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Volumn 288, Issue 21, 2013, Pages 15142-15147

Proteolytic processing of the caspase-9 zymogen is required for apoptosome-mediated activation of caspase-9

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSOMES; EXPERIMENTAL DATUM; HOMODIMERS; ORDERS OF MAGNITUDE; PROTEASE ACTIVITIES; PROTEOLYTIC ACTIVITIES; PROTEOLYTIC PROCESSING; TRIPLE MUTANTS;

EID: 84878242246     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.441568     Document Type: Article
Times cited : (55)

References (23)
  • 1
    • 0842281645 scopus 로고    scopus 로고
    • Cell Death: Critical Control Points
    • DOI 10.1016/S0092-8674(04)00046-7
    • Danial, N. N., and Korsmeyer, S. J. (2004) Cell death: critical control points. Cell 116, 205-219 (Pubitemid 38167313)
    • (2004) Cell , vol.116 , Issue.2 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 2
    • 81055125652 scopus 로고    scopus 로고
    • Programmed cell death in animal development and disease
    • Fuchs, Y., and Steller, H. (2011) Programmed cell death in animal development and disease. Cell 147, 742-758
    • (2011) Cell , vol.147 , pp. 742-758
    • Fuchs, Y.1    Steller, H.2
  • 3
    • 14044278251 scopus 로고    scopus 로고
    • Death receptor signaling
    • DOI 10.1242/jcs.01610
    • Lavrik, I., Golks, A., and Krammer, P. H. (2005) Death receptor signaling. J. Cell Sci. 118, 265-267 (Pubitemid 40277339)
    • (2005) Journal of Cell Science , vol.118 , Issue.2 , pp. 265-267
    • Lavrik, I.1    Golks, A.2    Krammer, P.H.3
  • 4
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • DOI 10.1038/nrm1496
    • Riedl, S. J., and Shi, Y. (2004) Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell Biol. 5, 897-907 (Pubitemid 39486541)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.11 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 5
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi, Y. (2002) Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell 9, 459-470
    • (2002) Mol. Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 6
    • 78649635776 scopus 로고    scopus 로고
    • Molecular cell death platforms and assemblies
    • Mace, P. D., and Riedl, S. J. (2010) Molecular cell death platforms and assemblies. Curr. Opin. Cell Biol. 22, 828-836
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 828-836
    • Mace, P.D.1    Riedl, S.J.2
  • 7
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • DOI 10.1016/S0092-8674(00)80085-9
    • Liu, X., Kim, C. N., Yang, J., Jemmerson, R., and Wang, X. (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86, 147-157 (Pubitemid 26256586)
    • (1996) Cell , vol.86 , Issue.1 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 8
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • DOI 10.1016/S0092-8674(00)80501-2
    • Zou, H., Henzel, W. J., Liu, X., Lutschg, A., and Wang, X. (1997) Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90, 405-413 (Pubitemid 27347231)
    • (1997) Cell , vol.90 , Issue.3 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 9
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • DOI 10.1016/S1097-2765(02)00442-2
    • Acehan, D., Jiang, X., Morgan, D. G., Heuser, J. E., Wang, X., and Akey, C. W. (2002) Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation. Mol. Cell 9, 423-432 (Pubitemid 34195566)
    • (2002) Molecular Cell , vol.9 , Issue.2 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 10
    • 0033573020 scopus 로고    scopus 로고
    • Caspase-9 and APAF-1 form an active holoenzyme
    • DOI 10.1101/gad.13.24.3179
    • Rodriguez, J., and Lazebnik, Y. (1999) Caspase-9 and APAF-1 form an active holoenzyme. Genes Dev. 13, 3179-3184 (Pubitemid 30030439)
    • (1999) Genes and Development , vol.13 , Issue.24 , pp. 3179-3184
    • Rodriguez, J.1    Lazebnik, Y.2
  • 11
    • 67650455882 scopus 로고    scopus 로고
    • The Apaf-1·procaspase-9 apoptosome complex functions as a proteolytic-based molecular timer
    • Malladi, S., Challa-Malladi, M., Fearnhead, H. O., and Bratton, S. B. (2009) The Apaf-1·procaspase-9 apoptosome complex functions as a proteolytic-based molecular timer. EMBO J. 28, 1916-1925
    • (2009) EMBO J. , vol.28 , pp. 1916-1925
    • Malladi, S.1    Challa-Malladi, M.2    Fearnhead, H.O.3    Bratton, S.B.4
  • 15
    • 17244368276 scopus 로고    scopus 로고
    • Structure of the apoptotic protease-activating factor 1 bound to ADP
    • DOI 10.1038/nature03465
    • Riedl, S. J., Li, W., Chao, Y., Schwarzenbacher, R., and Shi, Y. (2005) Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature 434, 926-933 (Pubitemid 40559008)
    • (2005) Nature , vol.434 , Issue.7035 , pp. 926-933
    • Riedl, S.J.1    Li, W.2    Chao, Y.3    Schwarzenbacher, R.4    Shi, Y.5
  • 16
    • 0032085941 scopus 로고    scopus 로고
    • Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization
    • Srinivasula, S. M., Ahmad, M., Fernandes-Alnemri, T., and Alnemri, E. S. (1998) Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol. Cell 1, 949-957 (Pubitemid 128379256)
    • (1998) Molecular Cell , vol.1 , Issue.7 , pp. 949-957
    • Srinivasula, S.M.1    Ahmad, M.2    Fernandes-Alnemri, T.3    Alnemri, E.S.4
  • 18
    • 0037291890 scopus 로고    scopus 로고
    • Insights into the regulatory mechanism for caspase-8 activation
    • DOI 10.1016/S1097-2765(03)00059-5
    • Donepudi, M., Mac Sweeney, A., Briand, C., and Grütter, M. G. (2003) Insights into the regulatory mechanism for caspase-8 activation. Mol. Cell 11, 543-549 (Pubitemid 36297058)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 543-549
    • Donepudi, M.1    Sweeney, A.M.2    Briand, C.3    Grutter, M.G.4
  • 19
    • 1542782158 scopus 로고    scopus 로고
    • Requirement of both the second and third BIR domains for the relief of X-linked inhibitor of apoptosis protein (XIAP)-mediated caspase inhibition by Smac
    • Huang, Y., Rich, R. L., Myszka, D. G., and Wu, H. (2003) Requirement of both the second and third BIR domains for the relief of X-linked inhibitor of apoptosis protein (XIAP)-mediated caspase inhibition by Smac. J. Biol. Chem. 278, 49517-49522
    • (2003) J. Biol. Chem. , vol.278 , pp. 49517-49522
    • Huang, Y.1    Rich, R.L.2    Myszka, D.G.3    Wu, H.4
  • 21
    • 35648961848 scopus 로고    scopus 로고
    • A dimeric Smac/Diablo peptide directly relieves caspase-3 inhibition by XIAP: Dynamic and cooperative regulation of XIAP by Smac/Diablo
    • DOI 10.1074/jbc.M705258200
    • Gao, Z., Tian, Y., Wang, J., Yin, Q., Wu, H., Li, Y. M., and Jiang, X. (2007) A dimeric Smac/Diablo peptide directly relieves caspase-3 inhibition by XIAP. Dynamic and cooperative regulation of XIAP by Smac/Diablo. J. Biol. Chem. 282, 30718-30727 (Pubitemid 350035215)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.42 , pp. 30718-30727
    • Gao, Z.1    Tian, Y.2    Wang, J.3    Yin, Q.4    Wu, H.5    Li, Y.-M.6    Jiang, X.7
  • 22
    • 77956932246 scopus 로고    scopus 로고
    • cIAP1 cooperatively inhibits procaspase-3 activation by the caspase-9 apoptosome
    • Burke, S. P., Smith, L., and Smith, J. B. (2010) cIAP1 cooperatively inhibits procaspase-3 activation by the caspase-9 apoptosome. J. Biol. Chem. 285, 30061-30068
    • (2010) J. Biol. Chem. , vol.285 , pp. 30061-30068
    • Burke, S.P.1    Smith, L.2    Smith, J.B.3
  • 23
    • 61449175831 scopus 로고    scopus 로고
    • Structural and biochemical studies on procaspase-8: New insights on initiator caspase activation
    • Keller, N., Mareš, J., Zerbe, O., and Grütter, M. G. (2009) Structural and biochemical studies on procaspase-8: new insights on initiator caspase activation. Structure 17, 438-448
    • (2009) Structure , vol.17 , pp. 438-448
    • Keller, N.1    Mareš, J.2    Zerbe, O.3    Grütter, M.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.