메뉴 건너뛰기




Volumn 8, Issue 7, 2012, Pages 655-660

Allosteric peptides bind a caspase zymogen and mediate caspase tetramerization

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 6; ENZYME PRECURSOR;

EID: 84862882878     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.967     Document Type: Article
Times cited : (33)

References (48)
  • 1
    • 0009530192 scopus 로고    scopus 로고
    • Human ICE/CED-3 protease nomenclature
    • Alnemri, E.S. et al. Human ICE/CED-3 protease nomenclature. Cell 87, 171 (1996).
    • (1996) Cell , vol.87 , pp. 171
    • Alnemri, E.S.1
  • 2
    • 0036931366 scopus 로고    scopus 로고
    • Caspases: Keys in the ignition of cell death
    • Denault, J.B. & Salvesen, G.S. Caspases: keys in the ignition of cell death. Chem. Rev. 102, 4489-4500 (2002).
    • (2002) Chem. Rev. , vol.102 , pp. 4489-4500
    • Denault, J.B.1    Salvesen, G.S.2
  • 3
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl, S.J. & Shi, Y. Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell Biol. 5, 897-907 (2004).
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 4
    • 0030948457 scopus 로고    scopus 로고
    • Substrate specificities of caspase family proteases
    • Talanian, R.V. et al. Substrate specificities of caspase family proteases. J. Biol. Chem. 272, 9677-9682 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 9677-9682
    • Talanian, R.V.1
  • 5
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
    • Stennicke, H.R., Renatus, M., Meldal, M. & Salvesen, G.S. Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem. J. 350, 563-568 (2000).
    • (2000) Biochem. J. , vol.350 , pp. 563-568
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 6
    • 0034615555 scopus 로고    scopus 로고
    • Caspases-controlling intracellular signals by protease zymogen activation
    • Stennicke, H.R. & Salvesen, G.S. Caspases-controlling intracellular signals by protease zymogen activation. Biochim. Biophys. Acta 1477, 299-306 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 299-306
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 7
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi, Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell 9, 459-470 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 8
    • 84862870531 scopus 로고    scopus 로고
    • Caspases: Cell signaling by proteolysis
    • 2nd edn (eds. Bradshaw, R.A. & Dennis, E.A.) Elsevier Inc.
    • Salvesen, G. Caspases: cell signaling by proteolysis. in Handbook of Cell Signaling 2nd edn (eds. Bradshaw, R.A. & Dennis, E.A.) 1297-1302 (Elsevier Inc., 2010).
    • (2010) Handbook of Cell Signaling , pp. 1297-1302
    • Salvesen, G.1
  • 9
    • 0035909889 scopus 로고    scopus 로고
    • Structural basis for the activation of human procaspase-7
    • Riedl, S.J. et al. Structural basis for the activation of human procaspase-7. Proc. Natl. Acad. Sci. USA 98, 14790-14795 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14790-14795
    • Riedl, S.J.1
  • 10
    • 0035798361 scopus 로고    scopus 로고
    • Crystal structure of a procaspase-7 zymogen. Mechanisms of activation and substrate binding
    • Chai, J. et al. Crystal structure of a procaspase-7 zymogen. Mechanisms of activation and substrate binding. Cell 107, 399-407 (2001).
    • (2001) Cell , vol.107 , pp. 399-407
    • Chai, J.1
  • 11
    • 78049347657 scopus 로고    scopus 로고
    • Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation
    • Wang, X.J. et al. Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation. EMBO Rep. 11, 841-847 (2010).
    • (2010) EMBO Rep. , vol.11 , pp. 841-847
    • Wang, X.J.1
  • 12
    • 0037291871 scopus 로고    scopus 로고
    • A unified model for apical caspase activation
    • Boatright, K.M. et al. A unified model for apical caspase activation. Mol. Cell 11, 529-541 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 529-541
    • Boatright, K.M.1
  • 13
    • 14044252160 scopus 로고    scopus 로고
    • Caspase-8 can be activated by interchain proteolysis without receptor-triggered dimerization during drug-induced apoptosis
    • Sohn, D., Schulze-Osthoff, K. & Janicke, R.U. Caspase-8 can be activated by interchain proteolysis without receptor-triggered dimerization during drug-induced apoptosis. J. Biol. Chem. 280, 5267-5273 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 5267-5273
    • Sohn, D.1    Schulze-Osthoff, K.2    Janicke, R.U.3
  • 14
    • 66249094552 scopus 로고    scopus 로고
    • Mechanism of procaspase-8 activation by c-FLIPL
    • Yu, J.W., Jeffrey, P.D. & Shi, Y. Mechanism of procaspase-8 activation by c-FLIPL. Proc. Natl. Acad. Sci. USA 106, 8169-8174 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8169-8174
    • Yu, J.W.1    Jeffrey, P.D.2    Shi, Y.3
  • 15
    • 0033613143 scopus 로고    scopus 로고
    • Caspase activation: The induced-proximity model
    • Salvesen, G.S. & Dixit, V.M. Caspase activation: the induced-proximity model. Proc. Natl. Acad. Sci. USA 96, 10964-10967 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10964-10967
    • Salvesen, G.S.1    Dixit, V.M.2
  • 16
    • 69249100500 scopus 로고    scopus 로고
    • Human caspases: Activation, specificity, and regulation
    • Pop, C. & Salvesen, G.S. Human caspases: activation, specificity, and regulation. J. Biol. Chem. 284, 21777-21781 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 21777-21781
    • Pop, C.1    Salvesen, G.S.2
  • 17
    • 3343011970 scopus 로고    scopus 로고
    • Caspase activation, inhibition, and reactivation: A mechanistic view
    • Shi, Y. Caspase activation, inhibition, and reactivation: a mechanistic view. Protein Sci. 13, 1979-1987 (2004).
    • (2004) Protein Sci. , vol.13 , pp. 1979-1987
    • Shi, Y.1
  • 18
    • 73349135640 scopus 로고    scopus 로고
    • Caspase-6 activation in familial Alzheimer disease brains carrying amyloid precursor protein or presenilin I or presenilin II mutations
    • Albrecht, S., Bogdanovic, N., Ghetti, B., Winblad, B. & LeBlanc, A.C. Caspase-6 activation in familial Alzheimer disease brains carrying amyloid precursor protein or presenilin I or presenilin II mutations. J. Neuropathol. Exp. Neurol. 68, 1282-1293 (2009).
    • (2009) J. Neuropathol. Exp. Neurol. , vol.68 , pp. 1282-1293
    • Albrecht, S.1    Bogdanovic, N.2    Ghetti, B.3    Winblad, B.4    LeBlanc, A.C.5
  • 19
    • 34247882772 scopus 로고    scopus 로고
    • Activation of caspase-6 in aging and mild cognitive impairment
    • Albrecht, S. et al. Activation of caspase-6 in aging and mild cognitive impairment. Am. J. Pathol. 170, 1200-1209 (2007).
    • (2007) Am. J. Pathol. , vol.170 , pp. 1200-1209
    • Albrecht, S.1
  • 20
    • 3242811902 scopus 로고    scopus 로고
    • Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease
    • Guo, H. et al. Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease. Am. J. Pathol. 165, 523-531 (2004).
    • (2004) Am. J. Pathol. , vol.165 , pp. 523-531
    • Guo, H.1
  • 21
    • 50249086898 scopus 로고    scopus 로고
    • Targets of caspase-6 activity in human neurons and Alzheimer disease
    • Klaiman, G., Petzke, T.L., Hammond, J. & Leblanc, A.C. Targets of caspase-6 activity in human neurons and Alzheimer disease. Mol. Cell. Proteomics 7, 1541-1555 (2008).
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1541-1555
    • Klaiman, G.1    Petzke, T.L.2    Hammond, J.3    Leblanc, A.C.4
  • 22
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev, A., McLaughlin, T., O'Leary, D.D. & Tessier-Lavigne, M. APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 457, 981-989 (2009).
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 23
    • 0037107151 scopus 로고    scopus 로고
    • Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease
    • Wellington, C.L. et al. Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease. J. Neurosci. 22, 7862-7872 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 7862-7872
    • Wellington, C.L.1
  • 24
    • 78149487690 scopus 로고    scopus 로고
    • Cleavage at the 586 amino acid caspase-6 site in mutant huntingtin influences caspase-6 activation in vivo
    • Graham, R.K. et al. Cleavage at the 586 amino acid caspase-6 site in mutant huntingtin influences caspase-6 activation in vivo. J. Neurosci. 30, 15019-15029 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 15019-15029
    • Graham, R.K.1
  • 25
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • Graham, R.K. et al. Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 125, 1179-1191 (2006).
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1
  • 26
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M. et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990-1993 (1997).
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1
  • 27
    • 11144357398 scopus 로고    scopus 로고
    • Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington's disease
    • Hermel, E. et al. Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington's disease. Cell Death Differ. 11, 424-438 (2004).
    • (2004) Cell Death Differ , vol.11 , pp. 424-438
    • Hermel, E.1
  • 28
    • 33645056953 scopus 로고    scopus 로고
    • Caspase inhibitors: A pharmaceutical industry perspective
    • Linton, S.D. Caspase inhibitors: a pharmaceutical industry perspective. Curr. Top. Med. Chem. 5, 1697-1717 (2005).
    • (2005) Curr. Top. Med. Chem. , vol.5 , pp. 1697-1717
    • Linton, S.D.1
  • 29
    • 33845472476 scopus 로고    scopus 로고
    • Caspase inhibitors: Viral, cellular and chemical
    • Callus, B.A. & Vaux, D.L. Caspase inhibitors: viral, cellular and chemical. Cell Death Differ. 14, 73-78 (2007).
    • (2007) Cell Death Differ. , vol.14 , pp. 73-78
    • Callus, B.A.1    Vaux, D.L.2
  • 33
    • 0035798361 scopus 로고    scopus 로고
    • Crystal structure of a procaspase-7 zymogen: Mechanisms of activation and substrate binding
    • Chai, J. et al. Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding. Cell 107, 399-407 (2001).
    • (2001) Cell , vol.107 , pp. 399-407
    • Chai, J.1
  • 34
    • 0028792105 scopus 로고
    • Guidelines for protein design: The energetics of â sheet side chain interactions
    • Smith, C.K. & Regan, L. Guidelines for protein design: the energetics of â sheet side chain interactions. Science 270, 980-982 (1995).
    • (1995) Science , vol.270 , pp. 980-982
    • Smith, C.K.1    Regan, L.2
  • 35
    • 0029891838 scopus 로고    scopus 로고
    • The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A
    • Orth, K., Chinnaiyan, A.M., Garg, M., Froelich, C.J. & Dixit, V.M. The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. J. Biol. Chem. 271, 16443-16446 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 16443-16446
    • Orth, K.1    Chinnaiyan, A.M.2    Garg, M.3    Froelich, C.J.4    Dixit, V.M.5
  • 36
    • 0029758833 scopus 로고    scopus 로고
    • Cleavage of lamin A by Mch2 but not CPP32: Multiple ICE-related proteases with distinct substrate recognition properties are active in apoptosis
    • Takahashi, A. et al. Cleavage of lamin A by Mch2 but not CPP32: multiple ICE-related proteases with distinct substrate recognition properties are active in apoptosis. Proc. Natl. Acad. Sci. USA 93, 8395-8400 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8395-8400
    • Takahashi, A.1
  • 37
    • 0035831473 scopus 로고    scopus 로고
    • Executioner caspase-3, -6 and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis
    • Slee, E.A., Adrain, C. & Martin, S.J. Executioner caspase-3, -6 and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis. J. Biol. Chem. 276, 7320-7326 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 7320-7326
    • Slee, E.A.1    Adrain, C.2    Martin, S.J.3
  • 38
    • 0037090614 scopus 로고    scopus 로고
    • Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation
    • Ruchaud, S. et al. Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation. EMBO J. 21, 1967-1977 (2002).
    • (2002) EMBO J. , vol.21 , pp. 1967-1977
    • Ruchaud, S.1
  • 39
    • 84855786390 scopus 로고    scopus 로고
    • A whole cell assay to measure caspase-6 activity by detecting cleavage of Lamin A/C
    • Mintzer, R. et al. A whole cell assay to measure caspase-6 activity by detecting cleavage of Lamin A/C. PLoS ONE 7, e30376 (2012).
    • (2012) PLoS ONE , vol.7
    • Mintzer, R.1
  • 40
    • 0042167442 scopus 로고    scopus 로고
    • Identification of the primary caspase 3 cleavage site in alpha II-spectrin during apoptosis
    • Williams, S.T., Smith, A.N., Cianci, C.D., Morrow, J.S. & Brown, T.L. Identification of the primary caspase 3 cleavage site in alpha II-spectrin during apoptosis. Apoptosis 8, 353-361 (2003).
    • (2003) Apoptosis , vol.8 , pp. 353-361
    • Williams, S.T.1    Smith, A.N.2    Cianci, C.D.3    Morrow, J.S.4    Brown, T.L.5
  • 41
    • 0033214624 scopus 로고    scopus 로고
    • Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis
    • Germain, M. et al. Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. J. Biol. Chem. 274, 28379-28384 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 28379-28384
    • Germain, M.1
  • 42
    • 0035932465 scopus 로고    scopus 로고
    • Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex
    • Xu, G. et al. Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex. Nature 410, 494-497 (2001).
    • (2001) Nature , vol.410 , pp. 494-497
    • Xu, G.1
  • 43
    • 60649093275 scopus 로고    scopus 로고
    • Self-activation of caspase-6 in vitro and in vivo: Caspase-6 activation does not induce cell death in HEK293T cells
    • Klaiman, G., Champagne, N. & LeBlanc, A.C. Self-activation of caspase-6 in vitro and in vivo: caspase-6 activation does not induce cell death in HEK293T cells. Biochim. Biophys. Acta 1793, 592-601 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 592-601
    • Klaiman, G.1    Champagne, N.2    LeBlanc, A.C.3
  • 44
    • 0036088471 scopus 로고    scopus 로고
    • IAP proteins: Blocking the road to death's door
    • Salvesen, G.S. & Duckett, C.S. IAP proteins: blocking the road to death's door. Nat. Rev. Mol. Cell Biol. 3, 401-410 (2002).
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 401-410
    • Salvesen, G.S.1    Duckett, C.S.2
  • 46
    • 79151469464 scopus 로고    scopus 로고
    • Substrate-induced conformational changes occur in all cleaved forms of caspase-6
    • Vaidya, S., Velazquez-Delgado, E.M., Abbruzzese, G. & Hardy, J.A. Substrate-induced conformational changes occur in all cleaved forms of caspase-6. J. Mol. Biol. 406, 75-91 (2011).
    • (2011) J. Mol. Biol. , vol.406 , pp. 75-91
    • Vaidya, S.1    Velazquez-Delgado, E.M.2    Abbruzzese, G.3    Hardy, J.A.4
  • 47
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D. & Zakour, R.A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154, 367-382 (1987).
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 48
    • 62649175248 scopus 로고    scopus 로고
    • Inhibition of Wnt signaling by Dishevelled PDZ peptides
    • Zhang, Y. et al. Inhibition of Wnt signaling by Dishevelled PDZ peptides. Nat. Chem. Biol. 5, 217-219 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 217-219
    • Zhang, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.