메뉴 건너뛰기




Volumn 18, Issue 1, 2011, Pages 38-47

Bcl-2 proteins regulate ER membrane permeability to luminal proteins during ER stress-induced apoptosis

Author keywords

apoptosis; Bcl 2 protein; endoplasmic reticulum; membrane permeability

Indexed keywords

PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN BID;

EID: 78650169392     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2010.68     Document Type: Article
Times cited : (81)

References (40)
  • 1
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • Cory S, Adams JM. The Bcl2 family: regulators of the cellular life-or-death switch. Nat Rev Cancer 2002; 2: 647-656.
    • (2002) Nat Rev Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 2
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • Danial NN, Korsmeyer SJ. Cell death: critical control points. Cell 2004; 116: 205-219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 3
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle RJ, Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 2008; 9: 47-59.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 4
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • Chipuk JE, Green DR. How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? Trends Cell Biol 2008; 18: 157-164.
    • (2008) Trends Cell Biol , vol.18 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 5
    • 0034508217 scopus 로고    scopus 로고
    • The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues
    • Lindsten T, Ross AJ, King A, Zong WX, Rathmell JC, Shiels HA et al. The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues. Mol Cell 2000; 6: 1389-1399.
    • (2000) Mol Cell , vol.6 , pp. 1389-1399
    • Lindsten, T.1    Ross, A.J.2    King, A.3    Zong, W.X.4    Rathmell, J.C.5    Shiels, H.A.6
  • 6
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei MC, Zong WX, Cheng EH, Lindsten T, Panoutsakopoulou V, Ross AJ et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 2001; 292: 727-730.
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3    Lindsten, T.4    Panoutsakopoulou, V.5    Ross, A.J.6
  • 7
    • 9344219714 scopus 로고    scopus 로고
    • Cellular distribution of Bcl-2 family proteins
    • Germain M, Shore GC. Cellular distribution of Bcl-2 family proteins. Sci STKE 2003; 2003: e10.
    • (2003) Sci STKE , vol.2003
    • Germain, M.1    Shore, G.C.2
  • 8
    • 3943071150 scopus 로고    scopus 로고
    • Cytochrome C-mediated apoptosis
    • Jiang X, Wang X. Cytochrome C-mediated apoptosis. Annu Rev Biochem 2004; 73: 87-106.
    • (2004) Annu Rev Biochem , vol.73 , pp. 87-106
    • Jiang, X.1    Wang, X.2
  • 9
    • 1642474148 scopus 로고    scopus 로고
    • Caspases: An ancient cellular sword of Damocles
    • Boyce M, Degterev A, Yuan J. Caspases: an ancient cellular sword of Damocles. Cell Death Differ 2004; 11: 29-37.
    • (2004) Cell Death Differ , vol.11 , pp. 29-37
    • Boyce, M.1    Degterev, A.2    Yuan, J.3
  • 10
    • 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. The control of endoplasmic reticulum-initiated apoptosis by the BCL-2 family of proteins. Curr Mol Med 2006; 6: 99-109.
    • (2006) Curr Mol Med , vol.6 , pp. 99-109
    • Oakes, S.A.1    Lin, S.S.2    Bassik, M.C.3
  • 11
    • 33745958168 scopus 로고    scopus 로고
    • Bcl-2 and Ca2+ homeostasis in the endoplasmic reticulum
    • Pinton P, Rizzuto R. Bcl-2 and Ca2+ homeostasis in the endoplasmic reticulum. Cell Death Differ 2006; 13: 1409-1418.
    • (2006) Cell Death Differ , vol.13 , pp. 1409-1418
    • Pinton, P.1    Rizzuto, R.2
  • 12
    • 0037035807 scopus 로고    scopus 로고
    • Bax-mediated Ca2+ mobilization promotes cytochrome c release during apoptosis
    • Nutt LK, Chandra J, Pataer A, Fang B, Roth JA, Swisher SG et al. Bax-mediated Ca2+ mobilization promotes cytochrome c release during apoptosis. J Biol Chem 2002; 277: 20301-20308.
    • (2002) J Biol Chem , vol.277 , pp. 20301-20308
    • Nutt, L.K.1    Chandra, J.2    Pataer, A.3    Fang, B.4    Roth, J.A.5    Swisher, S.G.6
  • 13
    • 0037810844 scopus 로고    scopus 로고
    • Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis
    • Zong WX, Li C, Hatzivassiliou G, Lindsten T, Yu QC, Yuan J et al. Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis. J Cell Biol 2003; 162: 59-69.
    • (2003) J Cell Biol , vol.162 , pp. 59-69
    • Zong, W.X.1    Li, C.2    Hatzivassiliou, G.3    Lindsten, T.4    Yu, Q.C.5    Yuan, J.6
  • 14
    • 21244462014 scopus 로고    scopus 로고
    • BH3-only BIK regulates BAX,BAK-dependent release of Ca2+ from endoplasmic reticulum stores and mitochondrial apoptosis during stress-induced cell death
    • Mathai JP, Germain M, Shore GC. BH3-only BIK regulates BAX,BAK-dependent release of Ca2+ from endoplasmic reticulum stores and mitochondrial apoptosis during stress-induced cell death. J Biol Chem 2005; 280: 23829-23836.
    • (2005) J Biol Chem , vol.280 , pp. 23829-23836
    • Mathai, J.P.1    Germain, M.2    Shore, G.C.3
  • 15
    • 42549144606 scopus 로고    scopus 로고
    • Bcl-2 protein family members: Versatile regulators of calcium signaling in cell survival and apoptosis
    • Rong Y, Distelhorst CW. Bcl-2 protein family members: versatile regulators of calcium signaling in cell survival and apoptosis. Annu Rev Physiol 2008; 70: 73-91.
    • (2008) Annu Rev Physiol , vol.70 , pp. 73-91
    • Rong, Y.1    Distelhorst, C.W.2
  • 16
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • De Brito OM, Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008; 456: 605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 18
    • 33746827856 scopus 로고    scopus 로고
    • Different mitochondrial intermembrane space proteins are released during apoptosis in a manner that is coordinately initiated but can vary in duration
    • Munoz-Pinedo C, Guio-Carrion A, Goldstein JC, Fitzgerald P, Newmeyer DD, Green DR. Different mitochondrial intermembrane space proteins are released during apoptosis in a manner that is coordinately initiated but can vary in duration. Proc Natl Acad Sci USA 2006; 103: 11573-11578.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11573-11578
    • Munoz-Pinedo, C.1    Guio-Carrion, A.2    Goldstein, J.C.3    Fitzgerald, P.4    Newmeyer, D.D.5    Green, D.R.6
  • 19
    • 34247549680 scopus 로고    scopus 로고
    • Methods for the assessment of mitochondrial membrane permeabilization in apoptosis
    • DOI 10.1007/s10495-007-0720-1, Special Issue on Mitochondria in Apoptosis
    • Galluzzi L, Zamzami N, de La Motte RT, Lemaire C, Brenner C, Kroemer G. Methods for the assessment of mitochondrial membrane permeabilization in apoptosis. Apoptosis 2007; 12: 803-813. (Pubitemid 46653289)
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 803-813
    • Galluzzi, L.1    Zamzami, N.2    De La Motte Rouge, T.3    Lemaire, C.4    Brenner, C.5    Kroemer, G.6
  • 20
    • 34247497716 scopus 로고    scopus 로고
    • Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes
    • Leber B, Lin J, Andrews DW. Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes. Apoptosis 2007; 12: 897-911.
    • (2007) Apoptosis , vol.12 , pp. 897-911
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 22
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum 1
    • Fujiki Y, Hubbard AL, Fowler S, Lazarow PB. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum 1. J Cell Biol 1982; 93: 97-102.
    • (1982) J Cell Biol , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 23
    • 16544394843 scopus 로고    scopus 로고
    • Translocation of Bax and Bid to mitochondria, endoplasmic reticulum and nuclear envelope: Possible control points in apoptosis 1
    • Gajkowska B, Wojewodzka U, Gajda J. Translocation of Bax and Bid to mitochondria, endoplasmic reticulum and nuclear envelope: possible control points in apoptosis 1. J Mol Histol 2004; 35: 11-19.
    • (2004) J Mol Histol , vol.35 , pp. 11-19
    • Gajkowska, B.1    Wojewodzka, U.2    Gajda, J.3
  • 24
    • 44949233264 scopus 로고    scopus 로고
    • Caspase-2 cleavage of BID is a critical apoptotic signal downstream of endoplasmic reticulum stress
    • Upton JP, Austgen K, Nishino M, Coakley KM, Hagen A, Han D et al. Caspase-2 cleavage of BID is a critical apoptotic signal downstream of endoplasmic reticulum stress. Mol Cell Biol 2008; 28: 3943-3951.
    • (2008) Mol Cell Biol , vol.28 , pp. 3943-3951
    • Upton, J.P.1    Austgen, K.2    Nishino, M.3    Coakley, K.M.4    Hagen, A.5    Han, D.6
  • 25
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana T, Mackey MR, Perkins G, Ellisman MH, Latterich M, Schneiter R et al. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 2002; 111: 331-342.
    • (2002) Cell , vol.111 , pp. 331-342
    • Kuwana, T.1    MacKey, M.R.2    Perkins, G.3    Ellisman, M.H.4    Latterich, M.5    Schneiter, R.6
  • 26
    • 34247348628 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced apoptosis requires bax for commitment and Apaf-1 for execution in primary neurons
    • Smith MI, Deshmukh M. Endoplasmic reticulum stress-induced apoptosis requires bax for commitment and Apaf-1 for execution in primary neurons. Cell Death Differ 2007; 14: 1011-1019.
    • (2007) Cell Death Differ , vol.14 , pp. 1011-1019
    • Smith, M.I.1    Deshmukh, M.2
  • 27
    • 33646373219 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced apoptosis: Multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53
    • Li J, Lee B, Lee AS. Endoplasmic reticulum stress-induced apoptosis: multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53. J Biol Chem 2006; 281: 7260-7270.
    • (2006) J Biol Chem , vol.281 , pp. 7260-7270
    • Li, J.1    Lee, B.2    Lee, A.S.3
  • 29
    • 19944432123 scopus 로고    scopus 로고
    • Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function
    • Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG et al. Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. Mol Cell 2005; 17: 393-403.
    • (2005) Mol Cell , vol.17 , pp. 393-403
    • Chen, L.1    Willis, S.N.2    Wei, A.3    Smith, B.J.4    Fletcher, J.I.5    Hinds, M.G.6
  • 30
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • Kuwana T, Bouchier-Hayes L, Chipuk JE, Bonzon C, Sullivan BA, Green DR et al. BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Mol Cell 2005; 17: 525-535.
    • (2005) Mol Cell , vol.17 , pp. 525-535
    • Kuwana, T.1    Bouchier-Hayes, L.2    Chipuk, J.E.3    Bonzon, C.4    Sullivan, B.A.5    Green, D.R.6
  • 31
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth C, Koch GL. Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 1989; 59: 729-737.
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.2
  • 33
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007; 8: 519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 34
    • 26844468253 scopus 로고    scopus 로고
    • Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte
    • Gardai SJ, McPhillips KA, Frasch SC, Janssen WJ, Starefeldt A, Murphy-Ullrich JE et al. Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte. Cell 2005; 123: 321-334.
    • (2005) Cell , vol.123 , pp. 321-334
    • Gardai, S.J.1    McPhillips, K.A.2    Frasch, S.C.3    Janssen, W.J.4    Starefeldt, A.5    Murphy-Ullrich, J.E.6
  • 35
    • 34548576109 scopus 로고    scopus 로고
    • Calreticulin exposure is required for the immunogenicity of gamma-irradiation and UVC light-induced apoptosis
    • Obeid M, Panaretakis T, Joza N, Tufi R, Tesniere A, van EP et al. Calreticulin exposure is required for the immunogenicity of gamma-irradiation and UVC light-induced apoptosis. Cell Death Differ 2007; 14: 1848-1850.
    • (2007) Cell Death Differ , vol.14 , pp. 1848-1850
    • Obeid, M.1    Panaretakis, T.2    Joza, N.3    Tufi, R.4    Tesniere, A.5    Van, E.P.6
  • 37
    • 12944303650 scopus 로고    scopus 로고
    • Growth factor regulation of autophagy and cell survival in the absence of apoptosis
    • Lum JJ, Bauer DE, Kong M, Harris MH, Li C, Lindsten T et al. Growth factor regulation of autophagy and cell survival in the absence of apoptosis. Cell 2005; 120: 237-248.
    • (2005) Cell , vol.120 , pp. 237-248
    • Lum, J.J.1    Bauer, D.E.2    Kong, M.3    Harris, M.H.4    Li, C.5    Lindsten, T.6
  • 38
    • 27144487808 scopus 로고    scopus 로고
    • The endoplasmic reticulum gateway to apoptosis by Bcl-X(L) modulation of the InsP3R
    • White C, Li C, Yang J, Petrenko NB, Madesh M, Thompson CB et al. The endoplasmic reticulum gateway to apoptosis by Bcl-X(L) modulation of the InsP3R. Nat Cell Biol 2005; 7: 1021-1028.
    • (2005) Nat Cell Biol , vol.7 , pp. 1021-1028
    • White, C.1    Li, C.2    Yang, J.3    Petrenko, N.B.4    Madesh, M.5    Thompson, C.B.6
  • 39
    • 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. Apoptosis regulation by Bcl-x(L) modulation of mammalian inositol 1,4,5-trisphosphate receptor channel isoform gating. Proc Natl Acad Sci USA 2007; 104: 12565-12570.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 12565-12570
    • Li, C.1    Wang, X.2    Vais, H.3    Thompson, C.B.4    Foskett, J.K.5    White, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.