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Volumn 166, Issue 1, 2009, Pages 32-37

Novel dimerization mode of the human Bcl-2 family protein Bak, a mitochondrial apoptosis regulator

Author keywords

Apoptosis regulator; Bak; Bcl 2 family protein; Crystal structure; Disulfide bridge; Homodimer

Indexed keywords

ASPARAGINE; CYSTEINE; PROTEIN BAK; SERINE;

EID: 60649103344     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2008.12.003     Document Type: Article
Times cited : (44)

References (40)
  • 1
    • 33847328289 scopus 로고    scopus 로고
    • The Bcl-2 apoptotic switch in cancer development and therapy
    • Adams J.M., and Cory S. The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 26 (2007) 1324-1337
    • (2007) Oncogene , vol.26 , pp. 1324-1337
    • Adams, J.M.1    Cory, S.2
  • 4
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: regulators of the cellular life-or-death switch
    • Cory S., and 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
  • 6
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • Danial N.N., and Korsmeyer S.J. Cell death: critical control points. Cell 116 (2004) 205-219
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 8
    • 32644473650 scopus 로고    scopus 로고
    • How the Bcl-2 family of proteins interact to regulate apoptosis
    • Delft M.F., and Huang D.C.S. How the Bcl-2 family of proteins interact to regulate apoptosis. Cell Res. 16 (2006) 203-213
    • (2006) Cell Res. , vol.16 , pp. 203-213
    • Delft, M.F.1    Huang, D.C.S.2
  • 9
    • 43049105074 scopus 로고    scopus 로고
    • To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3: groove interactions
    • Dewson G., Kratina T., Sim H., Puthalakath H., Adams J.M., Colman P.M., and Kluck R.M. To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3: groove interactions. Mol. Cell 30 (2008) 369-380
    • (2008) Mol. Cell , vol.30 , pp. 369-380
    • Dewson, G.1    Kratina, T.2    Sim, H.3    Puthalakath, H.4    Adams, J.M.5    Colman, P.M.6    Kluck, R.M.7
  • 10
    • 34547629939 scopus 로고    scopus 로고
    • A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax
    • George N.M., Evans J.J.D., and Luo X. A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax. Genes Dev. 21 (2007) 1937-1948
    • (2007) Genes Dev. , vol.21 , pp. 1937-1948
    • George, N.M.1    Evans, J.J.D.2    Luo, X.3
  • 11
    • 20444430478 scopus 로고    scopus 로고
    • Apoptotic pathways: ten minutes to dead
    • Green D.R. Apoptotic pathways: ten minutes to dead. Cell 121 (2005) 671-674
    • (2005) Cell , vol.121 , pp. 671-674
    • Green, D.R.1
  • 12
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L., and Park J. DaliLite workbench for protein structure comparison. Bioinformatics 16 (2000) 566-567
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 13
    • 0029109468 scopus 로고
    • Protein-protein interactions: a review of protein dimer structures
    • Jones S., and Thornton J.M. Protein-protein interactions: a review of protein dimer structures. Prog. Biophys. Mol. Biol. 63 (1995) 31-65
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 14
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard J. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, J.4
  • 15
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A 32 (1976) 922-923
    • (1976) Acta Crystallogr. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 16
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 18
    • 34250721692 scopus 로고    scopus 로고
    • Mitochondria-mediated apoptosis by diallyl trisulfide in human prostate cancer cells is associated with generation of reactive oxygen species and regulated by Bax/Bak
    • Kim Y.A., Xiao D., Xiao H., Powolny A.A., Lew K.L., Reilly M.L., Zeng Y., Wang Z., and Singh S.V. Mitochondria-mediated apoptosis by diallyl trisulfide in human prostate cancer cells is associated with generation of reactive oxygen species and regulated by Bax/Bak. Mol. Cancer Ther. 6 (2007) 1599-1609
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 1599-1609
    • Kim, Y.A.1    Xiao, D.2    Xiao, H.3    Powolny, A.A.4    Lew, K.L.5    Reilly, M.L.6    Zeng, Y.7    Wang, Z.8    Singh, S.V.9
  • 19
    • 0030841589 scopus 로고    scopus 로고
    • Detecting folding motifs and similarities in protein structures
    • Kleywegt G.J., and Jones T.A. Detecting folding motifs and similarities in protein structures. Methods Enzymol. 277 (1997) 525-545
    • (1997) Methods Enzymol. , vol.277 , pp. 525-545
    • Kleywegt, G.J.1    Jones, T.A.2
  • 20
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 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. The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site. Mol. Cell 24 (2006) 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
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan A., Smith C.L., Lamensdorf I., Yoon S.H., and Youle R.J. Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J. Cell Biol. 15 (2001) 1265-1276
    • (2001) J. Cell Biol. , vol.15 , pp. 1265-1276
    • Nechushtan, A.1    Smith, C.L.2    Lamensdorf, I.3    Yoon, S.H.4    Youle, R.J.5
  • 24
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: releasing power for life and unleashing the machineries of death
    • Newmeyer D.D., and 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
  • 25
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 (1991) 281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 27
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai Z.N., Milliman C.L., and Korsmeyer S.J. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74 (1993) 609-619
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: coregulation of dimer formation and intracellular localization
    • Suzuki M., Youle R.J., and 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
  • 33
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallogr. D 56 (2000) 965-972
    • (2000) Acta Crystallogr. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 34
  • 35
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 36
    • 0031660082 scopus 로고    scopus 로고
    • Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing
    • Wang K., Gross A., Waksman G., and Korsmeyer S.J. Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing. Mol. Cell. Biol. 18 (1998) 6083-6089
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6083-6089
    • Wang, K.1    Gross, A.2    Waksman, G.3    Korsmeyer, S.J.4
  • 38
    • 27544446991 scopus 로고    scopus 로고
    • Life in the balance: how BH3-only proteins induce apoptosis
    • Willis S.N., and Adams J.M. Life in the balance: how BH3-only proteins induce apoptosis. Curr. Opin. Cell Biol. 17 (2005) 617-625
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 617-625
    • Willis, S.N.1    Adams, J.M.2
  • 39
    • 22244464818 scopus 로고    scopus 로고
    • Pro-apoptotic Bak is sequestered by Mc1-1 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. Pro-apoptotic Bak is sequestered by Mc1-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev. 19 (2005) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.