메뉴 건너뛰기




Volumn 3, Issue 10, 2012, Pages 790-801

Human Bop is a novel BH3-only member of the Bcl-2 protein family

Author keywords

apoptosis; BH3 domain; Bop

Indexed keywords

BCL2 RELATED PROTEIN A1; BH3 PROTEIN; CYTOCHROME C; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL W; PROTEIN BCL XL; PROTEIN MCL 1; VINCRISTINE; VOLTAGE DEPENDENT ANION CHANNEL 1; BOP PROTEIN, HUMAN;

EID: 84878042396     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-012-2069-7     Document Type: Article
Times cited : (6)

References (44)
  • 1
    • 4444380912 scopus 로고    scopus 로고
    • Bax increases the pore size of rat brain mitochondrial voltage-dependent anion channel in the presence of tBid
    • Banerjee, J., and Ghosh, S. (2004). Bax increases the pore size of rat brain mitochondrial voltage-dependent anion channel in the presence of tBid. Biochem Biophys Res Commun 323, 310-314.
    • (2004) Biochem Biophys Res Commun , vol.323 , pp. 310-314
    • Banerjee, J.1    Ghosh, S.2
  • 2
    • 19944432123 scopus 로고    scopus 로고
    • Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function
    • Chen, L., Willis, S. N., Wei, A., Smith, B. J., Fletcher, J. I., Hinds, M. G., Colman, P. M., Day, C. L., Adams, J. M., and Huang, D. C. (2005). Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. Mol Cell 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    Colman, P.M.7    Day, C.L.8    Adams, J.M.9    Huang, D.C.10
  • 4
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: regulators of the cellular life-or-death switch
    • Cory, S., and Adams, J. M. (2002). The Bcl2 family: regulators of the cellular life-or-death switch. Nat Rev Cancer 2, 647-656.
    • (2002) Nat Rev Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 5
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton, M. (1999). The mitochondrial permeability transition pore and its role in cell death. Biochem J 341(Pt 2), 233-249.
    • (1999) Biochem J , vol.341 , Issue.Pt2 , pp. 233-249
    • Crompton, M.1
  • 6
    • 0036479049 scopus 로고    scopus 로고
    • Mitochondrial intermembrane junctional complexes and their involvement in cell death
    • Crompton, M., Barksby, E., Johnson, N., and Capano, M. (2002). Mitochondrial intermembrane junctional complexes and their involvement in cell death. Biochimie 84, 143-152.
    • (2002) Biochimie , vol.84 , pp. 143-152
    • Crompton, M.1    Barksby, E.2    Johnson, N.3    Capano, M.4
  • 7
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • Danial, N. N., and Korsmeyer, S. J. (2004). Cell death: critical control points. Cell 116, 205-219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 8
    • 68149154728 scopus 로고    scopus 로고
    • BH3-only proteins and their roles in programmed cell death
    • Giam, M., Huang, D. C., and Bouillet, P. (2008). BH3-only proteins and their roles in programmed cell death. Oncogene 27Suppl 1, S128-136.
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 1
    • Giam, M.1    Huang, D.C.2    Bouillet, P.3
  • 9
  • 10
    • 84861386162 scopus 로고    scopus 로고
    • BH3-only proteins in apoptosis at a glance
    • Happo, L., Strasser, A., and Cory, S. (2012). BH3-only proteins in apoptosis at a glance. J Cell Sci 125, 1081-1087.
    • (2012) J Cell Sci , vol.125 , pp. 1081-1087
    • Happo, L.1    Strasser, A.2    Cory, S.3
  • 11
    • 27944497377 scopus 로고    scopus 로고
    • Regulation of apoptosis: uncovering the binding determinants
    • Hinds, M. G., and Day, C. L. (2005). Regulation of apoptosis: uncovering the binding determinants. Curr Opin Struct Biol 15, 690-699.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 690-699
    • Hinds, M.G.1    Day, C.L.2
  • 12
    • 0033635733 scopus 로고    scopus 로고
    • BH3-Only proteins-essential initiators of apoptotic cell death
    • Huang, D. C., and Strasser, A. (2000). BH3-Only proteins-essential initiators of apoptotic cell death. Cell 103, 839-842.
    • (2000) Cell , vol.103 , pp. 839-842
    • Huang, D.C.1    Strasser, A.2
  • 13
    • 3943071150 scopus 로고    scopus 로고
    • Cytochrome C-mediated apoptosis
    • Jiang, X., and Wang, X. (2004). Cytochrome C-mediated apoptosis. Annu Rev Biochem 73, 87-106.
    • (2004) Annu Rev Biochem , vol.73 , pp. 87-106
    • Jiang, X.1    Wang, X.2
  • 14
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. (1999). Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 292, 195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 15
    • 0032146987 scopus 로고    scopus 로고
    • Bcl-2-family proteins: the role of the BH3 domain in apoptosis
    • Kelekar, A., and Thompson, C. B. (1998). Bcl-2-family proteins: the role of the BH3 domain in apoptosis. Trends Cell Biol 8, 324-330.
    • (1998) Trends Cell Biol , vol.8 , pp. 324-330
    • Kelekar, A.1    Thompson, C.B.2
  • 17
    • 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, J. E., Bonzon, C., Sullivan, B. A., Green, D. R., and Newmeyer, D. D. (2005). BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Mol Cell 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    Newmeyer, D.D.7
  • 18
    • 79952112980 scopus 로고    scopus 로고
    • Drugs targeting Bcl-2 family members as an emerging strategy in cancer
    • Leber, B., Geng, F., Kale, J., and Andrews, D. W. (2010). Drugs targeting Bcl-2 family members as an emerging strategy in cancer. Expert Rev Mol Med 12, e28.
    • (2010) Expert Rev Mol Med , vol.12
    • Leber, B.1    Geng, F.2    Kale, J.3    Andrews, D.W.4
  • 19
    • 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., and Korsmeyer, S. J. (2002). Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2, 183-192.
    • (2002) Cancer Cell , 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
  • 20
    • 84864643231 scopus 로고    scopus 로고
    • Activation of ERK-p53 and ERK-mediated phosphorylation of Bcl-2 are involved in autophagic cell death induced by the c-Met inhibitor SU11274 in human lung cancer A549 cells
    • Liu, Y., Yang, Y., Ye, Y. C., Shi, Q. F., Chai, K., Tashiro, S., Onodera, S., and Ikejima, T. (2012). Activation of ERK-p53 and ERK-mediated phosphorylation of Bcl-2 are involved in autophagic cell death induced by the c-Met inhibitor SU11274 in human lung cancer A549 cells. J Pharmacol Sci 118, 423-432.
    • (2012) J Pharmacol Sci , vol.118 , pp. 423-432
    • Liu, Y.1    Yang, Y.2    Ye, Y.C.3    Shi, Q.F.4    Chai, K.5    Tashiro, S.6    Onodera, S.7    Ikejima, T.8
  • 21
    • 68249106060 scopus 로고    scopus 로고
    • BH3-only proteins in apoptosis and beyond: an overview
    • Lomonosova, E., and Chinnadurai, G. (2008). BH3-only proteins in apoptosis and beyond: an overview. Oncogene 27Suppl 1, S2-19.
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 1 , pp. 2-19
    • Lomonosova, E.1    Chinnadurai, G.2
  • 22
    • 33751544565 scopus 로고    scopus 로고
    • The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site
    • Moldoveanu, T., Liu, Q., Tocilj, A., Watson, M., Shore, G., and Gehring, K. (2006). The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site. Mol Cell 24, 677-688.
    • (2006) Mol Cell , vol.24 , pp. 677-688
    • Moldoveanu, T.1    Liu, Q.2    Tocilj, A.3    Watson, M.4    Shore, G.5    Gehring, K.6
  • 23
    • 1442310957 scopus 로고    scopus 로고
    • Structural biology of the Bcl-2 family of proteins
    • Petros, A. M., Olejniczak, E. T., and Fesik, S. W. (2004). Structural biology of the Bcl-2 family of proteins. Biochim Biophys Acta 1644, 83-94.
    • (2004) Biochim Biophys Acta , vol.1644 , pp. 83-94
    • Petros, A.M.1    Olejniczak, E.T.2    Fesik, S.W.3
  • 24
    • 0033534594 scopus 로고    scopus 로고
    • Interleukin-3 induces the phosphorylation of a distinct fraction of bcl-2
    • Poommipanit, P. B., Chen, B., and Oltvai, Z. N. (1999). Interleukin-3 induces the phosphorylation of a distinct fraction of bcl-2. J Biol Chem 274, 1033-1039.
    • (1999) J Biol Chem , vol.274 , pp. 1033-1039
    • Poommipanit, P.B.1    Chen, B.2    Oltvai, Z.N.3
  • 26
    • 0037904834 scopus 로고    scopus 로고
    • Identification of the protein-protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins
    • Shi, Y., Chen, J., Weng, C., Chen, R., Zheng, Y., Chen, Q., and Tang, H. (2003). Identification of the protein-protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins. Biochem Biophys Res Commun 305, 989-996.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 989-996
    • Shi, Y.1    Chen, J.2    Weng, C.3    Chen, R.4    Zheng, Y.5    Chen, Q.6    Tang, H.7
  • 27
    • 0034697365 scopus 로고    scopus 로고
    • Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c
    • Shimizu, S., Ide, T., Yanagida, T., and Tsujimoto, Y. (2000). Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c. J Biol Chem 275, 12321-12325.
    • (2000) J Biol Chem , vol.275 , pp. 12321-12325
    • Shimizu, S.1    Ide, T.2    Yanagida, T.3    Tsujimoto, Y.4
  • 28
    • 0035931765 scopus 로고    scopus 로고
    • Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells
    • Shimizu, S., Matsuoka, Y., Shinohara, Y., Yoneda, Y., and Tsujimoto, Y. (2001). Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells. J Cell Biol 152, 237-250.
    • (2001) J Cell Biol , vol.152 , pp. 237-250
    • Shimizu, S.1    Matsuoka, Y.2    Shinohara, Y.3    Yoneda, Y.4    Tsujimoto, Y.5
  • 29
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu, S., Narita, M., and Tsujimoto, Y. (1999). Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399, 483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 30
    • 0031813790 scopus 로고    scopus 로고
    • Involvement of microtubules in the regulation of Bcl2 phosphorylation and apoptosis through cyclic AMP-dependent protein kinase
    • Srivastava, R. K., Srivastava, A. R., Korsmeyer, S. J., Nesterova, M., Cho-Chung, Y. S., and Longo, D. L. (1998). Involvement of microtubules in the regulation of Bcl2 phosphorylation and apoptosis through cyclic AMP-dependent protein kinase. Mol Cell Biol 18, 3509-3517.
    • (1998) Mol Cell Biol , vol.18 , pp. 3509-3517
    • Srivastava, R.K.1    Srivastava, A.R.2    Korsmeyer, S.J.3    Nesterova, M.4    Cho-Chung, Y.S.5    Longo, D.L.6
  • 32
    • 0037173741 scopus 로고    scopus 로고
    • Activation of mitochondrial voltage-dependent anion channel by apro-apoptotic BH3-only protein Bim
    • Sugiyama, T., Shimizu, S., Matsuoka, Y., Yoneda, Y., and Tsujimoto, Y. (2002). Activation of mitochondrial voltage-dependent anion channel by apro-apoptotic BH3-only protein Bim. Oncogene 21, 4944-4956.
    • (2002) Oncogene , vol.21 , pp. 4944-4956
    • Sugiyama, T.1    Shimizu, S.2    Matsuoka, Y.3    Yoneda, Y.4    Tsujimoto, Y.5
  • 33
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: coregulation of dimer formation and intracellular localization
    • Suzuki, M., Youle, R. J., and 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
  • 34
    • 0022429789 scopus 로고
    • The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA
    • Taylor, J. W., Ott, J., and Eckstein, F. (1985). The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA. Nucleic Acids Res 13, 8765-8785.
    • (1985) Nucleic Acids Res , vol.13 , pp. 8765-8785
    • Taylor, J.W.1    Ott, J.2    Eckstein, F.3
  • 35
    • 0036479011 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: an essential player in apoptosis
    • Tsujimoto, Y., and Shimizu, S. (2002). The voltage-dependent anion channel: an essential player in apoptosis. Biochimie 84, 187-193.
    • (2002) Biochimie , vol.84 , pp. 187-193
    • Tsujimoto, Y.1    Shimizu, S.2
  • 36
    • 32644473650 scopus 로고    scopus 로고
    • How the Bcl-2 family of proteins interact to regulate apoptosis
    • van Delft, M. F., and Huang, D. C. (2006). How the Bcl-2 family of proteins interact to regulate apoptosis. Cell Res 16, 203-213.
    • (2006) Cell Res , vol.16 , pp. 203-213
    • van Delft, M.F.1    Huang, D.C.2
  • 37
    • 77958128601 scopus 로고    scopus 로고
    • BH3-only proteins and their effects on cancer
    • Vo, T. T., and Letai, A. (2010). BH3-only proteins and their effects on cancer. Adv Exp Med Biol 687, 49-63.
    • (2010) Adv Exp Med Biol , vol.687 , pp. 49-63
    • Vo, T.T.1    Letai, A.2
  • 38
    • 15444373128 scopus 로고    scopus 로고
    • Specific cleavage of Mcl-1 by caspase-3 in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in Jurkat leukemia T cells
    • Weng, C., Li, Y., Xu, D., Shi, Y., and Tang, H. (2005). Specific cleavage of Mcl-1 by caspase-3 in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in Jurkat leukemia T cells. J Biol Chem 280, 10491-10500.
    • (2005) J Biol Chem , vol.280 , pp. 10491-10500
    • Weng, C.1    Li, Y.2    Xu, D.3    Shi, Y.4    Tang, H.5
  • 39
    • 27544446991 scopus 로고    scopus 로고
    • Life in the balance: how BH3-only proteins induce apoptosis
    • Willis, S. N., and Adams, J. M. (2005). Life in the balance: how BH3-only proteins induce apoptosis. Curr Opin Cell Biol 17, 617-625.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 617-625
    • Willis, S.N.1    Adams, J.M.2
  • 40
    • 22244464818 scopus 로고    scopus 로고
    • Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins
    • Willis, S. N., Chen, L., Dewson, G., Wei, A., Naik, E., Fletcher, J. I., Adams, J. M., and Huang, D. C. (2005). Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev 19, 1294-1305.
    • (2005) Genes Dev , vol.19 , pp. 1294-1305
    • Willis, S.N.1    Chen, L.2    Dewson, G.3    Wei, A.4    Naik, E.5    Fletcher, J.I.6    Adams, J.M.7    Huang, D.C.8
  • 41
    • 48849090371 scopus 로고    scopus 로고
    • Bcl-2 family proteins: the sentinels of the mitochondrial apoptosis pathway
    • Wong, W. W., and Puthalakath, H. (2008). Bcl-2 family proteins: the sentinels of the mitochondrial apoptosis pathway. IUBMB Life 60, 390-397.
    • (2008) IUBMB Life , vol.60 , pp. 390-397
    • Wong, W.W.1    Puthalakath, H.2
  • 42
    • 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
    • Yamamoto, K., Ichijo, H., and Korsmeyer, S. J. (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
  • 43
    • 1442327526 scopus 로고    scopus 로고
    • Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide
    • Zheng, Y., Shi, Y., Tian, C., Jiang, C., Jin, H., Chen, J., Almasan, A., Tang, H., and Chen, Q. (2004). Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide. Oncogene 23, 1239-1247.
    • (2004) Oncogene , vol.23 , pp. 1239-1247
    • Zheng, Y.1    Shi, Y.2    Tian, C.3    Jiang, C.4    Jin, H.5    Chen, J.6    Almasan, A.7    Tang, H.8    Chen, Q.9
  • 44
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong, W. X., Lindsten, T., Ross, A. J., MacGregor, G. R., and Thompson, C. B. (2001). BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev 15, 1481-1486.
    • (2001) Genes Dev , vol.15 , pp. 1481-1486
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.