , vol.13 , Issue.3 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 81
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schröder M, Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem 2005; 74: 739-89.
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schröder, M.1    Kaufman, R.J.2
  • 82
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi E, Logue SE, Gorman AM, Samali A. Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep 2006; 7(9): 880-5.
    • (2006) EMBO Rep , vol.7 , Issue.9 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 83
    • 0034013539 scopus 로고    scopus 로고
    • Stress protein GRP78 prevents apoptosis induced by calcium ionophore, ionomycin, but not by glycosylation inhibitor, tunicamycin, in human prostate cancer cells
    • Miyake H, Hara I, Arakawa S, Kamidono S. Stress protein GRP78 prevents apoptosis induced by calcium ionophore, ionomycin, but not by glycosylation inhibitor, tunicamycin, in human prostate cancer cells. J Cell Biochem 2000; 77(3): 396-408.
    • (2000) J Cell Biochem , vol.77 , Issue.3 , pp. 396-408
    • Miyake, H.1    Hara, I.2    Arakawa, S.3    Kamidono, S.4
  • 84
    • 0035279679 scopus 로고    scopus 로고
    • The ins and outs of calreticulin: From the ER lumen to the extracellular space
    • Johnson S, Michalak M, Opas M, Eggleton P. The ins and outs of calreticulin: from the ER lumen to the extracellular space. Trends Cell Biol 2001; 11(3): 122-9.
    • (2001) Trends Cell Biol , vol.11 , Issue.3 , pp. 122-129
    • Johnson, S.1    Michalak, M.2    Opas, M.3    Eggleton, P.4
  • 85
    • 0031977191 scopus 로고    scopus 로고
    • The role of calcium in apoptosis
    • Nicotera P, Orrenius S. The role of calcium in apoptosis. Cell Calcium 1998; 23(2-3): 173-80.
    • (1998) Cell Calcium , vol.23 , Issue.2-3 , pp. 173-180
    • Nicotera, P.1    Orrenius, S.2
  • 87
    • 29244476522 scopus 로고    scopus 로고
    • Apoptotic effect of ethanol is potentiated by caffeine-induced calcium release in rat astrocytes
    • Hirata H, Machado LS, Okuno CS, Brasolin A, Lopes GS, Smaili SS. Apoptotic effect of ethanol is potentiated by caffeine-induced calcium release in rat astrocytes. Neurosci Lett 2006; 393(2-3): 136-40.
    • (2006) Neurosci Lett , vol.393 , Issue.2-3 , pp. 136-140
    • Hirata, H.1    Machado, L.S.2    Okuno, C.S.3    Brasolin, A.4    Lopes, G.S.5    Smaili, S.S.6
  • 88
    • 79954430607 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium release engages Bax translocation in cortical astrocytes
    • Morales AP, Carvalho AC, Monteforte PT, et al. Endoplasmic reticulum calcium release engages Bax translocation in cortical astrocytes. Neurochem Res 2011; 36(5): 829-38.
    • (2011) Neurochem Res , vol.36 , Issue.5 , pp. 829-838
    • Morales, A.P.1    Carvalho, A.C.2    Monteforte, P.T.3
  • 89
    • 0037418843 scopus 로고    scopus 로고
    • BAX and BAK regulation of endoplasmic reticulum Ca2+: A control point for apoptosis
    • Scorrano L, Oakes SA, Opferman JT, et al. BAX and BAK regulation of endoplasmic reticulum Ca2+: a control point for apoptosis. Science 2003; 300(5616): 135-9.
    • (2003) Science , vol.300 , Issue.5616 , pp. 135-139
    • Scorrano, L.1    Oakes, S.A.2    Opferman, J.T.3
  • 90
    • 47349089719 scopus 로고    scopus 로고
    • Targeting Bcl-2-IP3 receptor interaction to reverse Bcl-2's inhibition of apoptotic calcium signals
    • Rong YP, Aromolaran AS, Bultynck G, et al. Targeting Bcl-2-IP3 receptor interaction to reverse Bcl-2's inhibition of apoptotic calcium signals. Mol Cell 2008; 31(2): 255-65.
    • (2008) Mol Cell , vol.31 , Issue.2 , pp. 255-265
    • Rong, Y.P.1    Aromolaran, A.S.2    Bultynck, G.3
  • 91
    • 0034698838 scopus 로고    scopus 로고
    • Changes in endoplasmic reticulum luminal environment affect cell sensitivity to apoptosis
    • Nakamura K, Bossy-Wetzel E, Burns K, et al. Changes in endoplasmic reticulum luminal environment affect cell sensitivity to apoptosis. J Cell Biol 2000; 150(4): 731-40.
    • (2000) J Cell Biol , vol.150 , Issue.4 , pp. 731-740
    • Nakamura, K.1    Bossy-Wetzel, E.2    Burns, K.3
  • 92
    • 0035355341 scopus 로고    scopus 로고
    • The Ca2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: Significance for the molecular mechanism of Bcl-2 action
    • Pinton P, Ferrari D, Rapizzi E, Di Virgilio F, Pozzan T, Rizzuto R. 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 2001; 20(11): 2690-701.
    • (2001) EMBO J , vol.20 , Issue.11 , pp. 2690-2701
    • Pinton, P.1    Ferrari, D.2    Rapizzi, E.3    Di Virgilio, F.4    Pozzan, T.5    Rizzuto, R.6
  • 93
    • 2942530420 scopus 로고    scopus 로고
    • Arachidonic acid released by phospholipase A(2) activation triggers Ca(2+)-dependent apoptosis through the mitochondrial pathway
    • Penzo D, Petronilli V, Angelin A, et al. Arachidonic acid released by phospholipase A(2) activation triggers Ca(2+)-dependent apoptosis through the mitochondrial pathway. J Biol Chem 2004; 279(24): 25219-25.
    • (2004) J Biol Chem , vol.279 , Issue.24 , pp. 25219-25225
    • Penzo, D.1    Petronilli, V.2    Angelin, A.3
  • 94
    • 0035853767 scopus 로고    scopus 로고
    • Arachidonic acid causes cell death through the mitochondrial permeability transition. Implications for tumor necrosis factoralpha aopototic signaling
    • Scorrano L, Penzo D, Petronilli V, Pagano F, Bernardi P. Arachidonic acid causes cell death through the mitochondrial permeability transition. Implications for tumor necrosis factoralpha aopototic signaling. J Biol Chem 2001; 276(15): 12035-40.
    • (2001) J Biol Chem , vol.276 , Issue.15 , pp. 12035-12040
    • Scorrano, L.1    Penzo, D.2    Petronilli, V.3    Pagano, F.4    Bernardi, P.5
  • 95
    • 0027173162 scopus 로고
    • Effect of glucocorticosteroid treatment on intracellular calcium homeostasis in mouse lymphoma cells
    • Lam M, Dubyak G, Distelhorst CW. Effect of glucocorticosteroid treatment on intracellular calcium homeostasis in mouse lymphoma cells. Mol Endocrinol 1993; 7(5): 686-93.
    • (1993) Mol Endocrinol , vol.7 , Issue.5 , pp. 686-693
    • Lam, M.1    Dubyak, G.2    Distelhorst, C.W.3
  • 96
    • 1342305497 scopus 로고    scopus 로고
    • Caspase-12 and ERstress-mediated apoptosis: The story so far
    • Szegezdi E, Fitzgerald U, Samali A. Caspase-12 and ERstress-mediated apoptosis: the story so far. Ann N Y Acad Sci 2003; 1010: 186-94.
    • (2003) Ann N Y Acad Sci , vol.1010 , pp. 186-194
    • Szegezdi, E.1    Fitzgerald, U.2    Samali, A.3
  • 97
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda T, Imaizumi K, Oono K, et al. Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem 2001; 276(17): 13935-40.
    • (2001) J Biol Chem , vol.276 , Issue.17 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3
  • 98
    • 80052621140 scopus 로고    scopus 로고
    • Calcium and cell death mechanisms: A perspective from the cell death community
    • Zhivotovsky B, Orrenius S. Calcium and cell death mechanisms: A perspective from the cell death community. Cell Calcium 2011; 50(3): 211-21.
    • (2011) Cell Calcium , vol.50 , Issue.3 , pp. 211-221
    • Zhivotovsky, B.1    Orrenius, S.2
  • 99
    • 79952196841 scopus 로고    scopus 로고
    • Apoptosis and autophagy: Decoding calcium signals that mediate life or death
    • Harr MW, Distelhorst CW. Apoptosis and autophagy: decoding calcium signals that mediate life or death. Cold Spring Harb Perspect Biol 2010; 2(10): a005579.
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , Issue.10
    • Harr, M.W.1    Distelhorst, C.W.2
  • 100
    • 0036086064 scopus 로고    scopus 로고
    • The unfolded protein response in nutrient sensing and differentiation
    • Kaufman RJ, Scheuner D, Schröder M, et al. The unfolded protein response in nutrient sensing and differentiation. Nat Rev Mol Cell Biol 2002; 3(6): 411-21.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , Issue.6 , pp. 411-421
    • Kaufman, R.J.1    Scheuner, D.2    Schröder, M.3
  • 101
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: Disease relevance and therapeutic opportunities
    • Kim I, Xu W, Reed JC. Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities. Nat Rev Drug Discov 2008; 7(12): 1013-30.
    • (2008) Nat Rev Drug Discov , vol.7 , Issue.12 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 102
    • 0029886877 scopus 로고    scopus 로고
    • Bcl-2 acts subsequent to and independent of Ca2+ fluxes to inhibit apoptosis in thapsigargin-and glucocorticoid-treated mouse lymphoma cells
    • Distelhorst CW, McCormick TS. Bcl-2 acts subsequent to and independent of Ca2+ fluxes to inhibit apoptosis in thapsigargin-and glucocorticoid-treated mouse lymphoma cells. Cell Calcium 1996; 19(6): 473-83.
    • (1996) Cell Calcium , vol.19 , Issue.6 , pp. 473-483
    • Distelhorst, C.W.1    McCormick, T.S.2
  • 103
    • 0034705141 scopus 로고    scopus 로고
    • Bcl-2 decreases the free Ca2+ concentration within the endoplasmic reticulum
    • Foyouzi-Youssefi R, Arnaudeau S, Borner C, et al. Bcl-2 decreases the free Ca2+ concentration within the endoplasmic reticulum. Proc Natl Acad Sci USA 2000; 97(11): 5723-8.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.11 , pp. 5723-5728
    • Foyouzi-Youssefi, R.1    Arnaudeau, S.2    Borner, C.3
  • 104
    • 34548030192 scopus 로고    scopus 로고
    • The proapoptotic factors Bax and Bak regulate T Cell proliferation through control of endoplasmic reticulum Ca(2+) homeostasis
    • Jones RG, Bui T, White C, et al. The proapoptotic factors Bax and Bak regulate T Cell proliferation through control of endoplasmic reticulum Ca(2+) homeostasis. Immunity 2007; 27(2): 268-80.
    • (2007) Immunity , vol.27 , Issue.2 , pp. 268-280
    • Jones, R.G.1    Bui, T.2    White, C.3
  • 105
    • 11844284861 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum
    • Oakes SA, Scorrano L, Opferman JT, et al. Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum. Proc Natl Acad Sci USA 2005; 102(1): 105-10.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.1 , pp. 105-110
    • Oakes, S.A.1    Scorrano, L.2    Opferman, J.T.3
  • 106
    • 41449101555 scopus 로고    scopus 로고
    • A specific pathway inducing autophagic cell death is marked by an IP3R mutation
    • Lam D, Golstein P. A specific pathway inducing autophagic cell death is marked by an IP3R mutation. Autophagy 2008; 4(3): 349-50.
    • (2008) Autophagy , vol.4 , Issue.3 , pp. 349-350
    • Lam, D.1    Golstein, P.2
  • 107
    • 3342984659 scopus 로고    scopus 로고
    • Bcl-2 functionally interacts with inositol 1,4,5-trisphosphate receptors to regulate calcium release from the ER in response to inositol 1,4,5-trisphosphate
    • Chen R, Valencia I, Zhong F, et al. Bcl-2 functionally interacts with inositol 1,4,5-trisphosphate receptors to regulate calcium release from the ER in response to inositol 1,4,5-trisphosphate. J Cell Biol 2004; 166(2): 193-203.
    • (2004) J Cell Biol , vol.166 , Issue.2 , pp. 193-203
    • Chen, R.1    Valencia, I.2    Zhong, F.3
  • 108
    • 70149105706 scopus 로고    scopus 로고
    • The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor
    • Rong YP, Bultynck G, Aromolaran AS, et al. The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor. Proc Natl Acad Sci USA 2009; 106(34): 14397-402.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.34 , pp. 14397-14402
    • Rong, Y.P.1    Bultynck, G.2    Aromolaran, A.S.3
  • 109
    • 0037131261 scopus 로고    scopus 로고
    • Protein kinase A and two phosphatases are components of the inositol 1,4,5-trisphosphate receptor macromolecular signaling complex
    • DeSouza N, Reiken S, Ondrias K, Yang YM, Matkovich S, Marks AR. Protein kinase A and two phosphatases are components of the inositol 1,4,5-trisphosphate receptor macromolecular signaling complex. J Biol Chem 2002; 277(42): 39397-400.
    • (2002) J Biol Chem , vol.277 , Issue.42 , pp. 39397-39400
    • Desouza, N.1    Reiken, S.2    Ondrias, K.3    Yang, Y.M.4    Matkovich, S.5    Marks, A.R.6
  • 110
    • 47349099011 scopus 로고    scopus 로고
    • Bcl-2 suppresses Ca2+ release through inositol 1,4,5-trisphosphate receptors and inhibits Ca2+ uptake by mitochondria without affecting ER calcium store content
    • Hanson CJ, Bootman MD, Distelhorst CW, Wojcikiewicz RJ, Roderick HL. Bcl-2 suppresses Ca2+ release through inositol 1,4,5-trisphosphate receptors and inhibits Ca2+ uptake by mitochondria without affecting ER calcium store content. Cell Calcium 2008; 44(3): 324-38.
    • (2008) Cell Calcium , vol.44 , Issue.3 , pp. 324-338
    • Hanson, C.J.1    Bootman, M.D.2    Distelhorst, C.W.3    Wojcikiewicz, R.J.4    Roderick, H.L.5
  • 111
    • 0031993255 scopus 로고    scopus 로고
    • Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast
    • Xu Q, Reed JC. Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast. Mol Cell 1998; 1(3): 337-46.
    • (1998) Mol Cell , vol.1 , Issue.3 , pp. 337-346
    • Xu, Q.1    Reed, J.C.2
  • 112
    • 4344648874 scopus 로고    scopus 로고
    • Activating transcription factor 4 is translationally regulated by hypoxic stress
    • Blais JD, Filipenko V, Bi M, et al. Activating transcription factor 4 is translationally regulated by hypoxic stress. Mol Cell Biol 2004; 24(17): 7469-82.
    • (2004) Mol Cell Biol , vol.24 , Issue.17 , pp. 7469-7482
    • Blais, J.D.1    Filipenko, V.2    Bi, M.3
  • 113
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe EL, Walker SA, Manifava M, et al. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J Cell Biol 2008; 182(4): 685-701.
    • (2008) J Cell Biol , vol.182 , Issue.4 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3
  • 115
    • 71649112895 scopus 로고    scopus 로고
    • 3D tomography reveals connections between the phagophore and endoplasmic reticulum
    • Ylä-Anttila P, Vihinen H, Jokitalo E, Eskelinen EL. 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy 2009; 5(8): 1180-5.
    • (2009) Autophagy , vol.5 , Issue.8 , pp. 1180-1185
    • Ylä-Anttila, P.1    Vihinen, H.2    Jokitalo, E.3    Eskelinen, E.L.4
  • 116
    • 34250891313 scopus 로고    scopus 로고
    • AMP-activated protein kinase: A universal regulator of autophagy?
    • Høyer-Hansen M, Jäättelä M. AMP-activated protein kinase: a universal regulator of autophagy? Autophagy 2007; 3(4): 381-3.
    • (2007) Autophagy , vol.3 , Issue.4 , pp. 381-383
    • Høyer-Hansen, M.1    Jäättelä, M.2
  • 117
    • 50249137038 scopus 로고    scopus 로고
    • Induction of macroautophagy by exogenously introduced calcium
    • Gao W, Ding WX, Stolz DB, Yin XM. Induction of macroautophagy by exogenously introduced calcium. Autophagy 2008; 4(6): 754-61.
    • (2008) Autophagy , vol.4 , Issue.6 , pp. 754-761
    • Gao, W.1    Ding, W.X.2    Stolz, D.B.3    Yin, X.M.4
  • 118
    • 68149139456 scopus 로고    scopus 로고
    • The autophagy effector Beclin 1: A novel BH3-only protein
    • Sinha S, Levine B. The autophagy effector Beclin 1: a novel BH3-only protein. Oncogene 2008; 27 (Suppl 1): S137-48.
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 1
    • Sinha, S.1    Levine, B.2
  • 119
    • 10344262564 scopus 로고    scopus 로고
    • Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes
    • Shimizu S, Kanaseki T, Mizushima N, et al. Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes. Nat Cell Biol 2004; 6(12): 1221-8.
    • (2004) Nat Cell Biol , vol.6 , Issue.12 , pp. 1221-1228
    • Shimizu, S.1    Kanaseki, T.2    Mizushima, N.3
  • 120
    • 77950252174 scopus 로고    scopus 로고
    • Cross talk between apoptosis and autophagy by caspase-mediated cleavage of Beclin 1
    • Djavaheri-Mergny M, Maiuri MC, Kroemer G. Cross talk between apoptosis and autophagy by caspase-mediated cleavage of Beclin 1. Oncogene 2010; 29(12): 1717-9.
    • (2010) Oncogene , vol.29 , Issue.12 , pp. 1717-1719
    • Djavaheri-Mergny, M.1    Maiuri, M.C.2    Kroemer, G.3
  • 121
    • 61849102389 scopus 로고    scopus 로고
    • DAP-kinasemediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy
    • Zalckvar E, Berissi H, Mizrachy L, et al. DAP-kinasemediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy. EMBO Rep 2009; 10(3): 285-92.
    • (2009) EMBO Rep , vol.10 , Issue.3 , pp. 285-292
    • Zalckvar, E.1    Berissi, H.2    Mizrachy, L.3
  • 122
    • 67549135655 scopus 로고    scopus 로고
    • The inositol 1,4,5-trisphosphate receptor regulates autophagy through its interaction with Beclin 1
    • Vicencio JM, Ortiz C, Criollo A, et al. The inositol 1,4,5-trisphosphate receptor regulates autophagy through its interaction with Beclin 1. Cell Death Differ 2009; 16(7): 1006-17.
    • (2009) Cell Death Differ , vol.16 , Issue.7 , pp. 1006-1017
    • Vicencio, J.M.1    Ortiz, C.2    Criollo, A.3
  • 123
    • 34247380330 scopus 로고    scopus 로고
    • Regulation of autophagy by the inositol trisphosphate receptor
    • Criollo A, Maiuri MC, Tasdemir E, et al. Regulation of autophagy by the inositol trisphosphate receptor. Cell Death Differ 2007; 14(5): 1029-39.
    • (2007) Cell Death Differ , vol.14 , Issue.5 , pp. 1029-1039
    • Criollo, A.1    Maiuri, M.C.2    Tasdemir, E.3
  • 124
    • 77952504754 scopus 로고    scopus 로고
    • Acidic calcium stores open for business: Expanding the potential for intracellular Ca2+ signaling
    • Patel S, Docampo R. Acidic calcium stores open for business: expanding the potential for intracellular Ca2+ signaling. Trends Cell Biol 2010; 20(5): 277-86.
    • (2010) Trends Cell Biol , vol.20 , Issue.5 , pp. 277-286
    • Patel, S.1    Docampo, R.2
  • 125
    • 0034643304 scopus 로고    scopus 로고
    • Molecular cloning of a novel form (two-repeat) protein related to voltage-gated sodium and calcium channels
    • Ishibashi K, Suzuki M, Imai M. Molecular cloning of a novel form (two-repeat) protein related to voltage-gated sodium and calcium channels. Biochem Biophys Res Commun 2000; 270(2): 370-6.
    • (2000) Biochem Biophys Res Commun , vol.270 , Issue.2 , pp. 370-376
    • Ishibashi, K.1    Suzuki, M.2    Imai, M.3
  • 126
    • 0034496224 scopus 로고    scopus 로고
    • Functional visualization of the separate but interacting calcium stores sensitive to NAADP and cyclic ADP-ribose
    • Lee HC, Aarhus R. Functional visualization of the separate but interacting calcium stores sensitive to NAADP and cyclic ADP-ribose. J Cell Sci 2000; 113 (Pt 24): 4413-20.
    • (2000) J Cell Sci , vol.113 , Issue.Pt 24 , pp. 4413-4420
    • Lee, H.C.1    Aarhus, R.2
  • 127
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: From phenomenology to molecular understanding in less than a decade
    • Klionsky DJ. Autophagy: from phenomenology to molecular understanding in less than a decade. Nat Rev Mol Cell Biol 2007; 8(11): 931-7.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.11 , pp. 931-937
    • Klionsky, D.J.1
  • 128
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function
    • Saftig P, Klumperman J. Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat Rev Mol Cell Biol 2009; 10(9): 623-35.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.9 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 129
    • 0028279373 scopus 로고
    • Use of glycyl-L-phenylalanine 2-naphthylamide, a lysosomedisrupting cathepsin C substrate, to distinguish between lysosomes and prelysosomal endocytic vacuoles
    • Berg TO, Strømhaug E, Løvdal T, Seglen O, Berg T. Use of glycyl-L-phenylalanine 2-naphthylamide, a lysosomedisrupting cathepsin C substrate, to distinguish between lysosomes and prelysosomal endocytic vacuoles. Biochem J 1994; 300 (Pt 1): 229-36.
    • (1994) Biochem J , vol.300 , Issue.Pt 1 , pp. 229-236
    • Berg, T.O.1    Strømhaug, E.2    Løvdal, T.3    Seglen, O.4    Berg, T.5
  • 130
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman EJ, Siebers A, Altendorf K. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc Natl Acad Sci USA 1988; 85(21): 7972-6.
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.21 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 131
    • 0028950282 scopus 로고
    • A derivative of NADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADPribose
    • Lee HC, Aarhus R. A derivative of NADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADPribose. J Biol Chem 1995; 270(5): 2152-7.
    • (1995) J Biol Chem , vol.270 , Issue.5 , pp. 2152-2157
    • Lee, H.C.1    Aarhus, R.2
  • 132
    • 0035033022 scopus 로고    scopus 로고
    • Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers
    • Lee HC. Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers. Annu Rev Pharmacol Toxicol 2001; 41: 317-45.
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 317-345
    • Lee, H.C.1
  • 133
    • 17844368321 scopus 로고    scopus 로고
    • The NAADP receptor: New receptors or new regulation?
    • Galione A, Petersen OH. The NAADP receptor: new receptors or new regulation? Mol Interv 2005; 5(2): 73-9.
    • (2005) Mol Interv , vol.5 , Issue.2 , pp. 73-79
    • Galione, A.1    Petersen, O.H.2
  • 135
    • 0034744519 scopus 로고    scopus 로고
    • Specific Ca2+ signaling evoked by cholecystokinin and acetylcholine: The roles of NAADP, cADPR, and IP3
    • Cancela JM. Specific Ca2+ signaling evoked by cholecystokinin and acetylcholine: the roles of NAADP, cADPR, and IP3. Annu Rev Physiol 2001; 63: 99-117.
    • (2001) Annu Rev Physiol , vol.63 , pp. 99-117
    • Cancela, J.M.1
  • 136
    • 0037195094 scopus 로고    scopus 로고
    • Nicotinic acid-adenine dinucleotide phosphate-sensitive calcium stores initiate insulin signaling in human beta cells
    • Johnson JD, Misler S. Nicotinic acid-adenine dinucleotide phosphate-sensitive calcium stores initiate insulin signaling in human beta cells. Proc Natl Acad Sci USA 2002; 99(22): 14566-71.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.22 , pp. 14566-14571
    • Johnson, J.D.1    Misler, S.2
  • 137
    • 0036289262 scopus 로고    scopus 로고
    • Ca(2+) response to cADPr during maturation and fertilization of starfish oocytes
    • Nusco GA, Lim D, Sabala P, Santella L. Ca(2+) response to cADPr during maturation and fertilization of starfish oocytes. Biochem Biophys Res Commun 2002; 290(3): 1015-21.
    • (2002) Biochem Biophys Res Commun , vol.290 , Issue.3 , pp. 1015-1021
    • Nusco, G.A.1    Lim, D.2    Sabala, P.3    Santella, L.4
  • 138
    • 0037418583 scopus 로고    scopus 로고
    • Calcium signaling: NAADP ascends as a new messenger
    • Lee HC. Calcium signaling: NAADP ascends as a new messenger. Curr Biol 2003; 13(5): R186-8.
    • (2003) Curr Biol , vol.13 , Issue.5
    • Lee, H.C.1
  • 139
    • 0035815631 scopus 로고    scopus 로고
    • Prolonged inactivation of nicotinic acid adenine dinucleotide phosphate-induced Ca2+ release mediates a spatiotemporal Ca2+ memory
    • Churchill GC, Galione A. Prolonged inactivation of nicotinic acid adenine dinucleotide phosphate-induced Ca2+ release mediates a spatiotemporal Ca2+ memory. J Biol Chem 2001; 276(14): 11223-5.
    • (2001) J Biol Chem , vol.276 , Issue.14 , pp. 11223-11225
    • Churchill, G.C.1    Galione, A.2
  • 140
    • 0036950248 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate mediates Ca2+ signals and contraction in arterial smooth muscle via a two-pool mechanism
    • Boittin FX, Galione A, Evans AM. Nicotinic acid adenine dinucleotide phosphate mediates Ca2+ signals and contraction in arterial smooth muscle via a two-pool mechanism. Circ Res 2002; 91(12): 1168-75.
    • (2002) Circ Res , vol.91 , Issue.12 , pp. 1168-1175
    • Boittin, F.X.1    Galione, A.2    Evans, A.M.3
  • 141
    • 0037108774 scopus 로고    scopus 로고
    • Nicotinic acid-adenine dinucleotide phosphate activates the skeletal muscle ryanodine receptor
    • Hohenegger M, Suko J, Gscheidlinger R, Drobny H, Zidar A. Nicotinic acid-adenine dinucleotide phosphate activates the skeletal muscle ryanodine receptor. Biochem J 2002; 367 (Pt 2): 423-31.
    • (2002) Biochem J , vol.367 , Issue.Pt 2 , pp. 423-431
    • Hohenegger, M.1    Suko, J.2    Gscheidlinger, R.3    Drobny, H.4    Zidar, A.5
  • 142
    • 34548479246 scopus 로고    scopus 로고
    • Reconstitution and characterization of a nicotinic acid adenine dinucleotide phosphate (NAADP)-sensitive Ca2+ release channel from liver lysosomes of rats
    • Zhang F, Li PL. Reconstitution and characterization of a nicotinic acid adenine dinucleotide phosphate (NAADP)-sensitive Ca2+ release channel from liver lysosomes of rats. J Biol Chem 2007; 282(35): 25259-69.
    • (2007) J Biol Chem , vol.282 , Issue.35 , pp. 25259-25269
    • Zhang, F.1    Li, P.L.2
  • 143
    • 33845602018 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate and cyclic ADP-ribose regulate TRPM2 channels in T lymphocytes
    • Beck A, Kolisek M, Bagley LA, Fleig A, Penner R. Nicotinic acid adenine dinucleotide phosphate and cyclic ADP-ribose regulate TRPM2 channels in T lymphocytes. FASEB J 2006; 20(7): 962-4.
    • (2006) FASEB J , vol.20 , Issue.7 , pp. 962-964
    • Beck, A.1    Kolisek, M.2    Bagley, L.A.3    Fleig, A.4    Penner, R.5
  • 144
    • 39749189470 scopus 로고    scopus 로고
    • NAADP+ is an agonist of the human P2Y11 purinergic receptor
    • Moreschi I, Bruzzone S, Bodrato N, et al. NAADP+ is an agonist of the human P2Y11 purinergic receptor. Cell Calcium 2008; 43(4): 344-55.
    • (2008) Cell Calcium , vol.43 , Issue.4 , pp. 344-355
    • Moreschi, I.1    Bruzzone, S.2    Bodrato, N.3
  • 145
    • 15244350821 scopus 로고    scopus 로고
    • The vacuolar Ca2+-activated channel TPC1 regulates germination and stomatal movement
    • Peiter E, Maathuis FJ, Mills LN, et al. The vacuolar Ca2+-activated channel TPC1 regulates germination and stomatal movement. Nature 2005; 434(7031): 404-8.
    • (2005) Nature , vol.434 , Issue.7031 , pp. 404-408
    • Peiter, E.1    Maathuis, F.J.2    Mills, L.N.3
  • 146
    • 68149149128 scopus 로고    scopus 로고
    • The acid test: The discovery of two-pore channels (TPCs) as NAADP-gated endolysosomal Ca(2+) release channels
    • Galione A, Evans AM, Ma J, et al. The acid test: the discovery of two-pore channels (TPCs) as NAADP-gated endolysosomal Ca(2+) release channels. Pflugers Arch 2009; 458(5): 869-76.
    • (2009) Pflugers Arch , vol.458 , Issue.5 , pp. 869-876
    • Galione, A.1    Evans, A.M.2    Ma, J.3
  • 147
    • 67349287016 scopus 로고    scopus 로고
    • NAADP mobilizes calcium from acidic organelles through two-pore channels
    • Calcraft PJ, Ruas M, Pan Z, et al. NAADP mobilizes calcium from acidic organelles through two-pore channels. Nature 2009; 459(7246): 596-600.
    • (2009) Nature , vol.459 , Issue.7246 , pp. 596-600
    • Calcraft, P.J.1    Ruas, M.2    Pan, Z.3
  • 148
    • 79953173921 scopus 로고    scopus 로고
    • Cyclic adenosine diphosphate ribose activates ryanodine receptors, whereas NAADP activates two-pore domain channels
    • Ogunbayo OA, Zhu Y, Rossi D, et al. Cyclic adenosine diphosphate ribose activates ryanodine receptors, whereas NAADP activates two-pore domain channels. J Biol Chem 2011; 286: 9136-40.
    • (2011) J Biol Chem , vol.286 , pp. 9136-9140
    • Ogunbayo, O.A.1    Zhu, Y.2    Rossi, D.3
  • 149
    • 77951205549 scopus 로고    scopus 로고
    • Purified TPC Isoforms Form NAADP Receptors with Distinct Roles for Ca(2+) Signaling and Endolysosomal Trafficking
    • Ruas M, Rietdorf K, Arredouani A, et al. Purified TPC Isoforms Form NAADP Receptors with Distinct Roles for Ca(2+) Signaling and Endolysosomal Trafficking. Curr Biol 2010; 20(8): 703-9.
    • (2010) Curr Biol , vol.20 , Issue.8 , pp. 703-709
    • Ruas, M.1    Rietdorf, K.2    Arredouani, A.3
  • 150
    • 0028222874 scopus 로고
    • Autophagy and related mechanisms of lysosomemediated protein degradation
    • Dunn WA. Autophagy and related mechanisms of lysosomemediated protein degradation. Trends Cell Biol 1994; 4(4): 139-43.
    • (1994) Trends Cell Biol , vol.4 , Issue.4 , pp. 139-143
    • Dunn, W.A.1
  • 151
    • 33749041268 scopus 로고    scopus 로고
    • Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy
    • Eskelinen EL. Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy. Mol Aspects Med 2006; 27(5-6): 495-502.
    • (2006) Mol Aspects Med , vol.27 , Issue.5-6 , pp. 495-502
    • Eskelinen, E.L.1
  • 152
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist M, Jäättelä M. Four deaths and a funeral: from caspases to alternative mechanisms. Nat Rev Mol Cell Biol 2001; 2(8): 589-98.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , Issue.8 , pp. 589-598
    • Leist, M.1    Jäättelä, M.2
  • 155
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • Kroemer G, Jäättelä M. Lysosomes and autophagy in cell death control. Nat Rev Cancer 2005; 5(11): 886-97.
    • (2005) Nat Rev Cancer , vol.5 , Issue.11 , pp. 886-897
    • Kroemer, G.1    Jäättelä, M.2
  • 156
    • 62949128915 scopus 로고    scopus 로고
    • Lysosomal involvement in cell death and cancer
    • Kirkegaard T, Jäättelä M. Lysosomal involvement in cell death and cancer. Biochim Biophys Acta 2009; 1793(4): 746-54.
    • (2009) Biochim Biophys Acta , vol.1793 , Issue.4 , pp. 746-754
    • Kirkegaard, T.1    Jäättelä, M.2
  • 158
    • 49649123891 scopus 로고    scopus 로고
    • Cysteine cathepsins trigger caspase-dependent cell death through cleavage of bid and antiapoptotic Bcl-2 homologues
    • Droga-Mazovec G, Bojic L, Petelin A, et al. Cysteine cathepsins trigger caspase-dependent cell death through cleavage of bid and antiapoptotic Bcl-2 homologues. J Biol Chem 2008; 283(27): 19140-50.
    • (2008) J Biol Chem , vol.283 , Issue.27 , pp. 19140-19150
    • Droga-Mazovec, G.1    Bojic, L.2    Petelin, A.3
  • 159
    • 79951580969 scopus 로고    scopus 로고
    • Lysosomal membrane permeabilization causes oxidative stress and ferritin induction in macrophages
    • Ghosh M, Carlsson F, Laskar A, Yuan XM, Li W. Lysosomal membrane permeabilization causes oxidative stress and ferritin induction in macrophages. FEBS Lett 2011; 585(4): 623-9.
    • (2011) FEBS Lett , vol.585 , Issue.4 , pp. 623-629
    • Ghosh, M.1    Carlsson, F.2    Laskar, A.3    Yuan, X.M.4    Li, W.5
  • 160
    • 0033756474 scopus 로고    scopus 로고
    • Cathepsin B contributes to TNF-alpha-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c
    • Guicciardi ME, Deussing J, Miyoshi H, et al. Cathepsin B contributes to TNF-alpha-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c. J Clin Invest 2000; 106(9): 1127-37.
    • (2000) J Clin Invest , vol.106 , Issue.9 , pp. 1127-1137
    • Guicciardi, M.E.1    Deussing, J.2    Miyoshi, H.3
  • 161
    • 0035947776 scopus 로고    scopus 로고
    • Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor
    • Foghsgaard L, Wissing D, Mauch D, et al. Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor. J Cell Biol 2001; 153(5): 999-1010.
    • (2001) J Cell Biol , vol.153 , Issue.5 , pp. 999-1010
    • Foghsgaard, L.1    Wissing, D.2    Mauch, D.3
  • 162
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosisinducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidère N, Lorenzo HK, Carmona S, et al. Cathepsin D triggers Bax activation, resulting in selective apoptosisinducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J Biol Chem 2003; 278(33): 31401-11.
    • (2003) J Biol Chem , vol.278 , Issue.33 , pp. 31401-31411
    • Bidère, N.1    Lorenzo, H.K.2    Carmona, S.3
  • 163
    • 33646133216 scopus 로고    scopus 로고
    • UVA/B-induced apoptosis in human melanocytes involves translocation of cathepsins and Bcl-2 family members
    • Bivik CA, Larsson PK, Kågedal KM, Rosdahl IK, Ollinger KM. UVA/B-induced apoptosis in human melanocytes involves translocation of cathepsins and Bcl-2 family members. J Invest Dermatol 2006; 126(5): 1119-27.
    • (2006) J Invest Dermatol , vol.126 , Issue.5 , pp. 1119-1127
    • Bivik, C.A.1    Larsson, P.K.2    Kågedal, K.M.3    Rosdahl, I.K.4    Ollinger, K.M.5
  • 164
    • 0031897739 scopus 로고    scopus 로고
    • Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes
    • Roberg K, Ollinger K. Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes. Am J Pathol 1998; 152(5): 1151-6.
    • (1998) Am J Pathol , vol.152 , Issue.5 , pp. 1151-1156
    • Roberg, K.1    Ollinger, K.2
  • 165
    • 0035408169 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress
    • Kågedal K, Johansson U, Ollinger K. The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress. FASEB J 2001; 15(9): 1592-4.
    • (2001) FASEB J , vol.15 , Issue.9 , pp. 1592-1594
    • Kågedal, K.1    Johansson, U.2    Ollinger, K.3
  • 166
    • 0348038755 scopus 로고    scopus 로고
    • Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1)
    • Houseweart MK, Vilaythong A, Yin XM, Turk B, Noebels JL, Myers RM. Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1). Cell Death Differ 2003; 10(12): 1329-35.
    • (2003) Cell Death Differ , vol.10 , Issue.12 , pp. 1329-1335
    • Houseweart, M.K.1    Vilaythong, A.2    Yin, X.M.3    Turk, B.4    Noebels, J.L.5    Myers, R.M.6
  • 167
    • 2442661614 scopus 로고    scopus 로고
    • Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation
    • Heinrich M, Neumeyer J, Jakob M, et al. Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation. Cell Death Differ 2004; 11(5): 550-63.
    • (2004) Cell Death Differ , vol.11 , Issue.5 , pp. 550-563
    • Heinrich, M.1    Neumeyer, J.2    Jakob, M.3
  • 168
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk V, Turk B, Turk D. Lysosomal cysteine proteases: facts and opportunities. EMBO J 2001; 20(17): 4629-33.
    • (2001) EMBO J , vol.20 , Issue.17 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 169
    • 41149098534 scopus 로고    scopus 로고
    • Caspase-8 is activated by cathepsin D initiating neutrophil apoptosis during the resolution of inflammation
    • Conus S, Perozzo R, Reinheckel T, et al. Caspase-8 is activated by cathepsin D initiating neutrophil apoptosis during the resolution of inflammation. J Exp Med 2008; 205(3): 685-98.
    • (2008) J Exp Med , vol.205 , Issue.3 , pp. 685-698
    • Conus, S.1    Perozzo, R.2    Reinheckel, T.3
  • 170
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • Jäättelä M, Tschopp J. Caspase-independent cell death in T lymphocytes. Nat Immunol 2003; 4(5): 416-23.
    • (2003) Nat Immunol , vol.4 , Issue.5 , pp. 416-423
    • Jäättelä, M.1    Tschopp, J.2
  • 171
    • 0038529617 scopus 로고    scopus 로고
    • Lysosomal membrane permeabilization induces cell death in a mitochondriondependent fashion
    • Boya P, Andreau K, Poncet D, et al. Lysosomal membrane permeabilization induces cell death in a mitochondriondependent fashion. J Exp Med 2003; 197(10): 1323-34.
    • (2003) J Exp Med , vol.197 , Issue.10 , pp. 1323-1334
    • Boya, P.1    Andreau, K.2    Poncet, D.3
  • 172
    • 33847388051 scopus 로고    scopus 로고
    • Calcium: A fundamental regulator of intracellular membrane fusion?
    • Hay JC. Calcium: a fundamental regulator of intracellular membrane fusion? EMBO Rep 2007; 8(3): 236-40.
    • (2007) EMBO Rep , vol.8 , Issue.3 , pp. 236-240
    • Hay, J.C.1
  • 173
    • 0032481105 scopus 로고    scopus 로고
    • Calcium uptake via endocytosis with rapid release from acidifying endosomes
    • Gerasimenko JV, Tepikin AV, Petersen OH, Gerasimenko OV. Calcium uptake via endocytosis with rapid release from acidifying endosomes. Curr Biol 1998; 8(24): 1335-8.
    • (1998) Curr Biol , vol.8 , Issue.24 , pp. 1335-1338
    • Gerasimenko, J.V.1    Tepikin, A.V.2    Petersen, O.H.3    Gerasimenko, O.V.4
  • 174
    • 0030866081 scopus 로고    scopus 로고
    • Homotypic fusion between aggregated lysosomes triggered by elevated [Ca2+]i in fibroblasts
    • Bakker AC, Webster P, Jacob WA, Andrews NW. Homotypic fusion between aggregated lysosomes triggered by elevated [Ca2+]i in fibroblasts. J Cell Sci 1997; 110 (Pt 18): 2227-38.
    • (1997) J Cell Sci , vol.110 , Issue.Pt 18 , pp. 2227-2238
    • Bakker, A.C.1    Webster, P.2    Jacob, W.A.3    Andrews, N.W.4
  • 175
    • 0025319665 scopus 로고
    • Role of calcium ions in regulation of mammalian intramitochondrial metabolism
    • McCormack JG, Halestrap AP, Denton RM. Role of calcium ions in regulation of mammalian intramitochondrial metabolism. Physiol Rev 1990; 70(2): 391-425.
    • (1990) Physiol Rev , vol.70 , Issue.2 , pp. 391-425
    • McCormack, J.G.1    Halestrap, A.P.2    Denton, R.M.3
  • 176
    • 0030615262 scopus 로고    scopus 로고
    • Lysosomes behave as Ca2+-regulated exocytic vesicles in fibroblasts and epithelial cells
    • Rodríguez A, Webster P, Ortego J, Andrews NW. Lysosomes behave as Ca2+-regulated exocytic vesicles in fibroblasts and epithelial cells. J Cell Biol 1997; 137(1): 93-104.
    • (1997) J Cell Biol , vol.137 , Issue.1 , pp. 93-104
    • Rodríguez, A.1    Webster, P.2    Ortego, J.3    Andrews, N.W.4
  • 178
    • 0027495705 scopus 로고
    • Dependence of hepatocytic autophagy on intracellularly sequestered calcium
    • Gordon PB, Holen I, Fosse M, Røtnes JS, Seglen PO. Dependence of hepatocytic autophagy on intracellularly sequestered calcium. J Biol Chem 1993; 268(35): 26107-12.
    • (1993) J Biol Chem , vol.268 , Issue.35 , pp. 26107-26112
    • Gordon, P.B.1    Holen, I.2    Fosse, M.3    Røtnes, J.S.4    Seglen, P.O.5
  • 179
    • 33846189759 scopus 로고    scopus 로고
    • Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2
    • Høyer-Hansen M, Bastholm L, Szyniarowski P, et al. Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2. Mol Cell 2007; 25(2): 193-205.
    • (2007) Mol Cell , vol.25 , Issue.2 , pp. 193-205
    • Høyer-Hansen, M.1    Bastholm, L.2    Szyniarowski, P.3
  • 180
    • 40449139980 scopus 로고    scopus 로고
    • The itinerary of autophagosomes: From peripheral formation to kiss-and-run fusion with lysosomes
    • Jahreiss L, Menzies FM, Rubinsztein DC. The itinerary of autophagosomes: from peripheral formation to kiss-and-run fusion with lysosomes. Traffic 2008; 9(4): 574-87.
    • (2008) Traffic , vol.9 , Issue.4 , pp. 574-587
    • Jahreiss, L.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 181
    • 47149089713 scopus 로고    scopus 로고
    • Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes
    • Kimura S, Noda T, Yoshimori T. Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes. Cell Struct Funct 2008; 33(1): 109-22.
    • (2008) Cell Struct Funct , vol.33 , Issue.1 , pp. 109-122
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 182
    • 69449093622 scopus 로고    scopus 로고
    • Mammalian macroautophagy at a glance
    • Ravikumar B, Futter M, Jahreiss L, et al. Mammalian macroautophagy at a glance. J Cell Sci 2009; 122 (Pt 11): 1707-11.
    • (2009) J Cell Sci , vol.122 , Issue.Pt 11 , pp. 1707-1711
    • Ravikumar, B.1    Futter, M.2    Jahreiss, L.3
  • 183
    • 0035192612 scopus 로고    scopus 로고
    • Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion
    • Ishihara N, Hamasaki M, Yokota S, et al. Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol Biol Cell 2001; 12(11): 3690-702.
    • (2001) Mol Biol Cell , vol.12 , Issue.11 , pp. 3690-3702
    • Ishihara, N.1    Hamasaki, M.2    Yokota, S.3
  • 184
    • 33745885329 scopus 로고    scopus 로고
    • DRAM, a p53-induced modulator of autophagy, is critical for apoptosis
    • Crighton D, Wilkinson S, O'Prey J, et al. DRAM, a p53-induced modulator of autophagy, is critical for apoptosis. Cell 2006; 126(1): 121-34.
    • (2006) Cell , vol.126 , Issue.1 , pp. 121-134
    • Crighton, D.1    Wilkinson, S.2    O'Prey, J.3
  • 185
    • 0032506510 scopus 로고    scopus 로고
    • Membrane fusion. Ready aim fire
    • Schekman R. Membrane fusion. Ready aim fire! Nature 1998; 396(6711): 514-5.
    • (1998) Nature , vol.396 , Issue.6711 , pp. 514-515
    • Schekman, R.1
  • 187
    • 0028014372 scopus 로고
    • Vacuolar ATPase activity is required for endosomal carrier vesicle formation
    • Clague MJ, Urbé S, Aniento F, Gruenberg J. Vacuolar ATPase activity is required for endosomal carrier vesicle formation. J Biol Chem 1994; 269(1): 21-4.
    • (1994) J Biol Chem , vol.269 , Issue.1 , pp. 21-24
    • Clague, M.J.1    Urbé, S.2    Aniento, F.3    Gruenberg, J.4
  • 188
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • Yamamoto A, Tagawa Y, Yoshimori T, Moriyama Y, Masaki R, Tashiro Y. Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct Funct 1998; 23(1): 33-42.
    • (1998) Cell Struct Funct , vol.23 , Issue.1 , pp. 33-42
    • Yamamoto, A.1    Tagawa, Y.2    Yoshimori, T.3    Moriyama, Y.4    Masaki, R.5    Tashiro, Y.6
  • 190
    • 64249134706 scopus 로고    scopus 로고
    • VMA21 deficiency causes an autophagic myopathy by compromising V-ATPase activity and lysosomal acidification
    • Ramachandran N, Munteanu I, Wang P, et al. VMA21 deficiency causes an autophagic myopathy by compromising V-ATPase activity and lysosomal acidification. Cell 2009; 137(2): 235-46.
    • (2009) Cell , vol.137 , Issue.2 , pp. 235-246
    • Ramachandran, N.1    Munteanu, I.2    Wang, P.3
  • 191
    • 79953316595 scopus 로고    scopus 로고
    • Lysosomal positioning coordinates cellular nutrient responses
    • Korolchuk VI, Saiki S, Lichtenberg M, et al. Lysosomal positioning coordinates cellular nutrient responses. Nat Cell Biol 2011; 13(4): 453-60.
    • (2011) Nat Cell Biol , vol.13 , Issue.4 , pp. 453-460
    • Korolchuk, V.I.1    Saiki, S.2    Lichtenberg, M.3
  • 192
    • 0033822172 scopus 로고    scopus 로고
    • Identification of the gene causing mucolipidosis type IV
    • Bargal R, Avidan N, Ben-Asher E, et al. Identification of the gene causing mucolipidosis type IV. Nat Genet 2000; 26(1): 118-23.
    • (2000) Nat Genet , vol.26 , Issue.1 , pp. 118-123
    • Bargal, R.1    Avidan, N.2    Ben-Asher, E.3
  • 194
    • 80051473235 scopus 로고    scopus 로고
    • PI(3,5)P(2) controls membrane trafficking by direct activation of mucolipin Ca(2+) release channels in the endolysosome
    • Dong XP, Shen D, Wang X, et al. PI(3,5)P(2) controls membrane trafficking by direct activation of mucolipin Ca(2+) release channels in the endolysosome. Nat Commun 2010; 1: 38.
    • (2010) Nat Commun , vol.1 , pp. 38
    • Dong, X.P.1    Shen, D.2    Wang, X.3
  • 195
    • 37549009562 scopus 로고    scopus 로고
    • Gain-of-function mutation in TRPML3 causes the mouse Varitint-Waddler phenotype
    • Kim HJ, Li Q, Tjon-Kon-Sang S, So I, Kiselyov K, Muallem S. Gain-of-function mutation in TRPML3 causes the mouse Varitint-Waddler phenotype. J Biol Chem 2007; 282(50): 36138-42.
    • (2007) J Biol Chem , vol.282 , Issue.50 , pp. 36138-36142
    • Kim, H.J.1    Li, Q.2    Tjon-Kon-Sang, S.3    So, I.4    Kiselyov, K.5    Muallem, S.6
  • 196
    • 42449103570 scopus 로고    scopus 로고
    • A novel mode of TRPML3 regulation by extracytosolic pH absent in the varitint-waddler phenotype
    • Kim HJ, Li Q, Tjon-Kon-Sang S, et al. A novel mode of TRPML3 regulation by extracytosolic pH absent in the varitint-waddler phenotype. EMBO J 2008; 27(8): 1197-205.
    • (2008) EMBO J , vol.27 , Issue.8 , pp. 1197-1205
    • Kim, H.J.1    Li, Q.2    Tjon-Kon-Sang, S.3
  • 197
    • 67649870315 scopus 로고    scopus 로고
    • The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy
    • Kim HJ, Soyombo AA, Tjon-Kon-Sang S, So I, Muallem S. The Ca(2+) channel TRPML3 regulates membrane trafficking and autophagy. Traffic 2009; 10(8): 1157-67.
    • (2009) Traffic , vol.10 , Issue.8 , pp. 1157-1167
    • Kim, H.J.1    Soyombo, A.A.2    Tjon-Kon-Sang, S.3    So, I.4    Muallem, S.5
  • 198
    • 79952315766 scopus 로고    scopus 로고
    • Influence of aging on membrane permeability transition in brain mitochondria
    • Toman J, Fiskum G. Influence of aging on membrane permeability transition in brain mitochondria. J Bioenerg Biomembr 2011; 43(1): 3-10.
    • (2011) J Bioenerg Biomembr , vol.43 , Issue.1 , pp. 3-10
    • Toman, J.1    Fiskum, G.2
  • 199
    • 77549088703 scopus 로고    scopus 로고
    • Calcium dysregulation in amyotrophic lateral sclerosis
    • Grosskreutz J, Van Den Bosch L, Keller BU. Calcium dysregulation in amyotrophic lateral sclerosis. Cell Calcium 2010; 47(2): 165-74.
    • (2010) Cell Calcium , vol.47 , Issue.2 , pp. 165-174
    • Grosskreutz, J.1    van den Bosch, L.2    Keller, B.U.3
  • 200
    • 77954403183 scopus 로고    scopus 로고
    • Glutamate-induced alterations in Ca2+ signaling are modulated by mitochondrial Ca2+ handling capacity in brain slices of R6/1 transgenic mice
    • Rosenstock TR, Bertoncini CR, Teles AV, Hirata H, Fernandes MJ, Smaili SS. Glutamate-induced alterations in Ca2+ signaling are modulated by mitochondrial Ca2+ handling capacity in brain slices of R6/1 transgenic mice. Eur J Neurosci 2010; 32(1): 60-70.
    • (2010) Eur J Neurosci , vol.32 , Issue.1 , pp. 60-70
    • Rosenstock, T.R.1    Bertoncini, C.R.2    Teles, A.V.3    Hirata, H.4    Fernandes, M.J.5    Smaili, S.S.6
  • 201
    • 77955383022 scopus 로고    scopus 로고
    • Mitochondrial calcium uptake capacity as a therapeutic target in the R6/2 mouse model of Huntington's disease
    • Perry GM, Tallaksen-Greene S, Kumar A, et al. Mitochondrial calcium uptake capacity as a therapeutic target in the R6/2 mouse model of Huntington's disease. Hum Mol Genet 2010; 19(17): 3354-71.
    • (2010) Hum Mol Genet , vol.19 , Issue.17 , pp. 3354-3371
    • Perry, G.M.1    Tallaksen-Greene, S.2    Kumar, A.3
  • 202
    • 80051497127 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate (NAADP) regulates autophagy in cultured astrocytes
    • Pereira GJ, Hirata H, Fimia GM, et al. Nicotinic acid adenine dinucleotide phosphate (NAADP) regulates autophagy in cultured astrocytes. J Biol Chem 2011; 286(32): 27875-81.
    • (2011) J Biol Chem , vol.286 , Issue.32 , pp. 27875-27881
    • Pereira, G.J.1    Hirata, H.2    Fimia, G.M.3


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