메뉴 건너뛰기




Volumn 1644, Issue 2-3, 2004, Pages 115-123

There is more to life and death than mitochondria: Bcl-2 proteins at the endoplasmic reticulum

Author keywords

Bap31; Bax; Bcl 2; Calcium; Endoplasmic reticulum

Indexed keywords

BIM PROTEIN; CALCIUM; CELL PROTEIN; MUTANT PROTEIN; PROTEIN BAD; PROTEIN BAK; PROTEIN BAP31; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL W; PROTEIN BCL XL; PROTEIN BID; PROTEIN BIK; PROTEIN MCL 1; UNCLASSIFIED DRUG;

EID: 1442359853     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2003.07.001     Document Type: Review
Times cited : (61)

References (76)
  • 1
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • Cory S., Adams J.M. The Bcl2 family: regulators of the cellular life-or-death switch. Nat. Rev., Cancer. 2:2002;647-656.
    • (2002) Nat. Rev., Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 2
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai A., Bassik M.C., Walensky L.D., Sorcinelli M.D., Weiler S., Korsmeyer S.J. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cells. 2:2002;183-192.
    • (2002) Cancer Cells , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 4
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of BID, an intracellular amplifier of apoptotic signaling
    • Chou J.J., Li H., Salvesen G.S., Yuan J., Wagner G. Solution structure of BID, an intracellular amplifier of apoptotic signaling. Cell. 96:1999;615-624.
    • (1999) Cell , vol.96 , pp. 615-624
    • Chou, J.J.1    Li, H.2    Salvesen, G.S.3    Yuan, J.4    Wagner, G.5
  • 5
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki M., Youle R.J., Tjandra N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell. 103:2000;645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 8
    • 0344608883 scopus 로고    scopus 로고
    • The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity
    • Hinds M.G., Lackmann M., Skea G.L., Harrison P.J., Huang D.C., Day C.L. The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity. EMBO J. 22:2003;1497-1507.
    • (2003) EMBO J. , vol.22 , pp. 1497-1507
    • Hinds, M.G.1    Lackmann, M.2    Skea, G.L.3    Harrison, P.J.4    Huang, D.C.5    Day, C.L.6
  • 9
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher S., Martinou J.C. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10:2000;369-377.
    • (2000) Trends Cell Biol. , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 10
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the Bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski S., Tanaka S., Takayama S., Schibler M.J., Fenton W., Reed J.C. Investigation of the subcellular distribution of the Bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res. 53:1993;4701-4714.
    • (1993) Cancer Res. , vol.53 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 11
    • 0027401769 scopus 로고
    • A class of membrane proteins with a C-terminal anchor
    • Kutay U., Hartmann E., Rapoport T.A. A class of membrane proteins with a C-terminal anchor. Trends Cell Biol. 3:1993;72-75.
    • (1993) Trends Cell Biol. , vol.3 , pp. 72-75
    • Kutay, U.1    Hartmann, E.2    Rapoport, T.A.3
  • 12
    • 0030798914 scopus 로고    scopus 로고
    • Evidence for multiple mechanisms for membrane binding and integration via carboxyl-terminal insertion sequences
    • Kim P.K., Janiak-Spens F., Trimble W.S., Leber B., Andrews D.W. Evidence for multiple mechanisms for membrane binding and integration via carboxyl-terminal insertion sequences. Biochemistry. 36:1997;8873-8882.
    • (1997) Biochemistry , vol.36 , pp. 8873-8882
    • Kim, P.K.1    Janiak-Spens, F.2    Trimble, W.S.3    Leber, B.4    Andrews, D.W.5
  • 13
    • 0029760303 scopus 로고    scopus 로고
    • Bcl-2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types
    • Zhu W., Cowie A., Wasfy G.W., Penn L.Z., Leber B., Andrews D.W. Bcl-2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types. EMBO J. 15:1996;4130-4141.
    • (1996) EMBO J. , vol.15 , pp. 4130-4141
    • Zhu, W.1    Cowie, A.2    Wasfy, G.W.3    Penn, L.Z.4    Leber, B.5    Andrews, D.W.6
  • 14
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X., Kim C.N., Yang J., Jemmerson R., Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell. 86:1996;147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 15
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria. Releasing power for life and unleashing the machineries of death
    • Newmeyer D.D., Ferguson-Miller S. Mitochondria. Releasing power for life and unleashing the machineries of death. Cell. 112:2003;481-490.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 16
    • 0027523461 scopus 로고
    • Apoptosis induced by withdrawal of interleukin-3 (IL-3) from an IL-3-dependent hematopoietic cell line is associated with repartitioning of intracellular calcium and is blocked by enforced Bcl-2 oncoprotein production
    • Baffy G., Miyashita T., Williamson J.R., Reed J.C. Apoptosis induced by withdrawal of interleukin-3 (IL-3) from an IL-3-dependent hematopoietic cell line is associated with repartitioning of intracellular calcium and is blocked by enforced Bcl-2 oncoprotein production. J. Biol. Chem. 268:1993;6511-6519.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6511-6519
    • Baffy, G.1    Miyashita, T.2    Williamson, J.R.3    Reed, J.C.4
  • 17
    • 0032532213 scopus 로고    scopus 로고
    • Modulation of endoplasmic reticulum calcium pump by Bcl-2
    • Kuo T.H., Kim H.R., Zhu L., Yu Y., Lin H.M., Tsang W. Modulation of endoplasmic reticulum calcium pump by Bcl-2. Oncogene. 17:1998;1903-1910.
    • (1998) Oncogene , vol.17 , pp. 1903-1910
    • Kuo, T.H.1    Kim, H.R.2    Zhu, L.3    Yu, Y.4    Lin, H.M.5    Tsang, W.6
  • 18
    • 0030824575 scopus 로고    scopus 로고
    • Maintenance of calcium homeostasis in the endoplasmic reticulum by Bcl-2
    • He H., Lam M., McCormick T.S., Distelhorst C.W. Maintenance of calcium homeostasis in the endoplasmic reticulum by Bcl-2. J. Cell Biol. 138:1997;1219-1228.
    • (1997) J. Cell Biol. , vol.138 , pp. 1219-1228
    • He, H.1    Lam, M.2    McCormick, T.S.3    Distelhorst, C.W.4
  • 19
    • 0034665043 scopus 로고    scopus 로고
    • Effects of PMCA and SERCA pump overexpression on the kinetics of cell Ca(2+) signalling
    • Brini M., Bano D., Manni S., Rizzuto R., Carafoli E. Effects of PMCA and SERCA pump overexpression on the kinetics of cell Ca(2+) signalling. EMBO J. 19:2000;4926-4935.
    • (2000) EMBO J. , vol.19 , pp. 4926-4935
    • Brini, M.1    Bano, D.2    Manni, S.3    Rizzuto, R.4    Carafoli, E.5
  • 20
    • 0034610995 scopus 로고    scopus 로고
    • Reduced loading of intracellular Ca(2+) stores and downregulation of capacitative Ca(2+) influx in Bcl-2-overexpressing cells
    • Pinton P., Ferrari D., Magalhaes P., Schulze-Osthoff K., Di Virgilio F., Pozzan T., Rizzuto R. Reduced loading of intracellular Ca(2+) stores and downregulation of capacitative Ca(2+) influx in Bcl-2-overexpressing cells. J. Cell Biol. 148:2000;857-862.
    • (2000) J. Cell Biol. , vol.148 , pp. 857-862
    • Pinton, P.1    Ferrari, D.2    Magalhaes, P.3    Schulze-Osthoff, K.4    Di Virgilio, F.5    Pozzan, T.6    Rizzuto, R.7
  • 27
    • 0035941360 scopus 로고    scopus 로고
    • Transient expression of wild-type or mitochondrially targeted Bcl-2 induces apoptosis, whereas transient expression of endoplasmic reticulum-targeted Bcl-2 is protective against Bax-induced cell death
    • Wang N.S., Unkila M.T., Reineks E.Z., Distelhorst C.W. Transient expression of wild-type or mitochondrially targeted Bcl-2 induces apoptosis, whereas transient expression of endoplasmic reticulum-targeted Bcl-2 is protective against Bax-induced cell death. J. Biol. Chem. 276:2001;44117-44128.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44117-44128
    • Wang, N.S.1    Unkila, M.T.2    Reineks, E.Z.3    Distelhorst, C.W.4
  • 28
    • 0026475219 scopus 로고
    • Stable expression of the calbindin-D28K complementary DNA interferes with the apoptotic pathway in lymphocytes
    • Dowd D.R., MacDonald P.N., Komm B.S., Haussler M.R., Miesfeld R.L. Stable expression of the calbindin-D28K complementary DNA interferes with the apoptotic pathway in lymphocytes. Mol. Endocrinol. 6:1992;1843-1848.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 1843-1848
    • Dowd, D.R.1    MacDonald, P.N.2    Komm, B.S.3    Haussler, M.R.4    Miesfeld, R.L.5
  • 29
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa T., Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J. Cell Biol. 150:2000;887-894.
    • (2000) J. Cell Biol. , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 30
    • 0034604033 scopus 로고    scopus 로고
    • Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2
    • Hacki J., Egger L., Monney L., Conus S., Rosse T., Fellay I., Borner C. Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2. Oncogene. 19:2000;2286-2295.
    • (2000) Oncogene , vol.19 , pp. 2286-2295
    • Hacki, J.1    Egger, L.2    Monney, L.3    Conus, S.4    Rosse, T.5    Fellay, I.6    Borner, C.7
  • 31
    • 0035848736 scopus 로고    scopus 로고
    • Endoplasmic reticulum localized Bcl-2 prevents apoptosis when redistribution of cytochrome c is a late event
    • Annis M.G., Zamzami N., Zhu W., Penn L.Z., Kroemer G., Leber B., Andrews D.W. Endoplasmic reticulum localized Bcl-2 prevents apoptosis when redistribution of cytochrome c is a late event. Oncogene. 20:2001;1939-1952.
    • (2001) Oncogene , vol.20 , pp. 1939-1952
    • Annis, M.G.1    Zamzami, N.2    Zhu, W.3    Penn, L.Z.4    Kroemer, G.5    Leber, B.6    Andrews, D.W.7
  • 32
    • 0035355341 scopus 로고    scopus 로고
    • 2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: Significance for the molecular mechanism of Bcl-2 action
    • 2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: significance for the molecular mechanism of Bcl-2 action. EMBO J. 20:2001;2690-2701.
    • (2001) EMBO J. , vol.20 , pp. 2690-2701
    • Pinton, P.1    Ferrari, D.2    Rapizzi, E.3    Di Virgilio, F.D.4    Pozzan, T.5    Rizzuto, R.6
  • 39
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A., Smith C.L., Hsu Y.T., Youle R.J. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J. 18:1999;2330-2341.
    • (1999) EMBO J. , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4
  • 41
    • 0013148718 scopus 로고    scopus 로고
    • Uncleaved BAP31 in association with A4 protein at the endoplasmic reticulum is an inhibitor of Fas-initiated release of cytochrome c from mitochondria
    • Wang B., Nguyen M., Breckenridge D.G., Stojanovic M., Clemons P.A., Kuppig S., Shore G.C. Uncleaved BAP31 in association with A4 protein at the endoplasmic reticulum is an inhibitor of Fas-initiated release of cytochrome c from mitochondria. J. Biol. Chem. 278:2003;14461-14468.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14461-14468
    • Wang, B.1    Nguyen, M.2    Breckenridge, D.G.3    Stojanovic, M.4    Clemons, P.A.5    Kuppig, S.6    Shore, G.C.7
  • 43
    • 0037070160 scopus 로고    scopus 로고
    • Involvement of the N-terminus of Bax in its intracellular localization and function
    • Cartron P.F., Moreau C., Oliver L., Mayat E., Meflah K., Vallette F.M. Involvement of the N-terminus of Bax in its intracellular localization and function. FEBS Lett. 512:2002;95-100.
    • (2002) FEBS Lett. , vol.512 , pp. 95-100
    • Cartron, P.F.1    Moreau, C.2    Oliver, L.3    Mayat, E.4    Meflah, K.5    Vallette, F.M.6
  • 46
    • 0037458540 scopus 로고    scopus 로고
    • Bcl-2 on the endoplasmic reticulum regulates bax activity by binding to BH3-only proteins
    • Thomenius M.J., Wang N.S., Reineks E.Z., Wang Z., Distelhorst C.W. Bcl-2 on the endoplasmic reticulum regulates bax activity by binding to BH3-only proteins. J. Biol. Chem. 278:2003;6243-6250.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6243-6250
    • Thomenius, M.J.1    Wang, N.S.2    Reineks, E.Z.3    Wang, Z.4    Distelhorst, C.W.5
  • 47
    • 0032802315 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-X(L) block thapsigargin-induced nitric oxide generation, c-Jun NH(2)-terminal kinase activity, and apoptosis
    • Srivastava R.K., Sollott S.J., Khan L., Hansford R., Lakatta E.G., Longo D.L. Bcl-2 and Bcl-X(L) block thapsigargin-induced nitric oxide generation, c-Jun NH(2)-terminal kinase activity, and apoptosis. Mol. Cell. Biol. 19:1999;5659-5674.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5659-5674
    • Srivastava, R.K.1    Sollott, S.J.2    Khan, L.3    Hansford, R.4    Lakatta, E.G.5    Longo, D.L.6
  • 48
  • 49
    • 0037007141 scopus 로고    scopus 로고
    • The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum
    • Breckenridge D.G., Nguyen M., Kuppig S., Reth M., Shore G.C. The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 99:2002;4331-4336.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4331-4336
    • Breckenridge, D.G.1    Nguyen, M.2    Kuppig, S.3    Reth, M.4    Shore, G.C.5
  • 50
    • 0033816610 scopus 로고    scopus 로고
    • Caspase-resistant BAP31 inhibits fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria
    • Nguyen M., Breckenridge D.G., Ducret A., Shore G.C. Caspase-resistant BAP31 inhibits fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria. Mol. Cell. Biol. 20:2000;6731-6740.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6731-6740
    • Nguyen, M.1    Breckenridge, D.G.2    Ducret, A.3    Shore, G.C.4
  • 51
    • 0037240794 scopus 로고    scopus 로고
    • The resident endoplasmic reticulum protein, BAP31, associates with gamma-actin and myosin B heavy chain
    • Ducret A., Nguyen M., Breckenridge D.G., Shore G.C. The resident endoplasmic reticulum protein, BAP31, associates with gamma-actin and myosin B heavy chain. Eur. J. Biochem. 270:2003;342-349.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 342-349
    • Ducret, A.1    Nguyen, M.2    Breckenridge, D.G.3    Shore, G.C.4
  • 52
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • Breckenridge D.G., Stojanovic M., Marcellus R.C., Shore G.C. Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. J. Cell Biol. 160:2003;1115-1127.
    • (2003) J. Cell Biol. , vol.160 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 53
    • 0037390872 scopus 로고    scopus 로고
    • Spike, a novel BH3-only protein, regulates apoptosis at the endoplasmic reticulum
    • Mund T., Gewies A., Schoenfeld N., Bauer M.K., Grimm S. Spike, a novel BH3-only protein, regulates apoptosis at the endoplasmic reticulum. FASEB J. 17:2003;696-698.
    • (2003) FASEB J. , vol.17 , pp. 696-698
    • Mund, T.1    Gewies, A.2    Schoenfeld, N.3    Bauer, M.K.4    Grimm, S.5
  • 54
    • 0030979773 scopus 로고    scopus 로고
    • Double identity for proteins of the Bcl-2 family
    • Reed J.C. Double identity for proteins of the Bcl-2 family. Nature. 19(387):1997;773-776.
    • (1997) Nature , vol.19 , Issue.387 , pp. 773-776
    • Reed, J.C.1
  • 55
    • 0037124113 scopus 로고    scopus 로고
    • BH-3-only BIK functions at the endoplasmic reticulum to stimulate cytochrome c release from mitochondria
    • Germain M., Mathai J.P., Shore G.C. BH-3-only BIK functions at the endoplasmic reticulum to stimulate cytochrome c release from mitochondria. J. Biol. Chem. 277:2002;18053-18060.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18053-18060
    • Germain, M.1    Mathai, J.P.2    Shore, G.C.3
  • 57
    • 0034737646 scopus 로고    scopus 로고
    • Caspase-8-mediated intracellular acidification precedes mitochondrial dysfunction in somatostatin-induced apoptosis
    • Liu D., Martino G., Thangaraju M., Sharma M., Halwani F., Shen S.H., Patel Y.C., Srikant C.B. Caspase-8-mediated intracellular acidification precedes mitochondrial dysfunction in somatostatin-induced apoptosis. J. Biol. Chem. 275:2000;9244-9250.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9244-9250
    • Liu, D.1    Martino, G.2    Thangaraju, M.3    Sharma, M.4    Halwani, F.5    Shen, S.H.6    Patel, Y.C.7    Srikant, C.B.8
  • 58
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the mammalian unfolded protein response
    • Harding H.P., Calfon M., Urano F., Novoa I., Ron D. Transcriptional and translational control in the mammalian unfolded protein response. Annu. Rev. Cell Dev. Biol. 18:2002;575-599.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 59
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu C.E., Walter P. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15:1996;3028-3039.
    • (1996) EMBO J. , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 60
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano F., Wang X., Bertolotti A., Zhang Y., Chung P., Harding H.P., Ron D. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science. 287:2000;664-666.
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 61
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control
    • Shi Y., Vattem K.M., Sood R., An J., Liang J., Stramm L., Wek R.C. Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. Mol. Cell. Biol. 18:1998;7499-7509.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7499-7509
    • Shi, Y.1    Vattem, K.M.2    Sood, R.3    An, J.4    Liang, J.5    Stramm, L.6    Wek, R.C.7
  • 62
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath H., Huang D.C., O'Reilly L.A., King S.M., Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol. Cell. 3:1999;287-296.
    • (1999) Mol. Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 63
    • 0035823238 scopus 로고    scopus 로고
    • Bmf: A proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis
    • Puthalakath H., Villunger A., O'Reilly L.A., Beaumont J.G., Coultas L., Cheney R.E., Huang D.C., Strasser A. Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Science. 293:2001;1829-1832.
    • (2001) Science , vol.293 , pp. 1829-1832
    • Puthalakath, H.1    Villunger, A.2    O'Reilly, L.A.3    Beaumont, J.G.4    Coultas, L.5    Cheney, R.E.6    Huang, D.C.7    Strasser, A.8
  • 64
    • 0037418238 scopus 로고    scopus 로고
    • JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis
    • Lei K., Davis R.J. JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis. Proc. Natl. Acad. Sci. U. S. A. 100:2003;2432-2437.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2432-2437
    • Lei, K.1    Davis, R.J.2
  • 65
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J., Harada H., Yang E., Jockel J., Korsmeyer S.J. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell. 87:1996;619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 66
    • 0037742249 scopus 로고    scopus 로고
    • Inhibition of PI-3 kinase sensitizes vascular endothelial cells to cytokine-initiated cathepsin-dependent apoptosis
    • Madge L.A., Li J.H., Choi J., Pober J.S. Inhibition of PI-3 kinase sensitizes vascular endothelial cells to cytokine-initiated cathepsin-dependent apoptosis. J. Biol. Chem. 278:2003;21296-21306.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21296-21306
    • Madge, L.A.1    Li, J.H.2    Choi, J.3    Pober, J.S.4
  • 67
    • 0035861890 scopus 로고    scopus 로고
    • Bcl-2 phosphorylation is required for inhibition of oxidative stress-induced lysosomal leak and ensuing apoptosis
    • Zhao M., Eaton J.W., Brunk U.T. Bcl-2 phosphorylation is required for inhibition of oxidative stress-induced lysosomal leak and ensuing apoptosis. FEBS Lett. 509:2001;405-412.
    • (2001) FEBS Lett. , vol.509 , pp. 405-412
    • Zhao, M.1    Eaton, J.W.2    Brunk, U.T.3
  • 68
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri K.F., Kroemer G. Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3:2001;E255-E263.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 255-E263
    • Ferri, K.F.1    Kroemer, G.2
  • 71
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • Hsu Y.T., Youle R.J. Nonionic detergents induce dimerization among members of the Bcl-2 family. J. Biol. Chem. 272:1997;13829-13834.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13829-13834
    • Hsu, Y.T.1    Youle, R.J.2
  • 73
    • 0028965578 scopus 로고
    • The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2
    • Yang T., Kozopas K.M., Craig R.W. The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2. J. Cell Biol. 128:1995;1173-1184.
    • (1995) J. Cell Biol. , vol.128 , pp. 1173-1184
    • Yang, T.1    Kozopas, K.M.2    Craig, R.W.3
  • 74
    • 0033521537 scopus 로고    scopus 로고
    • Boo, a novel negative regulator of cell death, interacts with Apaf-1
    • Song Q., Kuang Y., Dixit V.M., Vincenz C. Boo, a novel negative regulator of cell death, interacts with Apaf-1. EMBO J. 18:1999;167-178.
    • (1999) EMBO J. , vol.18 , pp. 167-178
    • Song, Q.1    Kuang, Y.2    Dixit, V.M.3    Vincenz, C.4
  • 75
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J., Harada H., Yang E., Jockel J., Korsmeyer S.J. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell. 87:1996;619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.