메뉴 건너뛰기




Volumn 21, Issue 12, 2014, Pages 1068-1074

Internal motions prime cIAP1 for rapid activation

Author keywords

[No Author keywords available]

Indexed keywords

INHIBITOR OF APOPTOSIS PROTEIN 1; MONOMER; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; BIRC2 PROTEIN, HUMAN; INHIBITOR OF APOPTOSIS PROTEIN; PROTEIN BINDING;

EID: 84925552884     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2916     Document Type: Article
Times cited : (16)

References (47)
  • 1
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan, D. & Weinberg, R.A. Hallmarks of cancer: the next generation. Cell 144, 646-674 (2011).
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 81055125652 scopus 로고    scopus 로고
    • Programmed cell death in animal development and disease
    • Fuchs, Y. & Steller, H. Programmed cell death in animal development and disease. Cell 147, 742-758 (2011).
    • (2011) Cell , vol.147 , pp. 742-758
    • Fuchs, Y.1    Steller, H.2
  • 3
    • 76149118435 scopus 로고    scopus 로고
    • Small-molecule pan-IAP antagonists: A patent review
    • Flygare, J.A. & Fairbrother, W.J. Small-molecule pan-IAP antagonists: a patent review. Expert Opin. Ther. Pat. 20, 251-267 (2010).
    • (2010) Expert Opin. Ther. Pat. , vol.20 , pp. 251-267
    • Flygare, J.A.1    Fairbrother, W.J.2
  • 4
    • 84856495152 scopus 로고    scopus 로고
    • Targeting IAP proteins for therapeutic intervention in cancer
    • Fulda, S. & Vucic, D. Targeting IAP proteins for therapeutic intervention in cancer. Nat. Rev. Drug Discov. 11, 109-124 (2012).
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 109-124
    • Fulda, S.1    Vucic, D.2
  • 5
    • 0034616945 scopus 로고    scopus 로고
    • A mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du, C., Fang, M., Li, Y., Li, L. & Wang, X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102, 33-42 (2000).
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Smac, W.X.5
  • 6
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen, A.M. et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102, 43-53 (2000).
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1
  • 7
    • 0034700495 scopus 로고    scopus 로고
    • Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
    • Liu, Z. et al. Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain. Nature 408, 1004-1008 (2000).
    • (2000) Nature , vol.408 , pp. 1004-1008
    • Liu, Z.1
  • 8
    • 0034700491 scopus 로고    scopus 로고
    • Structural basis of IAP recognition by Smac/DIABLO
    • Wu, G. et al. Structural basis of IAP recognition by Smac/DIABLO. Nature 408, 1008-1012 (2000).
    • (2000) Nature , vol.408 , pp. 1008-1012
    • Wu, G.1
  • 9
    • 19944431887 scopus 로고    scopus 로고
    • Engineering ML-IAP to produce an extraordinarily potent caspase 9 inhibitor: Implications for Smac-dependent anti-apoptotic activity of ML-IAP
    • Vucic, D. et al. Engineering ML-IAP to produce an extraordinarily potent caspase 9 inhibitor: implications for Smac-dependent anti-apoptotic activity of ML-IAP. Biochem. J. 385, 11-20 (2005).
    • (2005) Biochem. J. , vol.385 , pp. 11-20
    • Vucic, D.1
  • 10
    • 37749037799 scopus 로고    scopus 로고
    • Design, synthesis, and biological activity of a potent Smac mimetic that sensitizes cancer cells to apoptosis by antagonizing IAPs
    • Zobel, K. et al. Design, synthesis, and biological activity of a potent Smac mimetic that sensitizes cancer cells to apoptosis by antagonizing IAPs. ACS Chem. Biol. 1, 525-533 (2006).
    • (2006) ACS Chem. Biol. , vol.1 , pp. 525-533
    • Zobel, K.1
  • 11
    • 36048999753 scopus 로고    scopus 로고
    • IAP antagonists induce autoubiquitination of c-IAPs NF-κB activation, and TNFα-dependent apoptosis
    • Varfolomeev, E. et al. IAP antagonists induce autoubiquitination of c-IAPs, NF-κB activation, and TNFα-dependent apoptosis. Cell 131, 669-681 (2007).
    • (2007) Cell , vol.131 , pp. 669-681
    • Varfolomeev, E.1
  • 12
    • 37549000486 scopus 로고    scopus 로고
    • A Smac mimetic rescue screen reveals roles for inhibitor of apoptosis proteins in tumor necrosis factor-α signaling
    • Gaither, A. et al. A Smac mimetic rescue screen reveals roles for inhibitor of apoptosis proteins in tumor necrosis factor-α signaling. Cancer Res. 67, 11493-11498 (2007).
    • (2007) Cancer Res , vol.67 , pp. 11493-11498
    • Gaither, A.1
  • 13
    • 36148954336 scopus 로고    scopus 로고
    • IAP antagonists target cIAP1 to induce TNFα-dependent apoptosis
    • Vince, J.E. et al. IAP antagonists target cIAP1 to induce TNFα-dependent apoptosis. Cell 131, 682-693 (2007).
    • (2007) Cell , vol.131 , pp. 682-693
    • Vince, J.E.1
  • 14
    • 44949240664 scopus 로고    scopus 로고
    • CIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination
    • Bertrand, M.J.M. et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol. Cell 30, 689-700 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 689-700
    • Bertrand, M.J.M.1
  • 15
    • 54049155149 scopus 로고    scopus 로고
    • C-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFα)-induced NF-κB activation
    • Varfolomeev, E. et al. c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFα)-induced NF-κB activation. J. Biol. Chem. 283, 24295-24299 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 24295-24299
    • Varfolomeev, E.1
  • 16
    • 84865781586 scopus 로고    scopus 로고
    • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
    • Plechanovová, A., Jaffray, E.G., Tatham, M.H., Naismith, J.H. & Hay, R.T. Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489, 115-120 (2012).
    • (2012) Nature , vol.489 , pp. 115-120
    • Plechanovová, A.1    Jaffray, E.G.2    Tatham, M.H.3    Naismith, J.H.4    Hay, R.T.5
  • 17
    • 84866124869 scopus 로고    scopus 로고
    • BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
    • Dou, H., Buetow, L., Sibbet, G.J., Cameron, K. & Huang, D.T. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nat. Struct. Mol. Biol. 19, 876-883 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 876-883
    • Dou, H.1    Buetow, L.2    Sibbet, G.J.3    Cameron, K.4    Huang, D.T.5
  • 18
    • 57649120782 scopus 로고    scopus 로고
    • Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment
    • Mace, P.D. et al. Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment. J. Biol. Chem. 283, 31633-31640 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 31633-31640
    • MacE, P.D.1
  • 19
    • 79955759159 scopus 로고    scopus 로고
    • Smac mimetics activate the E3 ligase activity of cIAP1 protein by promoting RING domain dimerization
    • Feltham, R. et al. Smac mimetics activate the E3 ligase activity of cIAP1 protein by promoting RING domain dimerization. J. Biol. Chem. 286, 17015-17028 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 17015-17028
    • Feltham, R.1
  • 20
    • 80054837173 scopus 로고    scopus 로고
    • Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination
    • Dueber, E.C. et al. Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination. Science 334, 376-380 (2011).
    • (2011) Science , vol.334 , pp. 376-380
    • Dueber, E.C.1
  • 21
    • 79958051518 scopus 로고    scopus 로고
    • CARD-mediated autoinhibition of cIAP1′s E3 ligase activity suppresses cell proliferation and migration
    • Lopez, J. et al. CARD-mediated autoinhibition of cIAP1′s E3 ligase activity suppresses cell proliferation and migration. Mol. Cell 42, 569-583 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 569-583
    • Lopez, J.1
  • 22
    • 79958837339 scopus 로고    scopus 로고
    • An introduction to NMR-based approaches for measuring protein dynamics
    • Kleckner, I.R. & Foster, M.P. An introduction to NMR-based approaches for measuring protein dynamics. Biochim. Biophys. Acta 1814, 942-968 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 942-968
    • Kleckner, I.R.1    Foster, M.P.2
  • 23
    • 24744447629 scopus 로고    scopus 로고
    • Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins
    • Tugarinov, V. & Kay, L.E. Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins. ChemBioChem 6, 1567-1577 (2005).
    • (2005) ChemBioChem , vol.6 , pp. 1567-1577
    • Tugarinov, V.1    Kay, L.E.2
  • 24
    • 36049046667 scopus 로고    scopus 로고
    • Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR
    • Gelis, I. et al. Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR. Cell 131, 756-769 (2007).
    • (2007) Cell , vol.131 , pp. 756-769
    • Gelis, I.1
  • 25
    • 84860180269 scopus 로고    scopus 로고
    • An integrated high-throughput data acquisition system for biological solution X-ray scattering studies
    • Martel, A., Liu, P., Weiss, T.M., Niebuhr, M. & Tsuruta, H. An integrated high-throughput data acquisition system for biological solution X-ray scattering studies. J. Synchrotron Radiat. 19, 431-434 (2012).
    • (2012) J. Synchrotron Radiat. , vol.19 , pp. 431-434
    • Martel, A.1    Liu, P.2    Weiss, T.M.3    Niebuhr, M.4    Tsuruta, H.5
  • 26
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • Bernadó, P., Mylonas, E., Petoukhov, M.V., Blackledge, M. & Svergun, D.I. Structural characterization of flexible proteins using small-angle X-ray scattering. J. Am. Chem. Soc. 129, 5656-5664 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5656-5664
    • Bernadó, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 28
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman, K. & Kern, D. Dynamic personalities of proteins. Nature 450, 964-972 (2007).
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 29
    • 84879525973 scopus 로고    scopus 로고
    • Macromolecular juggling by ubiquitylation enzymes
    • Lorenz, S., Cantor, A.J., Rape, M. & Kuriyan, J. Macromolecular juggling by ubiquitylation enzymes. BMC Biol. 11, 65 (2013).
    • (2013) BMC Biol , vol.11 , pp. 65
    • Lorenz, S.1    Cantor, A.J.2    Rape, M.3    Kuriyan, J.4
  • 30
    • 0028053969 scopus 로고
    • Kinetics of the low pH-induced conformational changes and fusogenic activity of influenza hemagglutinin
    • Krumbiegel, M., Herrmann, A. & Blumenthal, R. Kinetics of the low pH-induced conformational changes and fusogenic activity of influenza hemagglutinin. Biophys. J. 67, 2355-2360 (1994).
    • (1994) Biophys. J. , vol.67 , pp. 2355-2360
    • Krumbiegel, M.1    Herrmann, A.2    Blumenthal, R.3
  • 31
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C.M. & Kim, P.S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823-832 (1993).
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 32
    • 17044420416 scopus 로고    scopus 로고
    • Structure of the UBA domain of Dsk2p in complex with ubiquitin molecular determinants for ubiquitin recognition
    • Ohno, A. et al. Structure of the UBA domain of Dsk2p in complex with ubiquitin molecular determinants for ubiquitin recognition. Structure 13, 521-532 (2005).
    • (2005) Structure , vol.13 , pp. 521-532
    • Ohno, A.1
  • 33
    • 33644850903 scopus 로고    scopus 로고
    • UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination
    • Brzovic, P.S., Lissounov, A., Christensen, D.E., Hoyt, D.W. & Klevit, R.E.A. UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination. Mol. Cell 21, 873-880 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 873-880
    • Brzovic, P.S.1    Lissounov, A.2    Christensen, D.E.3    Hoyt, D.W.4    Klevit, R.E.A.5
  • 34
    • 84866858702 scopus 로고    scopus 로고
    • Structure of an E3:E2~Ub complex reveals an allosteric mechanism shared among RING/U-box ligases
    • Pruneda, J.N. et al. Structure of an E3:E2~Ub complex reveals an allosteric mechanism shared among RING/U-box ligases. Mol. Cell 47, 933-942 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 933-942
    • Pruneda, J.N.1
  • 35
    • 80155198826 scopus 로고    scopus 로고
    • Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex
    • Bentley, M.L. et al. Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex. EMBO J. 30, 3285-3297 (2011).
    • (2011) EMBO J. , vol.30 , pp. 3285-3297
    • Bentley, M.L.1
  • 36
    • 80051514401 scopus 로고    scopus 로고
    • Preparation of distinct ubiquitin chain reagents of high purity and yield
    • Dong, K.C. et al. Preparation of distinct ubiquitin chain reagents of high purity and yield. Structure 19, 1053-1063 (2011).
    • (2011) Structure , vol.19 , pp. 1053-1063
    • Dong, K.C.1
  • 37
    • 0032520638 scopus 로고    scopus 로고
    • A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli
    • Smith, P.A. et al. A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli. Nucleic Acids Res. 26, 1414-1420 (1998).
    • (1998) Nucleic Acids Res , vol.26 , pp. 1414-1420
    • Smith, P.A.1
  • 38
    • 0031627465 scopus 로고    scopus 로고
    • An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli
    • Cai, M. et al. An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli. J. Biomol. NMR 11, 97-102 (1998).
    • (1998) J. Biomol. NMR , vol.11 , pp. 97-102
    • Cai, M.1
  • 39
    • 34547687784 scopus 로고    scopus 로고
    • Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy
    • Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy. Nat. Protoc. 1, 749-754 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 749-754
  • 41
    • 0002889918 scopus 로고
    • A general two-site solution for the chemical exchange produced dependence of T2 upon the Carr-Purcell pulse separation
    • Carver, J.P. & Richards, R.E. A general two-site solution for the chemical exchange produced dependence of T2 upon the Carr-Purcell pulse separation. J. Magn. Reson. 6, 89-105 (1972).
    • (1972) J. Magn. Reson. , vol.6 , pp. 89-105
    • Carver, J.P.1    Richards, R.E.2
  • 42
    • 84856520247 scopus 로고    scopus 로고
    • GUARDD: User-friendly MATLAB software for rigorous analysis of CPMG RD NMR data
    • Kleckner, I.R. & Foster, M.P. GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data. J. Biomol. NMR 52, 11-22 (2012).
    • (2012) J. Biomol. NMR , vol.52 , pp. 11-22
    • Kleckner, I.R.1    Foster, M.P.2
  • 43
    • 0000243599 scopus 로고    scopus 로고
    • A wide-bandpass multilayer monochromator for biological small-angle scattering and fiber diffraction studies
    • Tsuruta, H. et al. A wide-bandpass multilayer monochromator for biological small-angle scattering and fiber diffraction studies. J. Appl. Crystallogr. 31, 672-682 (1998).
    • (1998) J. Appl. Crystallogr. , vol.31 , pp. 672-682
    • Tsuruta, H.1
  • 44
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503 (1992).
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 45
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun, D.I., Petoukhov, M.V. & Koch, M. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80, 2946-2953 (2001).
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.3
  • 46
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V.V. & Svergun, D.I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864 (2003).
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 47
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov, M.V. & Svergun, D.I. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89, 1237-1250 (2005).
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.