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Volumn 18, Issue 2, 2013, Pages 212-225

Enhanced heterodimerization of Bax by Bcl-2 mutants improves irradiated cell survival

Author keywords

Apoptosis; Bax heterodimerization; Cell survival; Clonogenicity; Protein docking

Indexed keywords

CASPASE 9; PROTEIN BAX; PROTEIN BCL 2;

EID: 84877101490     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-012-0780-8     Document Type: Article
Times cited : (15)

References (43)
  • 1
    • 0141757504 scopus 로고    scopus 로고
    • P53 and radiation responses
    • 12947385 10.1038/sj.onc.1206677 1:CAS:528:DC%2BD3sXmslemt7o%3D
    • Fei P, El-Deiry WS (2003) p53 and radiation responses. Oncogene 22:5774-5783
    • (2003) Oncogene , vol.22 , pp. 5774-5783
    • Fei, P.1    El-Deiry, W.S.2
  • 3
    • 79955805684 scopus 로고    scopus 로고
    • Involvement of BH4 domain of Bcl-2 in the regulation of HIF-1-mediated VEGF expression in hypoxic tumor cells
    • 21233846 10.1038/cdd.2010.175 1:CAS:528:DC%2BC3MXlvFCrurc%3D
    • Trisciuoglio D, Gabellini C, Desideri M, Ragazzoni Y, De Luca T, Ziparo E, Del Bufalo D (2011) Involvement of BH4 domain of Bcl-2 in the regulation of HIF-1-mediated VEGF expression in hypoxic tumor cells. Cell Death Differ 18:1024-1035
    • (2011) Cell Death Differ , vol.18 , pp. 1024-1035
    • Trisciuoglio, D.1    Gabellini, C.2    Desideri, M.3    Ragazzoni, Y.4    De Luca, T.5    Ziparo, E.6    Del Bufalo, D.7
  • 4
    • 84861233732 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the Bcl-2 protein to predict the structure of its unordered flexible loop domain
    • 21866316 10.1007/s00894-011-1201-6 1:CAS:528:DC%2BC38XmsVaisL0%3D
    • Raghav PK, Verma YK, Gangenahalli GU (2012) Molecular dynamics simulations of the Bcl-2 protein to predict the structure of its unordered flexible loop domain. J Mol Model 18:1885-1906
    • (2012) J Mol Model , vol.18 , pp. 1885-1906
    • Raghav, P.K.1    Verma, Y.K.2    Gangenahalli, G.U.3
  • 5
    • 0028040019 scopus 로고
    • Bcl-2 and the regulation of programmed cell death
    • 8294493 10.1083/jcb.124.1.1 1:CAS:528:DyaK2cXntl2mtA%3D%3D
    • Reed JC (1994) Bcl-2 and the regulation of programmed cell death. J Cell Biol 124:1-6
    • (1994) J Cell Biol , vol.124 , pp. 1-6
    • Reed, J.C.1
  • 6
    • 0033593038 scopus 로고    scopus 로고
    • Constitutive Bcl-2 expression throughout the hematopoietic compartment affects multiple lineages and enhances progenitor cell survival
    • 10611317 10.1073/pnas.96.26.14943 1:CAS:528:DC%2BD3cXhtFamtQ%3D%3D
    • Ogilvy S, Metcalf D, Print CG, Bath ML, Harris AW, Adams JM (1999) Constitutive Bcl-2 expression throughout the hematopoietic compartment affects multiple lineages and enhances progenitor cell survival. Proc Natl Acad Sci USA 96:14943-14948
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14943-14948
    • Ogilvy, S.1    Metcalf, D.2    Print, C.G.3    Bath, M.L.4    Harris, A.W.5    Adams, J.M.6
  • 7
    • 0034641980 scopus 로고    scopus 로고
    • Apoptosis in development
    • 11048731 10.1038/35037734 1:CAS:528:DC%2BD3cXnsFWrsbg%3D
    • Meier P, Finch A, Evan G (2000) Apoptosis in development. Nature 407:796-801
    • (2000) Nature , vol.407 , pp. 796-801
    • Meier, P.1    Finch, A.2    Evan, G.3
  • 8
    • 0033603460 scopus 로고    scopus 로고
    • Bcl-2 and caspase inhibitor (zVAD-fmk) cooperate to inhibit tumor necrosis factor-α-induced cell death in a Bcl-2 cleavage independent fashion
    • 10373464 10.1074/jbc.274.26.18552 1:CAS:528:DyaK1MXkt1Shtr4%3D
    • Johnson BW, Boise LH (1999) Bcl-2 and caspase inhibitor (zVAD-fmk) cooperate to inhibit tumor necrosis factor-α-induced cell death in a Bcl-2 cleavage independent fashion. J Biol Chem 274:18552-18558
    • (1999) J Biol Chem , vol.274 , pp. 18552-18558
    • Johnson, B.W.1    Boise, L.H.2
  • 10
    • 0028307190 scopus 로고
    • The molecular basis for cell cycle delays following ionizing radiation: A review
    • 8041894 10.1016/0167-8140(94)90408-1 1:CAS:528:DyaK2cXlt1yktbs%3D
    • Maity A, McKenna WG, Muschel RJ (1994) The molecular basis for cell cycle delays following ionizing radiation: a review. Radiother Oncol 31:1-13
    • (1994) Radiother Oncol , vol.31 , pp. 1-13
    • Maity, A.1    McKenna, W.G.2    Muschel, R.J.3
  • 11
    • 21244476053 scopus 로고    scopus 로고
    • Structural conservation of residues in BH1 and BH2 domains of Bcl-2 family proteins
    • 15949801 10.1016/j.febslet.2005.05.015 1:CAS:528:DC%2BD2MXlvVWrtrg%3D
    • Gurudutta GU, Verma YK, Singh VK, Gupta P, Raj HG, Sharma RK, Chandra R (2005) Structural conservation of residues in BH1 and BH2 domains of Bcl-2 family proteins. FEBS Lett 579:3503-3507
    • (2005) FEBS Lett , vol.579 , pp. 3503-3507
    • Gurudutta, G.U.1    Verma, Y.K.2    Singh, V.K.3    Gupta, P.4    Raj, H.G.5    Sharma, R.K.6    Chandra, R.7
  • 13
    • 0023462730 scopus 로고
    • Oligonucleotide-directed mutagenesis: A simple method using two oligonucleotide primers and a single-stranded DNA template
    • 3323811 10.1016/0076-6879(87)54083-6 1:CAS:528:DyaL1cXhs1altbc%3D
    • Zoller MJ, Smith M (1987) Oligonucleotide-directed mutagenesis: a simple method using two oligonucleotide primers and a single-stranded DNA template. Methods Enzymol 154:329-350
    • (1987) Methods Enzymol , vol.154 , pp. 329-350
    • Zoller, M.J.1    Smith, M.2
  • 14
    • 0029081428 scopus 로고
    • Efficacy of tetracycline-controlled gene expression is influenced by cell type
    • 8527141 1:CAS:528:DyaK2MXntlGjtrc%3D
    • Gossen M, Bujard H (1995) Efficacy of tetracycline-controlled gene expression is influenced by cell type. Biotechniques 19:213-216
    • (1995) Biotechniques , vol.19 , pp. 213-216
    • Gossen, M.1    Bujard, H.2
  • 15
    • 0028030082 scopus 로고
    • Mechanisms underlying expression of tn10 encoded tetracycline resistance
    • 7826010 10.1146/annurev.mi.48.100194.002021 1:CAS:528:DyaK2MXhtl2rsr4%3D
    • Hillen W, Berens C (1994) Mechanisms underlying expression of tn10 encoded tetracycline resistance. Annu Rev Microbiol 48:345-369
    • (1994) Annu Rev Microbiol , vol.48 , pp. 345-369
    • Hillen, W.1    Berens, C.2
  • 16
    • 0030961033 scopus 로고    scopus 로고
    • Necrosis versus apoptosis as the mechanism of target cell death induced by Entamoeba histolytica
    • 9284127 1:CAS:528:DyaK2sXlvFKns7w%3D
    • Berninghausen O, Leippe M (1997) Necrosis versus apoptosis as the mechanism of target cell death induced by Entamoeba histolytica. Infect Immun 65:3615-3621
    • (1997) Infect Immun , vol.65 , pp. 3615-3621
    • Berninghausen, O.1    Leippe, M.2
  • 17
    • 0035892567 scopus 로고    scopus 로고
    • Improving the transfection efficiency of post-mitotic neurons
    • 11716945 10.1016/S0165-0270(01)00441-1 1:STN:280:DC%2BD3MnntFKgtg%3D%3D
    • Ohki EC, Tilkins ML, Ciccarone VC, Price PJ (2001) Improving the transfection efficiency of post-mitotic neurons. J Neurosci Methods 112:95-99
    • (2001) J Neurosci Methods , vol.112 , pp. 95-99
    • Ohki, E.C.1    Tilkins, M.L.2    Ciccarone, V.C.3    Price, P.J.4
  • 18
    • 0036721455 scopus 로고    scopus 로고
    • Spontaneous and drug-induced apoptosis is mediated by conformational changes of Bax and Bak in B-cell chronic lymphocytic leukemia
    • 12176904 10.1182/blood-2001-12-0327 1:CAS:528:DC%2BD38XmslyhtLg%3D
    • Bellosillo B, Villamor N, López-Guillermo A, Marcé S, Bosch F, Campo E, Montserrat E, Colomer D (2002) Spontaneous and drug-induced apoptosis is mediated by conformational changes of Bax and Bak in B-cell chronic lymphocytic leukemia. Blood 100:1810-1816
    • (2002) Blood , vol.100 , pp. 1810-1816
    • Bellosillo, B.1    Villamor, N.2    López-Guillermo, A.3    Marcé, S.4    Bosch, F.5    Campo, E.6    Montserrat, E.7    Colomer, D.8
  • 19
    • 0025247903 scopus 로고
    • Apoptosis. The role of the endonuclease
    • 2156431 1:CAS:528:DyaK3cXitlems74%3D
    • Arends MJ, Morris RG, Wyllie AH (1990) Apoptosis. The role of the endonuclease. Am J Pathol 136:593-608
    • (1990) Am J Pathol , vol.136 , pp. 593-608
    • Arends, M.J.1    Morris, R.G.2    Wyllie, A.H.3
  • 21
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • 8254673 10.1006/jmbi.1993.1626 1:CAS:528:DyaK2cXnt1ylug%3D%3D
    • Sali A, Blundell TL (1993) Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol 234:779-815
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 22
    • 84986512474 scopus 로고
    • CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
    • 10.1002/jcc.540040211 1:CAS:528:DyaL3sXit1aiu7w%3D
    • Brooks BR, Bruccoleri RE, Swaminathan S, Karplus M (1983) CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J Comput Chem 4:187-217
    • (1983) J Comput Chem , vol.4 , pp. 187-217
    • Brooks, B.R.1    Bruccoleri, R.E.2    Swaminathan, S.3    Karplus, M.4
  • 23
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: Three related resources
    • 9694991 10.1093/bioinformatics/14.6.523 1:CAS:528:DyaK1cXmtFWlt7w%3D
    • Rodriguez R, Chinea G, Lopez N, Pons T, Vriend G (1998) Homology modeling, model and software evaluation: three related resources. Bioinformatics 14:523-528
    • (1998) Bioinformatics , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 24
    • 0025283002 scopus 로고
    • Electrostatic interactions in macromolecules: Theory and applications
    • 10.1146/annurev.bb.19.060190.001505 1:CAS:528:DyaK3cXlvVOgtbs%3D
    • Sharp K, Honig B (1990) Electrostatic interactions in macromolecules: theory and applications. Annu Rev Biophys Chem 19:301-332
    • (1990) Ann Rev Biophys Chem , vol.19 , pp. 301-332
    • Sharp, K.1    Honig, B.2
  • 25
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • 11106734 10.1016/S0092-8674(00)00167-7 1:CAS:528:DC%2BD3cXot1Gnu7c%3D
    • Suzuki M, Youle RJ, Tjandra N (2000) Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103:645-654
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 26
    • 41949111630 scopus 로고    scopus 로고
    • Recent progress and future directions in protein-protein docking
    • 18336319 10.2174/138920308783565741 1:CAS:528:DC%2BD1cXhsFOntrw%3D
    • Ritchie DW (2008) Recent progress and future directions in protein-protein docking. Curr Protein Pept Sci 9:1-15
    • (2008) Curr Protein Pept Sci , vol.9 , pp. 1-15
    • Ritchie, D.W.1
  • 27
    • 0037016720 scopus 로고    scopus 로고
    • Cloning and expression of human core 1 beta1,3-galactosyltransferase
    • 11677243 10.1074/jbc.M109060200 1:CAS:528:DC%2BD38XjslCqtw%3D%3D
    • Ju T, Brewer K, D'Souza A, Cummings RD, Canfield WM (2002) Cloning and expression of human core 1 beta1,3-galactosyltransferase. J Biol Chem 277:178-186
    • (2002) J Biol Chem , vol.277 , pp. 178-186
    • Ju, T.1    Brewer, K.2    D'Souza, A.3    Cummings, R.D.4    Canfield, W.M.5
  • 28
    • 0032944499 scopus 로고    scopus 로고
    • Mitotic chromosomal Bcl-2: Stable expression throughout the cell cycle and association with isolated chromosomes
    • 9889250 10.1177/002215549904700203 1:CAS:528:DyaK1MXns1Oksw%3D%3D
    • Schandl CA, Li S, Re GG, Fan W, Willingham MC (1999) Mitotic chromosomal Bcl-2: stable expression throughout the cell cycle and association with isolated chromosomes. J Histochem Cytochem 47:139-149
    • (1999) J Histochem Cytochem , vol.47 , pp. 139-149
    • Schandl, C.A.1    Li, S.2    Re, G.G.3    Fan, W.4    Willingham, M.C.5
  • 29
    • 79958822049 scopus 로고    scopus 로고
    • MTBP plays a crucial role in mitotic progression and chromosome segregation
    • 21274008 10.1038/cdd.2010.189 1:CAS:528:DC%2BC3MXnsVShtLk%3D
    • Agarwal N, Tochigi Y, Adhikari AS, Cui S, Cui Y, Iwakuma T (2011) MTBP plays a crucial role in mitotic progression and chromosome segregation. Cell Death Differ 18:1208-1219
    • (2011) Cell Death Differ , vol.18 , pp. 1208-1219
    • Agarwal, N.1    Tochigi, Y.2    Adhikari, A.S.3    Cui, S.4    Cui, Y.5    Iwakuma, T.6
  • 31
    • 79953153877 scopus 로고    scopus 로고
    • Ursolic acid, a pentacyclin triterpene, potentiates TRAIL-induced apoptosis through p53-independent up-regulation of death receptors: Evidence for the role of reactive oxygen species and JNK
    • 21156789 10.1074/jbc.M110.183699 1:CAS:528:DC%2BC3MXhvVCjs7k%3D
    • Prasad S, Yadav R, Kannappan R, Aggarwal BB (2011) Ursolic acid, a pentacyclin triterpene, potentiates TRAIL-induced apoptosis through p53-independent up-regulation of death receptors: evidence for the role of reactive oxygen species and JNK. J Biol Chem 286:5546-5557
    • (2011) J Biol Chem , vol.286 , pp. 5546-5557
    • Prasad, S.1    Yadav, R.2    Kannappan, R.3    Aggarwal, B.B.4
  • 32
    • 0030897988 scopus 로고    scopus 로고
    • Substrate and inhibitor specificity of interleukin-1β-converting enzyme and related caspases
    • 9054418 10.1074/jbc.272.11.7223 1:CAS:528:DyaK2sXhvFKrurY%3D
    • Margolin N, Raybuck SA, Wilson KP (1997) Substrate and inhibitor specificity of interleukin-1β-converting enzyme and related caspases. J Biol Chem 272:7223-7228
    • (1997) J Biol Chem , vol.272 , pp. 7223-7228
    • Margolin, N.1    Raybuck, S.A.2    Wilson, K.P.3
  • 33
    • 0035073292 scopus 로고    scopus 로고
    • Phosphorylation of Bcl-2 and regulation of apoptosis
    • 11368354 10.1038/sj.leu.2402090 1:CAS:528:DC%2BD3MXjt1egs78%3D
    • Ruvolo PP, Deng X, May W (2001) Phosphorylation of Bcl-2 and regulation of apoptosis. Leukemia 15:515-522
    • (2001) Leukemia , vol.15 , pp. 515-522
    • Ruvolo, P.P.1    Deng, X.2    May, W.3
  • 34
    • 33745017872 scopus 로고    scopus 로고
    • Bcl2's flexible loop domain regulates p53 binding and survival
    • 16738310 10.1128/MCB.01647-05 1:CAS:528:DC%2BD28XlvVeqtb0%3D
    • Deng X, Gao F, Flagg T, Anderson J, May WS (2006) Bcl2's flexible loop domain regulates p53 binding and survival. Mol Cell Biol 26:4421-4434
    • (2006) Mol Cell Biol , vol.26 , pp. 4421-4434
    • Deng, X.1    Gao, F.2    Flagg, T.3    Anderson, J.4    May, W.S.5
  • 35
    • 1342306819 scopus 로고    scopus 로고
    • Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3
    • 14980220 10.1016/S0092-8674(04)00162-X 1:CAS:528:DC%2BD2cXhvVKru70%3D
    • Lin B, Kolluri SK, Lin F, Liu W, Han YH, Cao X, Dawson MI, Reed JC, Zhang XK (2004) Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3. Cell 116:527-540
    • (2004) Cell , vol.116 , pp. 527-540
    • Lin, B.1    Kolluri, S.K.2    Lin, F.3    Liu, W.4    Han, Y.H.5    Cao, X.6    Dawson, M.I.7    Reed, J.C.8    Zhang, X.K.9
  • 36
    • 43549097825 scopus 로고    scopus 로고
    • Bcl-2 associates with the Nur77 family members and exposes its BH3 pro-apoptotic domain during negative selection
    • 18443228 10.1084/jem.20080101 1:CAS:528:DC%2BD1cXlvFWrsrg%3D
    • Thompson J, Winoto A (2008) Bcl-2 associates with the Nur77 family members and exposes its BH3 pro-apoptotic domain during negative selection. J Exp Med 205:1029-1036
    • (2008) J Exp Med , vol.205 , pp. 1029-1036
    • Thompson, J.1    Winoto, A.2
  • 37
    • 0032126465 scopus 로고    scopus 로고
    • Bax protein expression correlates with radiation-induced apoptosis in radiation therapy for cervical carcinoma
    • 9655299 10.1002/(SICI)1097-0142(19980701)83:1<103: AID-CNCR14>3.0.CO;2-0 1:CAS:528:DyaK1cXktlejsbY%3D
    • Ohno T, Nakano T, Niibe Y, Tsujii H, Oka K (1998) Bax protein expression correlates with radiation-induced apoptosis in radiation therapy for cervical carcinoma. Cancer 83:103-110
    • (1998) Cancer , vol.83 , pp. 103-110
    • Ohno, T.1    Nakano, T.2    Niibe, Y.3    Tsujii, H.4    Oka, K.5
  • 38
    • 0033525538 scopus 로고    scopus 로고
    • Long term lithium treatment suppresses p53 and Bax expression but increases Bcl-2 expression
    • 10.1074/jbc.274.10.6039 1:CAS:528:DyaK1MXhs1ensb0%3D
    • Chen RW, Chuang DM (1999) Long term lithium treatment suppresses p53 and Bax expression but increases Bcl-2 expression. J Biol Chem 274:6039-6042
    • (1999) The J Biol Chem , vol.274 , pp. 6039-6042
    • Chen, R.W.1    Chuang, D.M.2
  • 39
    • 33746265824 scopus 로고    scopus 로고
    • Lithium inhibits ceramide- and etoposide-induced protein phosphatase 2A methylation, Bcl-2 dephosphorylation, caspase-2 activation, and apoptosis
    • 16682503 10.1124/mol.106.024059 1:CAS:528:DC%2BD28Xnslyjsrw%3D
    • Chen CL, Lin CF, Chiang CW, Jan MS, Lin YS (2006) Lithium inhibits ceramide- and etoposide-induced protein phosphatase 2A methylation, Bcl-2 dephosphorylation, caspase-2 activation, and apoptosis. Mol Pharmacol 70:510-517
    • (2006) Mol Pharmacol , vol.70 , pp. 510-517
    • Chen, C.L.1    Lin, C.F.2    Chiang, C.W.3    Jan, M.S.4    Lin, Y.S.5
  • 40
    • 0030712040 scopus 로고    scopus 로고
    • Early identification of radiation accident victims for therapy of bone marrow failure
    • 9368314 10.1002/stem.5530150737
    • Dainiak A, Sorba S (1997) Early identification of radiation accident victims for therapy of bone marrow failure. Stem Cells 15:275-285
    • (1997) Stem Cells , vol.15 , pp. 275-285
    • Dainiak, A.1    Sorba, S.2
  • 41
    • 0033499801 scopus 로고    scopus 로고
    • Bcl-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M
    • 10567572 1:CAS:528:DyaK1MXns1yguro%3D
    • Yamamoto K, Ichijo H, Korsmeyer SJ (1999) Bcl-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M. Mol Cell Biol 19:8469-8478
    • (1999) Mol Cell Biol , vol.19 , pp. 8469-8478
    • Yamamoto, K.1    Ichijo, H.2    Korsmeyer, S.J.3


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