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Volumn 9789400743519, Issue , 2012, Pages 107-142

ER stress and UPR through dysregulated ER Ca2+ homeostasis and signaling

Author keywords

Apoptosis; BI 1; Ca2+; Ca2+ homeostasis; Calcium binding proteins; ER intracellular Ca2+ release channels; ER stress; ERO1 a; ERp44; GRP78 Bip; IP3Rs; IRE1 a; PERK; SERCA; Sigma1 receptors; Unfolded protein response

Indexed keywords


EID: 84872591461     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-94-007-4351-9_5     Document Type: Chapter
Times cited : (8)

References (204)
  • 1
  • 2
    • 79952196841 scopus 로고    scopus 로고
    • Apoptosis and autophagy: Decoding calcium signals that mediate life or death
    • Harr MW, Distelhorst CW (2010) Apoptosis and autophagy: decoding calcium signals that mediate life or death. Cold Spring Harb Perspect Biol. 2(10):a005579
    • (2010) Cold Spring Harb Perspect Biol. , vol.2 , Issue.10 , pp. a005579
    • Harr, M.W.1    Distelhorst, C.W.2
  • 5
    • 0036877142 scopus 로고    scopus 로고
    • The endoplasmic reticulum: A multifunctional signaling organelle
    • Berridge MJ (2002) The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium 32(5-6):235-249
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 235-249
    • Berridge, M.J.1
  • 6
    • 77950860036 scopus 로고    scopus 로고
    • Intracellular Ca2 + storage in health and disease: A dynamic equilibrium
    • Sammels E, Parys JB, Missiaen L, Smedt H De, Bultynck G (2010) Intracellular Ca2 + storage in health and disease: a dynamic equilibrium. Cell Calcium 47(4):297-314
    • (2010) Cell Calcium , vol.47 , Issue.4 , pp. 297-314
    • Sammels, E.1    Parys, J.B.2    Missiaen, L.3    De Smedt, H.4    Bultynck, G.5
  • 8
    • 0031594742 scopus 로고    scopus 로고
    • The endoplasmic reticulum Ca2 + store: A view from the lumen
    • Meldolesi J, Pozzan T (1998) The endoplasmic reticulum Ca2 + store: a view from the lumen. Trends Biochem Sci 23(1):10-14
    • (1998) Trends Biochem Sci , vol.23 , Issue.1 , pp. 10-14
    • Meldolesi, J.1    Pozzan, T.2
  • 10
    • 1842431755 scopus 로고    scopus 로고
    • Calsequestrin and the calcium release channel of skeletal and cardiac muscle
    • Beard NA, Laver DR, Dulhunty AF (2004) Calsequestrin and the calcium release channel of skeletal and cardiac muscle. Prog Biophys Mol Biol 85(1):33-69
    • (2004) Prog Biophys Mol Biol , vol.85 , Issue.1 , pp. 33-69
    • Beard, N.A.1    Laver, D.R.2    Dulhunty, A.F.3
  • 11
    • 0142075876 scopus 로고    scopus 로고
    • Molecular chaperones, stress proteins and redox homeostasis
    • Papp E, Nardai G, Soti C, Csermely, P (2003) Molecular chaperones, stress proteins and redox homeostasis. Biofactors 17(1-4):249-257
    • (2003) Biofactors , vol.17 , Issue.1-4 , pp. 249-257
    • Papp, E.1    Nardai, G.2    Soti, C.3    Csermely, P.4
  • 12
    • 59849120392 scopus 로고    scopus 로고
    • Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
    • Michalak M, Groenendyk J, Szabo E, Gold LI, Opas M (2009) Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem J 417(3):651-66
    • (2009) Biochem J , vol.417 , Issue.3 , pp. 651-666
    • Michalak, M.1    Groenendyk, J.2    Szabo, E.3    Gold, L.I.4    Opas, M.5
  • 14
    • 0037119465 scopus 로고    scopus 로고
    • Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin
    • Leach MR, Cohen-Doyle MF, Thomas DY, Williams DB (2002) Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin. J Biol Chem 277(33):29686-29697
    • (2002) J Biol Chem , vol.277 , Issue.33 , pp. 29686-29697
    • Leach, M.R.1    Cohen-Doyle, M.F.2    Thomas, D.Y.3    Williams, D.B.4
  • 15
    • 0346727443 scopus 로고    scopus 로고
    • Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: Pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition
    • Kapoor M, Ellgaard L, Gopalakrishnapai J, Schirra C, Gemma E, Oscarson S, Helenius A, Surolia A (2004) Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition. Biochemistry 43(1):97-106
    • (2004) Biochemistry , vol.43 , Issue.1 , pp. 97-106
    • Kapoor, M.1    Ellgaard, L.2    Gopalakrishnapai, J.3    Schirra, C.4    Gemma, E.5    Oscarson, S.6    Helenius, A.7    Surolia, A.8
  • 17
    • 0035846853 scopus 로고    scopus 로고
    • Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment
    • Ellgaard L, Riek R, Braun D, Herrmann T, Helenius A, Wuthrich K (2001) Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment. FEBS Lett 488(1-2):69-73
    • (2001) FEBS Lett , vol.488 , Issue.1-2 , pp. 69-73
    • Ellgaard, L.1    Riek, R.2    Braun, D.3    Herrmann, T.4    Helenius, A.5    Wuthrich, K.6
  • 18
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • Vassilakos A, Michalak M, Lehrman MA, Williams DB (1998) Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 37(10):3480-3490
    • (1998) Biochemistry , vol.37 , Issue.10 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Williams, D.B.4
  • 20
    • 0025788270 scopus 로고
    • Expression of calreticulin in Escherichia coli and identification of its Ca2 + binding domains
    • Baksh S, Michalak M (1991) Expression of calreticulin in Escherichia coli and identification of its Ca2 + binding domains. J Biol Chem 266(32):21458-21465.
    • (1991) J Biol Chem , vol.266 , Issue.32 , pp. 21458-21458
    • Baksh, S.1    Michalak, M.2
  • 21
    • 1842405433 scopus 로고    scopus 로고
    • BiP, a major chaperone protein of the endoplasmic reticulum lumen, plays a direct and important role in the storage of the rapidly exchanging pool of Ca2 +
    • Lievremont JP, Rizzuto R, Hendershot L, Meldolesi J (1997) BiP, a major chaperone protein of the endoplasmic reticulum lumen, plays a direct and important role in the storage of the rapidly exchanging pool of Ca2 +. J Biol Chem 272(49):30873-30879
    • (1997) J Biol Chem , vol.272 , Issue.49 , pp. 30873-30879
    • Lievremont, J.P.1    Rizzuto, R.2    Hendershot, L.3    Meldolesi, J.4
  • 22
    • 0033210210 scopus 로고    scopus 로고
    • GRP94, an ER chaperone with protein and peptide binding properties
    • Argon Y, Simen BB (1999) GRP94, an ER chaperone with protein and peptide binding properties. Semin Cell Dev Biol 10(5):495-505
    • (1999) Semin Cell Dev Biol , vol.10 , Issue.5 , pp. 495-505
    • Argon, Y.1    Simen, B.B.2
  • 23
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • Brini M, Carafoli E (2009) Calcium pumps in health and disease. Physiol Rev 89(4):1341-1378
    • (2009) Physiol Rev , vol.89 , Issue.4 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 24
    • 38849097238 scopus 로고    scopus 로고
    • SERCA pumps and human diseases
    • Hovnanian A (2007) SERCA pumps and human diseases. Subcell Biochem 45:337-363
    • (2007) Subcell Biochem , vol.45 , pp. 337-363
    • Hovnanian, A.1
  • 26
    • 34047219171 scopus 로고    scopus 로고
    • SERCA pump isoforms: Their role in calcium transport and disease
    • Periasamy M, Kalyanasundaram A (2007) SERCA pump isoforms: their role in calcium transport and disease. Muscle Nerve 35(4):430-442
    • (2007) Muscle Nerve , vol.35 , Issue.4 , pp. 430-442
    • Periasamy, M.1    Kalyanasundaram, A.2
  • 28
    • 84870313272 scopus 로고    scopus 로고
    • A diversity of SERCA Ca2 + pump inhibitors
    • Michelangeli F, East JM (2011) A diversity of SERCA Ca2 + pump inhibitors. Biochem Soc Trans 39(3):789-797
    • (2011) Biochem Soc Trans , vol.39 , Issue.3 , pp. 789-797
    • Michelangeli, F.1    East, J.M.2
  • 29
    • 0032913349 scopus 로고    scopus 로고
    • Calcium signaling and cytotoxicity
    • Kass GE, Orrenius S (1999) Calcium signaling and cytotoxicity. Environ Health Perspect 107(Suppl 1):25-35
    • (1999) Environ Health Perspect , vol.107 , Issue.1 , pp. 25-35
    • Kass, G.E.1    Orrenius, S.2
  • 30
    • 84931415807 scopus 로고    scopus 로고
    • Intracellular Ca2 + channels -A growing community
    • Taylor CW, Dale P (2011) Intracellular Ca2 + channels -A growing community. Mol Cell Endocrinol.
    • (2011) Mol Cell Endocrinol.
    • Taylor, C.W.1    Dale, P.2
  • 31
    • 34248584090 scopus 로고    scopus 로고
    • Inositol trisphosphate receptor Ca2 + release channels
    • Foskett JK, White C, Cheung KH, Mak DO (2007) Inositol trisphosphate receptor Ca2 + release channels. Physiol Rev 87(2):593-658
    • (2007) Physiol Rev , vol.87 , Issue.2 , pp. 593-658
    • Foskett, J.K.1    White, C.2    Cheung, K.H.3    Mak, D.O.4
  • 32
    • 34547897405 scopus 로고    scopus 로고
    • IP3 receptor/Ca2 + channel: From discovery to new signaling concepts
    • Mikoshiba K (2007) IP3 receptor/Ca2 + channel: from discovery to new signaling concepts. J Neurochem 102(5):1426-1446
    • (2007) J Neurochem , vol.102 , Issue.5 , pp. 1426-1446
    • Mikoshiba, K.1
  • 33
    • 84857501714 scopus 로고    scopus 로고
    • The IP3 receptor/Ca2 + channel and its cellular function
    • Mikoshiba K (2007) The IP3 receptor/Ca2 + channel and its cellular function. Biochem Soc Symp (74):9-22
    • (2007) Biochem Soc Symp , Issue.74 , pp. 9-22
    • Mikoshiba, K.1
  • 36
    • 0036878801 scopus 로고    scopus 로고
    • The endoplasmic reticulum and neuronal calcium signalling
    • Verkhratsky A (2002) The endoplasmic reticulum and neuronal calcium signalling. Cell Calcium 32(5-6):393-404
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 393-404
    • Verkhratsky, A.1
  • 37
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signalling
    • Berridge MJ, Irvine RF (1989) Inositol phosphates and cell signalling. Nature 341(6239):197-205
    • (1989) Nature , vol.341 , Issue.6239 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 38
    • 79952592038 scopus 로고    scopus 로고
    • IP3 receptors: Toward understanding their activation
    • Taylor CW, Tovey SC (2010) IP3 receptors: toward understanding their activation. Cold Spring Harb Perspect Biol 2(12):a004010
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , Issue.12 , pp. a004010
    • Taylor, C.W.1    Tovey, S.C.2
  • 39
    • 0026432666 scopus 로고
    • Ehrlich BE Bell-shaped calcium-response curves of Ins(1,4,5)P3-and calcium-gated channels from endoplasmic reticulum of cerebellum
    • Bezprozvanny I, Watras J (1991) Ehrlich BE Bell-shaped calcium-response curves of Ins(1,4,5)P3-and calcium-gated channels from endoplasmic reticulum of cerebellum. Nature 351(6329):751-754
    • (1991) Nature , vol.351 , Issue.6329 , pp. 751-754
    • Bezprozvanny, I.1    Watras, J.2
  • 40
    • 0026611054 scopus 로고
    • Ca2 + release induced by inositol 1,4,5-trisphosphate is a steady-state phenomenon controlled by luminal Ca2 + in permeabilized cells
    • Missiaen L, Smedt, H De, Droogmans G, Casteels R (1992) Ca2 + release induced by inositol 1,4,5-trisphosphate is a steady-state phenomenon controlled by luminal Ca2 + in permeabilized cells. Nature 357(6379):599-602
    • (1992) Nature , vol.357 , Issue.6379 , pp. 599-602
    • Missiaen, L.1    Smedt, H.D.2    Droogmans, G.3    Casteels, R.4
  • 41
    • 0026613092 scopus 로고
    • Luminal Ca2 + controls the activation of the inositol 1,4,5-trisphosphate receptor by cytosolic Ca2 +
    • Missiaen L, Smedt, H De, Droogmans G, Casteels R (1992) Luminal Ca2 + controls the activation of the inositol 1,4,5-trisphosphate receptor by cytosolic Ca2 +. J Biol Chem 267(32):22961-22966
    • (1992) J Biol Chem , vol.267 , Issue.32 , pp. 22961-22966
    • Missiaen, L.1    Smedt, H.D.2    Droogmans, G.3    Casteels, R.4
  • 42
    • 70349686734 scopus 로고    scopus 로고
    • Calcium-induced calcium release in skeletal muscle
    • Endo M (2009) Calcium-induced calcium release in skeletal muscle. Physiol Rev 89(4):1153-1176
    • (2009) Physiol Rev , vol.89 , Issue.4 , pp. 1153-1176
    • Endo, M.1
  • 43
    • 35449001639 scopus 로고    scopus 로고
    • Regulation of ryanodine receptors in the heart
    • Lehnart S, Marks AR (2007) Regulation of ryanodine receptors in the heart. Circ Res 101(8):746-749
    • (2007) Circ Res , vol.101 , Issue.8 , pp. 746-749
    • Lehnart, S.1    Marks, A.R.2
  • 45
    • 0033083405 scopus 로고    scopus 로고
    • Protein-protein interactions in intracellular Ca2 + -release channel function
    • Mackrill JJ (1999) Protein-protein interactions in intracellular Ca2 + -release channel function. Biochem J 337 (Pt 3): 345-361
    • (1999) Biochem J , vol.337 , pp. 345-361
    • Mackrill, J.J.1
  • 46
    • 34548644786 scopus 로고    scopus 로고
    • Modulation of the ryanodine receptor and intracellular calcium
    • Zalk R, Lehnart SE, Marks AR (2007) Modulation of the ryanodine receptor and intracellular calcium. Annu Rev Biochem 76:367-385
    • (2007) Annu Rev Biochem , vol.76 , pp. 367-385
    • Zalk, R.1    Lehnart, S.E.2    Marks, A.R.3
  • 47
    • 80052619373 scopus 로고    scopus 로고
    • Bcl-2 interaction with the inositol 1,4,5-trisphosphate receptor: Role in Ca2 + signaling and disease
    • Distelhorst CW, Bootman MD (2011) Bcl-2 interaction with the inositol 1,4,5-trisphosphate receptor: Role in Ca2 + signaling and disease. Cell Calcium 50(3):234-241
    • (2011) Cell Calcium , vol.50 , Issue.3 , pp. 234-241
    • Distelhorst, C.W.1    Bootman, M.D.2
  • 48
    • 80052638037 scopus 로고    scopus 로고
    • A dual role for Ca2 + in autophagy regulation
    • Decuypere JP, Bultynck G, Parys JB (2011) A dual role for Ca2 + in autophagy regulation. Cell Calcium 50(3):242-250
    • (2011) Cell Calcium , vol.50 , Issue.3 , pp. 242-250
    • Decuypere, J.P.1    Bultynck, G.2    Parys, J.B.3
  • 51
    • 80054015726 scopus 로고    scopus 로고
    • Molecular mechanisms of endolysosomal Ca2 + signalling in health and disease
    • Morgan AJ, Platt FM, Lloyd-Evans E, Galione A (2011) Molecular mechanisms of endolysosomal Ca2 + signalling in health and disease. Biochem J 439(3):349-374
    • (2011) Biochem J , vol.439 , Issue.3 , pp. 349-374
    • Morgan, A.J.1    Platt, F.M.2    Lloyd-Evans, E.3    Galione, A.4
  • 52
    • 0032530396 scopus 로고    scopus 로고
    • The Golgi apparatus is an inositol 1,4,5-trisphosphatesensitive Ca2 + store, with functional properties distinct from those of the endoplasmic reticulum
    • Pinton P, Pozzan T, Rizzuto R (1998) The Golgi apparatus is an inositol 1,4,5-trisphosphatesensitive Ca2 + store, with functional properties distinct from those of the endoplasmic reticulum. EMBO J. 17(18):5298-5308
    • (1998) EMBO J. , vol.17 , Issue.18 , pp. 5298-5308
    • Pinton, P.1    Pozzan, T.2    Rizzuto, R.3
  • 55
    • 80054961068 scopus 로고    scopus 로고
    • The trans-golgi compartment: A new distinct intracellular Ca store
    • Pizzo P, Lissandron V, Pozzan T (2010) The trans-golgi compartment: A new distinct intracellular Ca store. Commun Integr Biol 3(5):462-464
    • (2010) Commun Integr Biol , vol.3 , Issue.5 , pp. 462-464
    • Pizzo, P.1    Lissandron, V.2    Pozzan, T.3
  • 56
    • 77952710840 scopus 로고    scopus 로고
    • Unique characteristics of Ca2 + homeostasis of the trans-Golgi compartment
    • Lissandron V, Podini P, Pizzo P, Pozzan T (2010) Unique characteristics of Ca2 + homeostasis of the trans-Golgi compartment. Proc Natl Acad Sci U S A 107(20):9198-9203
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.20 , pp. 9198-9203
    • Lissandron, V.1    Podini, P.2    Pizzo, P.3    Pozzan, T.4
  • 58
    • 77952671939 scopus 로고    scopus 로고
    • TPCs: Endolysosomal channels for Ca2 + mobilization from acidic organelles triggered by NAADP
    • Zhu MX, Ma J, Parrington J, Galione A, Evans AM (2010) TPCs: Endolysosomal channels for Ca2 + mobilization from acidic organelles triggered by NAADP. FEBS Lett 584(10):1966-1974
    • (2010) FEBS Lett , vol.584 , Issue.10 , pp. 1966-1974
    • Zhu, M.X.1    Ma, J.2    Parrington, J.3    Galione, A.4    Evans, A.M.5
  • 60
    • 79960644805 scopus 로고    scopus 로고
    • Physiological roles of NAADP-mediated Ca2 + signaling
    • Galione A, Parrington J, Funnell T (2011) Physiological roles of NAADP-mediated Ca2 + signaling. Sci China Life Sci 54(8):725-732
    • (2011) Sci China Life Sci , vol.54 , Issue.8 , pp. 725-732
    • Galione, A.1    Parrington, J.2    Funnell, T.3
  • 64
    • 0036878809 scopus 로고    scopus 로고
    • Interactions between calcium release pathways: Multiple messengers and multiple stores
    • Galione A, Churchill GC (2002) Interactions between calcium release pathways: multiple messengers and multiple stores. Cell Calcium 32(5-6):343-354
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 343-354
    • Galione, A.1    Churchill, G.C.2
  • 65
    • 0036878788 scopus 로고    scopus 로고
    • Calcium leak from intracellular stores\-The enigma of calcium signalling
    • Camello C, Lomax R, Petersen OH, Tepikin AV (2002) Calcium leak from intracellular stores\-The enigma of calcium signalling. Cell Calcium 32(5-6):355-361
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 355-361
    • Camello, C.1    Lomax, R.2    Petersen, O.H.3    Tepikin, A.V.4
  • 67
    • 33847136350 scopus 로고    scopus 로고
    • Intracellular Ca2 + release via the ER translocon activates store-operated calcium entry
    • Ong HL, Liu X, Sharma A, Hegde RS, Ambudkar IS (2007) Intracellular Ca2 + release via the ER translocon activates store-operated calcium entry. Pflugers Arch 453(6):797-808
    • (2007) Pflugers Arch , vol.453 , Issue.6 , pp. 797-808
    • Ong, H.L.1    Liu, X.2    Sharma, A.3    Hegde, R.S.4    Ambudkar, I.S.5
  • 68
    • 33845656359 scopus 로고    scopus 로고
    • Passive calcium leak via translocon is a first step for iPLA2-pathway regulated store operated channels activation
    • Flourakis M, Coppenolle F Van, Lehen'kyi V, Beck B, Skryma R, Prevarskaya N (2006) Passive calcium leak via translocon is a first step for iPLA2-pathway regulated store operated channels activation. FASEB J 20(8):1215-1217
    • (2006) FASEB J , vol.20 , Issue.8 , pp. 1215-1217
    • Flourakis, M.1    De Coppenolle, F.2    Lehen'kyi, V.3    Beck, B.4    Skryma, R.5    Prevarskaya, N.6
  • 70
    • 0037033784 scopus 로고    scopus 로고
    • Internal Ca2 + release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue
    • Denis V, Cyert MS (2002) Internal Ca2 + release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue. J Cell Biol 156(1):29-34
    • (2002) J Cell Biol , vol.156 , Issue.1 , pp. 29-34
    • Denis, V.1    Cyert, M.S.2
  • 71
    • 73649098810 scopus 로고    scopus 로고
    • Transient receptor potential canonical type 1(TRPC1) operates as a sarcoplasmic reticulum calcium leak channel in skeletal muscle
    • Berbey C, Weiss N, Legrand C, Allard B (2009) Transient receptor potential canonical type 1 (TRPC1) operates as a sarcoplasmic reticulum calcium leak channel in skeletal muscle. J Biol Chem 284(52):36387-36394
    • (2009) J Biol Chem , vol.284 , Issue.52 , pp. 36387-36394
    • Berbey, C.1    Weiss, N.2    Legrand, C.3    Allard, B.4
  • 72
    • 0038751852 scopus 로고    scopus 로고
    • Versatile regulation of cytosolic Ca2 + by vanilloid receptor i in rat dorsal root ganglion neurons
    • Liu M, Liu MC, Magoulas C, Priestley JV, Willmott NJ (2003) Versatile regulation of cytosolic Ca2 + by vanilloid receptor I in rat dorsal root ganglion neurons. J Biol Chem 278(7):5462-5472
    • (2003) J Biol Chem , vol.278 , Issue.7 , pp. 5462-5472
    • Liu, M.1    Liu, M.C.2    Magoulas, C.3    Priestley, J.V.4    Willmott, N.J.5
  • 73
    • 0038414614 scopus 로고    scopus 로고
    • Discrimination of intracellular calcium store subcompartments using TRPV1(transient receptor potential channel, vanilloid subfamily member 1) release channel activity
    • Turner H, Fleig A, Stokes A, Kinet JP, Penner R (2003) Discrimination of intracellular calcium store subcompartments using TRPV1 (transient receptor potential channel, vanilloid subfamily member 1) release channel activity. Biochem J 371(Pt 2):341-50
    • (2003) Biochem J , vol.371 , pp. 341-350
    • Turner, H.1    Fleig, A.2    Stokes, A.3    Kinet, J.P.4    Penner, R.5
  • 74
    • 70450247017 scopus 로고    scopus 로고
    • The endoplasmic reticulum of dorsal root ganglion neurons contains functional TRPV1 channels
    • Gallego-Sandin S, Rodriguez-Garcia A, Alonso MT, Garcia-Sancho J (2009) The endoplasmic reticulum of dorsal root ganglion neurons contains functional TRPV1 channels. J Biol Chem 284(47):32591-3601
    • (2009) J Biol Chem , vol.284 , Issue.47 , pp. 32591-33601
    • Gallego-Sandin, S.1    Rodriguez-Garcia, A.2    Alonso, M.T.3    Garcia-Sancho, J.4
  • 75
    • 62149132733 scopus 로고    scopus 로고
    • A small component of the endoplasmic reticulum is required for store-operated Ca2 + channel activation in liver cells: Evidence from studies using TRPV1 and taurodeoxycholic acid
    • Castro J, Aromataris EC, Rychkov GY, Barritt GJ (2009) A small component of the endoplasmic reticulum is required for store-operated Ca2 + channel activation in liver cells: evidence from studies using TRPV1 and taurodeoxycholic acid. Biochem J 418(3):553-566
    • (2009) Biochem J , vol.418 , Issue.3 , pp. 553-566
    • Castro, J.1    Aromataris, E.C.2    Rychkov, G.Y.3    Barritt, G.J.4
  • 81
    • 29244462514 scopus 로고    scopus 로고
    • Polycystin 2 interacts with type i inositol 1,4,5-trisphosphate receptor to modulate intracellular Ca2 + signaling
    • Li Y, Wright JM, Qian F, Germino GG, Guggino WB (2005) Polycystin 2 interacts with type I inositol 1,4,5-trisphosphate receptor to modulate intracellular Ca2 + signaling. J Biol Chem 280(50):41298-41306
    • (2005) J Biol Chem , vol.280 , Issue.50 , pp. 41298-41306
    • Li, Y.1    Wright, J.M.2    Qian, F.3    Germino, G.G.4    Guggino, W.B.5
  • 82
  • 83
    • 77953319993 scopus 로고    scopus 로고
    • Polycystin-2 activation by inositol 1,4,5-trisphosphate-induced Ca2 + release requires its direct association with the inositol 1,4,5-trisphosphate receptor in a signaling microdomain
    • Sammels E, Devogelaere B, Mekahli D, Bultynck G, Missiaen L, Parys JB, Cai Y, Somlo S, Smedt H De (2010) Polycystin-2 activation by inositol 1,4,5-trisphosphate-induced Ca2 + release requires its direct association with the inositol 1,4,5-trisphosphate receptor in a signaling microdomain. J Biol Chem 285(24):18794-18805
    • (2010) J Biol Chem , vol.285 , Issue.24 , pp. 18794-18805
    • Sammels, E.1    Devogelaere, B.2    Mekahli, D.3    Bultynck, G.4    Missiaen, L.5    Parys, J.B.6    Cai, Y.7    Somlo, S.8    De Smedt, H.9
  • 90
    • 45549102988 scopus 로고    scopus 로고
    • BI-1 regulates endoplasmic reticulum Ca2 + homeostasis downstream of Bcl-2 family proteins
    • Xu C, Xu W, Palmer AE, Reed JC (2008) BI-1 regulates endoplasmic reticulum Ca2 + homeostasis downstream of Bcl-2 family proteins. J Biol Chem 283(17):11477-11484
    • (2008) J Biol Chem , vol.283 , Issue.17 , pp. 11477-11484
    • Xu, C.1    Xu, W.2    Palmer, A.E.3    Reed, J.C.4
  • 91
    • 63049085256 scopus 로고    scopus 로고
    • Ca2+/H+ antiporter-like activity of human recombinant Bax inhibitor-1 reconstituted into liposomes
    • Ahn T, Yun CH, Chae HZ, Kim HR, Chae HJ (2009) Ca2+/H+ antiporter-like activity of human recombinant Bax inhibitor-1 reconstituted into liposomes. FEBS J 276(8):2285-2291
    • (2009) FEBS J , vol.276 , Issue.8 , pp. 2285-2291
    • Ahn, T.1    Yun, C.H.2    Chae, H.Z.3    Kim, H.R.4    Chae, H.J.5
  • 96
    • 56849113081 scopus 로고    scopus 로고
    • Role of SERCA1 truncated isoform in the proapoptotic calcium transfer from ER to mitochondria during ER stress
    • Chami M, Oules B, Szabadkai G, Tacine R, Rizzuto R, Paterlini-Brechot P (2008) Role of SERCA1 truncated isoform in the proapoptotic calcium transfer from ER to mitochondria during ER stress. Mol Cell 32(5):641-651
    • (2008) Mol Cell , vol.32 , Issue.5 , pp. 641-651
    • Chami, M.1    Oules, B.2    Szabadkai, G.3    Tacine, R.4    Rizzuto, R.5    Paterlini-Brechot, P.6
  • 97
    • 18844404413 scopus 로고    scopus 로고
    • Capacitative calcium entry: Sensing the calcium stores
    • Putney JW Jr (2005) Capacitative calcium entry: sensing the calcium stores. J Cell Biol 169(3):381-382
    • (2005) J Cell Biol , vol.169 , Issue.3 , pp. 381-382
    • Putney, J.W.1
  • 98
    • 34347324120 scopus 로고    scopus 로고
    • New molecular players in capacitative Ca2 + entry
    • Putney JW Jr (2007) New molecular players in capacitative Ca2 + entry. J Cell Sci 120(Pt 12):1959-1965
    • (2007) J Cell Sci , vol.120 , pp. 1959-1965
    • Putney, J.W.1
  • 99
    • 77950377028 scopus 로고    scopus 로고
    • Molecular basis of calcium signaling in lymphocytes: STIM and ORAI
    • Hogan PG, Lewis RS, Rao A (2010) Molecular basis of calcium signaling in lymphocytes: STIM and ORAI. Annu Rev Immunol 28:491-533
    • (2010) Annu Rev Immunol , vol.28 , pp. 491-533
    • Hogan, P.G.1    Lewis, R.S.2    Rao, A.3
  • 100
    • 37349129852 scopus 로고    scopus 로고
    • STIM2 is a feedback regulator that stabilizes basal cytosolic and endoplasmic reticulum Ca2 + levels
    • Brandman O, Liou J, Park WS, Meyer T (2007) STIM2 is a feedback regulator that stabilizes basal cytosolic and endoplasmic reticulum Ca2 + levels. Cell 131(7):1327-1339
    • (2007) Cell , vol.131 , Issue.7 , pp. 1327-1339
    • Brandman, O.1    Liou, J.2    Park, W.S.3    Meyer, T.4
  • 101
    • 0344897663 scopus 로고    scopus 로고
    • Bcl-2 on the endoplasmic reticulum: Protecting the mitochondria from a distance
    • Thomenius MJ, Distelhorst CW (2003) Bcl-2 on the endoplasmic reticulum: protecting the mitochondria from a distance. J Cell Sci 116(Pt 22):4493-4499
    • (2003) J Cell Sci , vol.116 , pp. 4493-4499
    • Thomenius, M.J.1    Distelhorst, C.W.2
  • 107
    • 70449088871 scopus 로고    scopus 로고
    • GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca2 + -dependent mitochondrial apoptosis
    • Sano R, Annunziata I, Patterson A, Moshiach S, Gomero E, Opferman J, Forte M, d'Azzo A (2009) GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca2 + -dependent mitochondrial apoptosis. Mol Cell 36(3):500-511
    • (2009) Mol Cell , vol.36 , Issue.3 , pp. 500-511
    • Sano, R.1    Annunziata, I.2    Patterson, A.3    Moshiach, S.4    Gomero, E.5    Opferman, J.6    Forte, M.7    D'azzo, A.8
  • 109
    • 0033104513 scopus 로고    scopus 로고
    • Encoding of Ca2 + signals by differential expression of IP3 receptor subtypes
    • Miyakawa T, Maeda A, Yamazawa T, Hirose K, Kurosaki T, Iino M (1999) Encoding of Ca2 + signals by differential expression of IP3 receptor subtypes. EMBO J 18(5):1303-1308
    • (1999) EMBO J , vol.18 , Issue.5 , pp. 1303-1308
    • Miyakawa, T.1    Maeda, A.2    Yamazawa, T.3    Hirose, K.4    Kurosaki, T.5    Iino, M.6
  • 112
    • 29944435173 scopus 로고    scopus 로고
    • Bcl-2 differentially regulates Ca2 + signals according to the strength of T cell receptor activation
    • Zhong F, Davis MC, McColl KS, Distelhorst CW (2006) Bcl-2 differentially regulates Ca2 + signals according to the strength of T cell receptor activation. J Cell Biol 172(1):127-37
    • (2006) J Cell Biol , vol.172 , Issue.1 , pp. 127-137
    • Zhong, F.1    Davis, M.C.2    McColl, K.S.3    Distelhorst, C.W.4
  • 115
    • 34547617018 scopus 로고    scopus 로고
    • Apoptosis regulation by Bcl-x(L) modulation of mammalian inositol 1,4,5-trisphosphate receptor channel isoform gating
    • Li C, Wang X, Vais H, Thompson CB, Foskett JK, White C (2007) Apoptosis regulation by Bcl-x(L) modulation of mammalian inositol 1,4,5-trisphosphate receptor channel isoform gating. Proc Natl Acad Sci U S A 104(30):12565-12570
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.30 , pp. 12565-12570
    • Li, C.1    Wang, X.2    Vais, H.3    Thompson, C.B.4    Foskett, J.K.5    White, C.6
  • 117
    • 84855643937 scopus 로고    scopus 로고
    • Bcl-xL Regulation of InsP3 Receptor Gating Mediated by Dual Ca2 + Release Channel BH3 Domains
    • Foskett JK, Yang Y, Cheung KH, Vais H (2009) Bcl-xL Regulation of InsP3 Receptor Gating Mediated by Dual Ca2 + Release Channel BH3 Domains. Biophys J 96(3 Suppl 1):391a
    • (2009) Biophys J , vol.96 , Issue.3 , pp. 391a
    • Foskett, J.K.1    Yang, Y.2    Cheung, K.H.3    Vais, H.4
  • 118
    • 77951562760 scopus 로고    scopus 로고
    • Apoptosis protection by Mcl-1 and Bcl-2 modulation of inositol 1,4,5-trisphosphate receptor-dependent Ca2 + signaling
    • Eckenrode EF, Yang J, Velmurugan GV, Foskett JK, White C (2010) Apoptosis protection by Mcl-1 and Bcl-2 modulation of inositol 1,4,5-trisphosphate receptor-dependent Ca2 + signaling. J Biol Chem. 285(18):13678-13684
    • (2010) J Biol Chem. , vol.285 , Issue.18 , pp. 13678-13684
    • Eckenrode, E.F.1    Yang, J.2    Velmurugan, G.V.3    Foskett, J.K.4    White, C.5
  • 119
    • 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, Bassik MC, Nishino M, Pozzan T, Korsmeyer SJ (2005) Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum. Proc Natl Acad Sci U S A 102(1):105-110
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.1 , pp. 105-110
    • Oakes, S.A.1    Scorrano, L.2    Opferman, J.T.3    Bassik, M.C.4    Nishino, M.5    Pozzan, T.6    Korsmeyer, S.J.7
  • 120
  • 121
    • 78649918654 scopus 로고    scopus 로고
    • Ca2 + transfer from the ER to mitochondria: Channeling cell death by a tumor suppressor
    • Jones AW, Szabadkai G (2010) Ca2 + transfer from the ER to mitochondria: channeling cell death by a tumor suppressor. Dev Cell 19(6):789-790
    • (2010) Dev Cell , vol.19 , Issue.6 , pp. 789-790
    • Jones, A.W.1    Szabadkai, G.2
  • 123
    • 80051770868 scopus 로고    scopus 로고
    • The role of PML in the control of apoptotic cell fate: A new key player at ER-mitochondria sites
    • Pinton P, Giorgi C, Pandolfi PP (2011) The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites. Cell Death Differ 18(9):1450-1456
    • (2011) Cell Death Differ , vol.18 , Issue.9 , pp. 1450-1456
    • Pinton, P.1    Giorgi, C.2    Pandolfi, P.P.3
  • 124
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol(1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • Boehning D, Patterson RL, Sedaghat L, Glebova NO, Kurosaki T, Snyder SH (2003) Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis. Nat Cell Biol 5(12):1051-1061
    • (2003) Nat Cell Biol , vol.5 , Issue.12 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.H.6
  • 125
    • 4544252174 scopus 로고    scopus 로고
    • Apoptosis and calcium: New roles for cytochrome c and inositol 1,4,5-trisphosphate
    • Boehning D, Patterson RL, Snyder SH (2004) Apoptosis and calcium: new roles for cytochrome c and inositol 1,4,5-trisphosphate. Cell Cycle 3(3):252-254
    • (2004) Cell Cycle , vol.3 , Issue.3 , pp. 252-254
    • Boehning, D.1    Patterson, R.L.2    Snyder, S.H.3
  • 126
    • 13444274308 scopus 로고    scopus 로고
    • A peptide inhibitor of cytochrome c/inositol 1,4,5-trisphosphate receptor binding blocks intrinsic and extrinsic cell death pathways
    • Boehning D, Rossum DB van, Patterson RL, Snyder SH (2005) A peptide inhibitor of cytochrome c/inositol 1,4,5-trisphosphate receptor binding blocks intrinsic and extrinsic cell death pathways. Proc Natl Acad Sci U S A 102(5):1466-1471
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.5 , pp. 1466-1471
    • Boehning, D.1    Van Rossum, D.B.2    Patterson, R.L.3    Snyder, S.H.4
  • 128
    • 5644261222 scopus 로고    scopus 로고
    • Caspase-3-induced truncation of type 1 inositol trisphosphate receptor accelerates apoptotic cell death and induces inositol trisphosphateindependent calcium release during apoptosis
    • Assefa Z, Bultynck G, Szlufcik K, Nadif Kasri N, Vermassen E, Goris J, Missiaen L, Callewaert G, Parys JB, Smedt H De (2004) Caspase-3-induced truncation of type 1 inositol trisphosphate receptor accelerates apoptotic cell death and induces inositol trisphosphateindependent calcium release during apoptosis. J Biol Chem 279(41):43227-43236
    • (2004) J Biol Chem , vol.279 , Issue.41 , pp. 43227-43236
    • Assefa, Z.1    Bultynck, G.2    Szlufcik, K.3    Nadif, K.N.4    Vermassen, E.5    Goris, J.6    Missiaen, L.7    Callewaert, G.8    Parys, J.B.9    De Smedt, H.10
  • 129
    • 38849174384 scopus 로고    scopus 로고
    • Bultynck G. Caspase-3-truncated type 1 inositol 1,4,5-trisphosphate receptor enhances intracellular Ca2 + leak and disturbs Ca2 + signaling
    • Verbert L, Lee B, Kocks SL, Assefa Z, Parys JB, Missiaen L, Callewaert G, Fissore RA, Smedt H De (2008) Bultynck, G., Caspase-3-truncated type 1 inositol 1,4,5-trisphosphate receptor enhances intracellular Ca2 + leak and disturbs Ca2 + signalling. Biol Cell 100(1):39-49
    • (2008) Biol Cell , vol.100 , Issue.1 , pp. 39-49
    • Verbert, L.1    Lee, B.2    Kocks, S.L.3    Assefa, Z.4    Parys, J.B.5    Missiaen, L.6    Callewaert, G.7    Fissore, R.A.8    De Smedt, H.9
  • 130
    • 34547134260 scopus 로고    scopus 로고
    • SPFH2 mediates the endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors and other substrates in mammalian cells
    • Pearce MM, Wang Y, Kelley GG, Wojcikiewicz RJ (2007) SPFH2 mediates the endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors and other substrates in mammalian cells. J Biol Chem 282(28):20104-20115
    • (2007) J Biol Chem , vol.282 , Issue.28 , pp. 20104-20115
    • Pearce, M.M.1    Wang, Y.2    Kelley, G.G.3    Wojcikiewicz, R.J.4
  • 131
  • 133
    • 67449102905 scopus 로고    scopus 로고
    • An endoplasmic reticulum(ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors
    • Pearce MM, Wormer DB, Wilkens S, Wojcikiewicz RJ (2009) An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors. J Biol Chem 284(16):10433-10445
    • (2009) J Biol Chem , vol.284 , Issue.16 , pp. 10433-10445
    • Pearce, M.M.1    Wormer, D.B.2    Wilkens, S.3    Wojcikiewicz, R.J.4
  • 136
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • Xu C, Bailly-Maitre B, Reed JC (2005) Endoplasmic reticulum stress: cell life and death decisions. J Clin Invest 115(10):2656-2664
    • (2005) J Clin Invest , vol.115 , Issue.10 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 138
    • 0033598828 scopus 로고    scopus 로고
    • Regulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming
    • 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 U S A 96(24):13807-13812
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.24 , pp. 13807-13812
    • Jouaville, L.S.1    Pinton, P.2    Bastianutto, C.3    Rutter, G.A.4    Rizzuto, R.5
  • 139
    • 23744440457 scopus 로고    scopus 로고
    • Mitochondrial Ca2 + homeostasis in health and disease
    • Campanella M, Pinton P, Rizzuto R (2004) Mitochondrial Ca2 + homeostasis in health and disease. Biol Res 37(4):653-660
    • (2004) Biol Res , vol.37 , Issue.4 , pp. 653-660
    • Campanella, M.1    Pinton, P.2    Rizzuto, R.3
  • 141
    • 34247480926 scopus 로고    scopus 로고
    • IP3 receptors in cell survival and apoptosis: Ca2 + release and beyond
    • Joseph SK, Hajnoczky G (2007) IP3 receptors in cell survival and apoptosis: Ca2 + release and beyond. Apoptosis 12(5):951-968
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 951-968
    • Joseph, S.K.1    Hajnoczky, G.2
  • 142
    • 54949110895 scopus 로고    scopus 로고
    • Calcium and apoptosis: ERmitochondria Ca2 + transfer in the control of apoptosis
    • Pinton P, Giorgi C, Siviero R, Zecchini E, Rizzuto R (2008) Calcium and apoptosis: ERmitochondria Ca2 + transfer in the control of apoptosis. Oncogene 27(50):6407-6418
    • (2008) Oncogene , vol.27 , Issue.50 , pp. 6407-6418
    • Pinton, P.1    Giorgi, C.2    Siviero, R.3    Zecchini, E.4    Rizzuto, R.5
  • 145
    • 0642345210 scopus 로고    scopus 로고
    • Regulation of endoplasmic reticulum Ca2 + dynamics by proapoptotic BCL-2 family members
    • Oakes SA, Opferman JT, Pozzan T, Korsmeyer SJ, Scorrano L (2003) Regulation of endoplasmic reticulum Ca2 + dynamics by proapoptotic BCL-2 family members. Biochem Pharmacol 66(8):1335-1340
    • (2003) Biochem Pharmacol , vol.66 , Issue.80 , pp. 1335-1340
    • Oakes, S.A.1    Opferman, J.T.2    Pozzan, T.3    Korsmeyer, S.J.4    Scorrano, L.5
  • 146
    • 33646183455 scopus 로고    scopus 로고
    • The control of endoplasmic reticulum-initiated apoptosis by the BCL-2 family of proteins
    • Oakes SA, Lin SS, Bassik MC (2006) The control of endoplasmic reticulum-initiated apoptosis by the BCL-2 family of proteins. Curr Mol Med 6(1):99-109
    • (2006) Curr Mol Med , vol.6 , Issue.1 , pp. 99-109
    • Oakes, S.A.1    Lin, S.S.2    Bassik, M.C.3
  • 147
    • 0027639966 scopus 로고
    • The modification and assembly of proteins in the endoplasmic reticulum
    • Gaut JR, Hendershot LM (1993) The modification and assembly of proteins in the endoplasmic reticulum. Curr Opin Cell Biol 5(4):589-595
    • (1993) Curr Opin Cell Biol , vol.5 , Issue.4 , pp. 589-595
    • Gaut, J.R.1    Hendershot, L.M.2
  • 148
    • 4444318357 scopus 로고    scopus 로고
    • ER chaperone functions during normal and stress conditions
    • Ma Y, Hendershot LM (2004) ER chaperone functions during normal and stress conditions. J Chem Neuroanat 28(1-2):51-65
    • (2004) J Chem Neuroanat , vol.28 , Issue.1-2 , pp. 51-65
    • Ma, Y.1    Hendershot, L.M.2
  • 149
    • 33646121053 scopus 로고    scopus 로고
    • Depletion of intracellular Ca2 + store itself may be a major factor in thapsigargin-induced ER stress and apoptosis in PC12 cells
    • Yoshida I, Monji A, Tashiro K, Nakamura K, Inoue R, Kanba S (2006) Depletion of intracellular Ca2 + store itself may be a major factor in thapsigargin-induced ER stress and apoptosis in PC12 cells. Neurochem Int 48(8):696-702
    • (2006) Neurochem Int , vol.48 , Issue.8 , pp. 696-702
    • Yoshida, I.1    Monji, A.2    Tashiro, K.3    Nakamura, K.4    Inoue, R.5    Kanba, S.6
  • 150
    • 79951705219 scopus 로고    scopus 로고
    • PERK activation at low glucose concentration is mediated by SERCA pump inhibition and confers preemptive cytoprotection to pancreatic beta-cells
    • Moore CE, Omikorede O, Gomez E, Willars GB, Herbert TP (2011) PERK activation at low glucose concentration is mediated by SERCA pump inhibition and confers preemptive cytoprotection to pancreatic beta-cells. Mol Endocrinol 25(2):315-326
    • (2011) Mol Endocrinol , vol.25 , Issue.2 , pp. 315-326
    • Moore, C.E.1    Omikorede, O.2    Gomez, E.3    Willars, G.B.4    Herbert, T.P.5
  • 151
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M, Kaufman RJ (2005) The mammalian unfolded protein response. Annu Rev Biochem 74:739-789
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 152
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • Schroder M, Kaufman RJ (2005) ER stress and the unfolded protein response. Mutat Res 569(1-2):29-63
    • (2005) Mutat Res , vol.569 , Issue.1-2 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 153
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra JD, Kaufman RJ (2007) The endoplasmic reticulum and the unfolded protein response. Semin Cell Dev Biol 18(6):716-731
    • (2007) Semin Cell Dev Biol , vol.18 , Issue.6 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 154
    • 57749111961 scopus 로고    scopus 로고
    • C-Src-p38 mitogen-activated protein kinase signaling is required for Akt activation in response to ionizing radiation
    • Kim MJ, Byun JY, Yun CH, Park IC, Lee KH, Lee SJ (2008) c-Src-p38 mitogen-activated protein kinase signaling is required for Akt activation in response to ionizing radiation. Mol Cancer Res 6(12):1872-1880
    • (2008) Mol Cancer Res , vol.6 , Issue.12 , pp. 1872-1880
    • Kim, M.J.1    Byun, J.Y.2    Yun, C.H.3    Park, I.C.4    Lee, K.H.5    Lee, S.J.6
  • 155
    • 79954426601 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells
    • Kimata Y, Kohno K (2011) Endoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells. Curr Opin Cell Biol 23(2):135-142
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.2 , pp. 135-142
    • Kimata, Y.1    Kohno, K.2
  • 156
    • 0030765016 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperones GRP78 and calreticulin prevent oxidative stress, Ca2 + disturbances, and cell death in renal epithelial cells
    • Liu H, Bowes RC 3rd, Water B van de, Sillence C, Nagelkerke JF, Stevens JL (1997) Endoplasmic reticulum chaperones GRP78 and calreticulin prevent oxidative stress, Ca2 + disturbances, and cell death in renal epithelial cells. J Biol Chem 272(35):21751-21759
    • (1997) J Biol Chem , vol.272 , Issue.35 , pp. 21751-21759
    • Liu, H.1    Bowes Iii, R.C.2    Van W. B, E.D.3    Sillence, C.4    Nagelkerke, J.F.5    Stevens, J.L.6
  • 158
    • 77950887221 scopus 로고    scopus 로고
    • Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1
    • Wiseman RL, Zhang Y, Lee KP, Harding HP, Haynes CM, Price J, Sicheri F, Ron D (2010) Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. Mol Cell 38(2):291-304
    • (2010) Mol Cell , vol.38 , Issue.2 , pp. 291-304
    • Wiseman, R.L.1    Zhang, Y.2    Lee, K.P.3    Harding, H.P.4    Haynes, C.M.5    Price, J.6    Sicheri, F.7    Ron, D.8
  • 159
    • 35549006797 scopus 로고    scopus 로고
    • Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca2 + signaling and cell survival
    • Hayashi T, Su TP (2007) Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca2 + signaling and cell survival. Cell 131(3):596-610
    • (2007) Cell , vol.131 , Issue.3 , pp. 596-610
    • Hayashi, T.1    Su, T.P.2
  • 162
    • 74949101860 scopus 로고    scopus 로고
    • Pivotal role of calcium/calmodulin-dependent protein kinase II in ER stress-induced apoptosis
    • Ozcan L, Tabas I (2010) Pivotal role of calcium/calmodulin-dependent protein kinase II in ER stress-induced apoptosis. Cell Cycle 9(2):223-224
    • (2010) Cell Cycle , vol.9 , Issue.2 , pp. 223-224
    • Ozcan, L.1    Tabas, I.2
  • 163
    • 77649192183 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium release potentiates the ER stress and cell death caused by an oxidative stress in MCF-7 cells
    • Dejeans N, Tajeddine N, Beck R, Verrax J, Taper H, Gailly P, Calderon PB (2010) Endoplasmic reticulum calcium release potentiates the ER stress and cell death caused by an oxidative stress in MCF-7 cells. Biochem Pharmacol 79(9):1221-1230
    • (2010) Biochem Pharmacol , vol.79 , Issue.9 , pp. 1221-1230
    • Dejeans, N.1    Tajeddine, N.2    Beck, R.3    Verrax, J.4    Taper, H.5    Gailly, P.6    Calderon, P.B.7
  • 164
    • 70349829186 scopus 로고    scopus 로고
    • Endoplasmic reticulum Ca2 + release through ryanodine and IP3 receptors contributes to neuronal excitotoxicity
    • Ruiz A, Matute C, Alberdi E (2009) Endoplasmic reticulum Ca2 + release through ryanodine and IP3 receptors contributes to neuronal excitotoxicity. Cell Calcium 46(4):273-281
    • (2009) Cell Calcium , vol.46 , Issue.4 , pp. 273-281
    • Ruiz, A.1    Matute, C.2    Alberdi, E.3
  • 165
    • 0037093384 scopus 로고    scopus 로고
    • Essential role of calcineurin in response to endoplasmic reticulum stress
    • Bonilla M, Nastase KK, Cunningham KW (2002) Essential role of calcineurin in response to endoplasmic reticulum stress. EMBO J 21(10):2343-2353
    • (2002) EMBO J , vol.21 , Issue.10 , pp. 2343-2353
    • Bonilla, M.1    Nastase, K.K.2    Cunningham, K.W.3
  • 166
    • 34548037901 scopus 로고    scopus 로고
    • Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium
    • Hoyer-Hansen M, Jaattela M (2007) Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium. Cell Death Differ 14(9):1576-1582
    • (2007) Cell Death Differ , vol.14 , Issue.9 , pp. 1576-1582
    • Hoyer-Hansen, M.1    Jaattela, M.2
  • 167
  • 170
    • 79954603845 scopus 로고    scopus 로고
    • AMPK activates autophagy by phosphorylating ULK1
    • Mao K, Klionsky DJ (2011) AMPK activates autophagy by phosphorylating ULK1. Circ Res 108(7):787-788
    • (2011) Circ Res , vol.108 , Issue.7 , pp. 787-788
    • Mao, K.1    Klionsky, D.J.2
  • 171
    • 79551507263 scopus 로고    scopus 로고
    • AMPK-dependent phosphorylation of ULK1 induces autophagy
    • Zhao M, Klionsky DJ (2011) AMPK-dependent phosphorylation of ULK1 induces autophagy. Cell Metab 13(2):119-120
    • (2011) Cell Metab , vol.13 , Issue.2 , pp. 119-120
    • Zhao, M.1    Klionsky, D.J.2
  • 173
    • 33646267694 scopus 로고    scopus 로고
    • Conformational diseases and ER stress-mediated cell death: Apoptotic cell death and autophagic cell death
    • Momoi T (2006) Conformational diseases and ER stress-mediated cell death: apoptotic cell death and autophagic cell death. Curr Mol Med 6(1):111-118
    • (2006) Curr Mol Med , vol.6 , Issue.1 , pp. 111-118
    • Momoi, T.1
  • 174
    • 78650843400 scopus 로고    scopus 로고
    • Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress
    • Torres M, Castillo K, Armisen R, Stutzin A, Soto C, Hetz C (2010) Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress. PLoS ONE 5(12):e15658
    • (2010) PLoS ONE , vol.5 , Issue.12 , pp. e15658
    • Torres, M.1    Castillo, K.2    Armisen, R.3    Stutzin, A.4    Soto, C.5    Hetz, C.6
  • 176
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li G, Mongillo M, Chin KT, Harding H, Ron D, Marks AR, Tabas I (2009) Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol 186(6):783-792
    • (2009) J Cell Biol , vol.186 , Issue.6 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6    Tabas, I.7
  • 177
    • 11844269232 scopus 로고    scopus 로고
    • Subtypespecific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44
    • Higo T, Hattori M, Nakamura T, Natsume T, Michikawa T, Mikoshiba K (2005) Subtypespecific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell 120(1):85-98
    • (2005) Cell , vol.120 , Issue.1 , pp. 85-98
    • Higo, T.1    Hattori, M.2    Nakamura, T.3    Natsume, T.4    Michikawa, T.5    Mikoshiba, K.6
  • 178
    • 31644442034 scopus 로고    scopus 로고
    • ER stress disrupts Ca2 + -signaling complexes and Ca2 + regulation in secretory and muscle cells from PERK-knockout mice
    • Huang G, Yao J, Zeng W, Mizuno Y, Kamm KE, Stull JT, Harding HP, Ron D, Muallem S (2006) ER stress disrupts Ca2 + -signaling complexes and Ca2 + regulation in secretory and muscle cells from PERK-knockout mice. J Cell Sci 119(Pt 1):153-161
    • (2006) J Cell Sci , vol.119 , pp. 153-161
    • Huang, G.1    Yao, J.2    Zeng, W.3    Mizuno, Y.4    Kamm, K.E.5    Stull, J.T.6    Harding, H.P.7    Ron, D.8    Muallem, S.9
  • 179
    • 0028963278 scopus 로고
    • Independent signaling of grp78 gene transcription and phosphorylation of eukaryotic initiator factor 2 alpha by the stressed endoplasmic reticulum
    • Brostrom MA, Prostko CR, Gmitter D, Brostrom CO (1995) Independent signaling of grp78 gene transcription and phosphorylation of eukaryotic initiator factor 2 alpha by the stressed endoplasmic reticulum. J Biol Chem 270(8):4127-4132
    • (1995) J Biol Chem , vol.270 , Issue.8 , pp. 4127-4132
    • Brostrom, M.A.1    Prostko, C.R.2    Gmitter, D.3    Brostrom, C.O.4
  • 180
    • 0033015485 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: Suppression of oxidative stress and stabilization of calcium homeostasis
    • Yu Z, Luo H, Fu W, Mattson MP (1999) The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis. Exp Neurol 155(2):302-314
    • (1999) Exp Neurol , vol.155 , Issue.2 , pp. 302-314
    • Yu, Z.1    Luo, H.2    Fu, W.3    Mattson, M.P.4
  • 181
    • 77957758520 scopus 로고    scopus 로고
    • Calcineurin interacts with PERK and dephosphorylates calnexin to relieve ER stress in mammals and frogs
    • Bollo M, Paredes RM, Holstein D, Zheleznova N, Camacho P, Lechleiter JD (2010) Calcineurin interacts with PERK and dephosphorylates calnexin to relieve ER stress in mammals and frogs. PLoS ONE 5(8):e11925
    • (2010) PLoS ONE , vol.5 , Issue.8 , pp. e11925
    • Bollo, M.1    Paredes, R.M.2    Holstein, D.3    Zheleznova, N.4    Camacho, P.5    Lechleiter, J.D.6
  • 182
    • 0029128663 scopus 로고
    • Overexpression of calreticulin increases the Ca2 + capacity of rapidly exchanging Ca2 + stores and reveals aspects of their lumenal microenvironment and function
    • Bastianutto C, Clementi E, Codazzi F, Podini P, Giorgi F De, Rizzuto R, Meldolesi J, Pozzan T (1995) Overexpression of calreticulin increases the Ca2 + capacity of rapidly exchanging Ca2 + stores and reveals aspects of their lumenal microenvironment and function. J Cell Biol 130(4):847-855
    • (1995) J Cell Biol , vol.130 , Issue.4 , pp. 847-855
    • Bastianutto, C.1    Clementi, E.2    Codazzi, F.3    Podini, P.4    De Giorgi, F.5    Rizzuto, R.6    Meldolesi, J.7    Pozzan, T.8
  • 183
    • 0032563599 scopus 로고    scopus 로고
    • Differential modulation of SERCA2 isoforms by calreticulin
    • John LM, Lechleiter JD, Camacho P (1998) Differential modulation of SERCA2 isoforms by calreticulin. J Cell Biol 142(4):963-973
    • (1998) J Cell Biol , vol.142 , Issue.4 , pp. 963-973
    • John, L.M.1    Lechleiter, J.D.2    Camacho, P.3
  • 184
    • 0034640960 scopus 로고    scopus 로고
    • Cytosolic phosphorylation of calnexin controls intracellular Ca2 + oscillations via an interaction with SERCA2b
    • Roderick HL, Lechleiter JD, Camacho P (2000) Cytosolic phosphorylation of calnexin controls intracellular Ca2 + oscillations via an interaction with SERCA2b. J Cell Biol 149(6):1235-1248
    • (2000) J Cell Biol , vol.149 , Issue.6 , pp. 1235-1248
    • Roderick, H.L.1    Lechleiter, J.D.2    Camacho, P.3
  • 185
    • 0029564658 scopus 로고
    • Interaction of calreticulin with protein disulfide isomerase
    • Baksh S, Burns K, Andrin C, Michalak M (1995) Interaction of calreticulin with protein disulfide isomerase. J Biol Chem 270(52):31338-43134
    • (1995) J Biol Chem , vol.270 , Issue.52 , pp. 31338-43134
    • Baksh, S.1    Burns, K.2    Andrin, C.3    Michalak, M.4
  • 186
    • 0347753252 scopus 로고    scopus 로고
    • Ca2 +-dependent redox modulation of SERCA 2b by ERp57
    • Li Y, Camacho P (2004) Ca2 +-dependent redox modulation of SERCA 2b by ERp57. J Cell Biol 164(1):35-46
    • (2004) J Cell Biol , vol.164 , Issue.1 , pp. 35-46
    • Li, Y.1    Camacho, P.2
  • 187
    • 0022510755 scopus 로고
    • Cytochrome P-450-dependent H2O2 production demonstrated in vivo Influence of phenobarbital and allylisopropylacetamide
    • Premereur N, Branden C Van Den, Roels F (1986) Cytochrome P-450-dependent H2O2 production demonstrated in vivo. Influence of phenobarbital and allylisopropylacetamide. FEBS Lett 199(1):19-22
    • (1986) FEBS Lett , vol.199 , Issue.1 , pp. 19-22
    • Premereur, N.1    Roels, F.2
  • 188
    • 0035699972 scopus 로고    scopus 로고
    • Association of cytochromes P450 1A2 and 2B4: Are the interactions between different P450 species involved in the control of the monooxygenase activity and coupling
    • Davydov DR, Petushkova NA, Bobrovnikova EV, Knyushko TV, Dansette P (2001) Association of cytochromes P450 1A2 and 2B4: are the interactions between different P450 species involved in the control of the monooxygenase activity and coupling? Adv Exp Med Biol 500:335-338
    • (2001) Adv Exp Med Biol , vol.500 , pp. 335-338
    • Davydov, D.R.1    Petushkova, N.A.2    Bobrovnikova, E.V.3    Knyushko, T.V.4    Dansette, P.5
  • 189
    • 4444265582 scopus 로고    scopus 로고
    • Degradation of misfolded proteins prevents ERderived oxidative stress and cell death
    • Haynes CM, Titus EA, Cooper AA ( 2004) Degradation of misfolded proteins prevents ERderived oxidative stress and cell death. Mol Cell 15(5):767-776
    • (2004) Mol Cell , vol.15 , Issue.5 , pp. 767-776
    • Haynes, C.M.1    Titus, E.A.2    Cooper, A.A.3
  • 190
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • Tu BP, Weissman JS (2004) Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 164(3):341-346
    • (2004) J Cell Biol , vol.164 , Issue.3 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 192
    • 79960216863 scopus 로고    scopus 로고
    • Bax inhibitor-1: A highly conserved endoplasmic reticulum-resident cell death suppressor
    • Ishikawa T, Watanabe N, Nagano M, Kawai-Yamada M, Lam E (2011) Bax inhibitor-1: a highly conserved endoplasmic reticulum-resident cell death suppressor. Cell Death Differ 18(8):1271-1278
    • (2011) Cell Death Differ , vol.18 , Issue.8 , pp. 1271-1278
    • Ishikawa, T.1    Watanabe, N.2    Nagano, M.3    Kawai-Yamada, M.4    Lam, E.5
  • 193
    • 0031993255 scopus 로고    scopus 로고
    • Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast
    • Xu Q, Reed JC (1998) Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast. Mol Cell 1(3):337-346
    • (1998) Mol Cell , vol.1 , Issue.3 , pp. 337-346
    • Xu, Q.1    Reed, J.C.2
  • 194
    • 0345059069 scopus 로고    scopus 로고
    • Evolutionarily conserved cytoprotection provided by Bax Inhibitor-1 homologs from animals, plants, and yeast
    • Chae HJ, Ke N, Kim HR, Chen S, Godzik A, Dickman M, Reed JC (2003) Evolutionarily conserved cytoprotection provided by Bax Inhibitor-1 homologs from animals, plants, and yeast. Gene 323:101-113
    • (2003) Gene , vol.323 , pp. 101-113
    • Chae, H.J.1    Ke, N.2    Kim, H.R.3    Chen, S.4    Godzik, A.5    Dickman, M.6    Reed, J.C.7
  • 195
    • 79960134603 scopus 로고    scopus 로고
    • Enhanced lysosomal activity is involved in Bax inhibitor-1-induced regulation of the endoplasmic reticulum(ER) stress response and cell death against ER stress: Involvement of vacuolar H + -ATPase(V-ATPase)
    • Lee GH, Kim DS, Kim HT, Lee JW, Chung CH, Ahn T, Lim JM, Kim IK, Chae HJ, Kim HR (2011) Enhanced lysosomal activity is involved in Bax inhibitor-1-induced regulation of the endoplasmic reticulum (ER) stress response and cell death against ER stress: involvement of vacuolar H + -ATPase (V-ATPase). J Biol Chem 286(28):24743-24753
    • (2011) J Biol Chem , vol.286 , Issue.28 , pp. 24743-24753
    • Lee, G.H.1    Kim, D.S.2    Kim, H.T.3    Lee, J.W.4    Chung, C.H.5    Ahn, T.6    Lim, J.M.7    Kim, I.K.8    Chae, H.J.9    Kim, H.R.10
  • 197
    • 14944347389 scopus 로고    scopus 로고
    • BI-1 protects cells from oxygen glucose deprivation by reducing the calcium content of the endoplasmic reticulum
    • Westphalen BC, Wessig J, Leypoldt F, Arnold S, Methner A (2005) BI-1 protects cells from oxygen glucose deprivation by reducing the calcium content of the endoplasmic reticulum. Cell Death Differ 12(3):304-3046
    • (2005) Cell Death Differ , vol.12 , Issue.3 , pp. 304-3046
    • Westphalen, B.C.1    Wessig, J.2    Leypoldt, F.3    Arnold, S.4    Methner, A.5
  • 199
    • 34547607269 scopus 로고    scopus 로고
    • Bax inhibitor-1 regulates endoplasmic reticulum stress-associated reactive oxygen species and heme oxygenase-1 expression
    • Lee GH, Kim HK, Chae SW, Kim DS, Ha KC, Cuddy M, Kress C, Reed JC, Kim HR, Chae HJ (2007) Bax inhibitor-1 regulates endoplasmic reticulum stress-associated reactive oxygen species and heme oxygenase-1 expression. J Biol Chem 282(30):21618-21628
    • (2007) J Biol Chem , vol.282 , Issue.30 , pp. 21618-21628
    • Lee, G.H.1    Kim, H.K.2    Chae, S.W.3    Kim, D.S.4    Ha, K.C.5    Cuddy, M.6    Kress, C.7    Reed, J.C.8    Kim, H.R.9    Chae, H.J.10
  • 200
    • 66849138212 scopus 로고    scopus 로고
    • Bax inhibitor 1 regulates ERstress-induced ROS accumulation through the regulation of cytochrome P450 2E1
    • Kim HR, Lee GH, Cho EY, Chae SW, Ahn T, Chae HJ (2009) Bax inhibitor 1 regulates ERstress-induced ROS accumulation through the regulation of cytochrome P450 2E1. J Cell Sci 122(Pt 8):1126-1133
    • (2009) J Cell Sci , vol.122 , pp. 1126-1133
    • Kim, H.R.1    Lee, G.H.2    Cho, E.Y.3    Chae, S.W.4    Ahn, T.5    Chae, H.J.6


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