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Volumn 20, Issue 4, 2012, Pages 742-751

Phosphorylation regulates assembly of the caspase-6 substrate-binding groove

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 6; PROLINE; SERINE;

EID: 84859416412     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.02.003     Document Type: Article
Times cited : (36)

References (39)
  • 1
    • 0026033985 scopus 로고
    • Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP
    • D. Barford, S.H. Hu, and L.N. Johnson Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP J. Mol. Biol. 218 1991 233 260
    • (1991) J. Mol. Biol. , vol.218 , pp. 233-260
    • Barford, D.1    Hu, S.H.2    Johnson, L.N.3
  • 5
    • 0036790423 scopus 로고    scopus 로고
    • Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: Absolute requirement for removal of caspase-6 prodomain
    • V. Cowling, and J. Downward Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomain Cell Death Differ. 9 2002 1046 1056
    • (2002) Cell Death Differ. , vol.9 , pp. 1046-1056
    • Cowling, V.1    Downward, J.2
  • 6
    • 0035859911 scopus 로고    scopus 로고
    • Selection and characterization of a new class of peptide exosite inhibitors of coagulation factor VIIa
    • M.S. Dennis, M. Roberge, C. Quan, and R.A. Lazarus Selection and characterization of a new class of peptide exosite inhibitors of coagulation factor VIIa Biochemistry 40 2001 9513 9521
    • (2001) Biochemistry , vol.40 , pp. 9513-9521
    • Dennis, M.S.1    Roberge, M.2    Quan, C.3    Lazarus, R.A.4
  • 7
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Q.L. Deveraux, R. Takahashi, G.S. Salvesen, and J.C. Reed X-linked IAP is a direct inhibitor of cell-death proteases Nature 388 1997 300 304
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 9
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • P. Fuentes-Prior, and G.S. Salvesen The protein structures that shape caspase activity, specificity, activation and inhibition Biochem. J. 384 2004 201 232
    • (2004) Biochem. J. , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 13
    • 19644378636 scopus 로고    scopus 로고
    • Allosteric inhibition of PTP1B activity by selective modification of a non-active site cysteine residue
    • S.K. Hansen, M.T. Cancilla, T.P. Shiau, J. Kung, T. Chen, and D.A. Erlanson Allosteric inhibition of PTP1B activity by selective modification of a non-active site cysteine residue Biochemistry 44 2005 7704 7712
    • (2005) Biochemistry , vol.44 , pp. 7704-7712
    • Hansen, S.K.1    Cancilla, M.T.2    Shiau, T.P.3    Kung, J.4    Chen, T.5    Erlanson, D.A.6
  • 15
    • 70350033973 scopus 로고    scopus 로고
    • Dissecting an allosteric switch in caspase-7 using chemical and mutational probes
    • J.A. Hardy, and J.A. Wells Dissecting an allosteric switch in caspase-7 using chemical and mutational probes J. Biol. Chem. 284 2009 26063 26069
    • (2009) J. Biol. Chem. , vol.284 , pp. 26063-26069
    • Hardy, J.A.1    Wells, J.A.2
  • 17
    • 41949117115 scopus 로고    scopus 로고
    • Dynamic regulation of neutrophil survival through tyrosine phosphorylation or dephosphorylation of caspase-8
    • S.H. Jia, J. Parodo, A. Kapus, O.D. Rotstein, and J.C. Marshall Dynamic regulation of neutrophil survival through tyrosine phosphorylation or dephosphorylation of caspase-8 J. Biol. Chem. 283 2008 5402 5413
    • (2008) J. Biol. Chem. , vol.283 , pp. 5402-5413
    • Jia, S.H.1    Parodo, J.2    Kapus, A.3    Rotstein, O.D.4    Marshall, J.C.5
  • 18
    • 0026562948 scopus 로고
    • Glycogen phosphorylase: Control by phosphorylation and allosteric effectors
    • L.N. Johnson Glycogen phosphorylase: control by phosphorylation and allosteric effectors FASEB J. 6 1992 2274 2282
    • (1992) FASEB J. , vol.6 , pp. 2274-2282
    • Johnson, L.N.1
  • 19
    • 0027946039 scopus 로고
    • Electrostatic effects in the control of glycogen phosphorylase by phosphorylation
    • L.N. Johnson, and D. Barford Electrostatic effects in the control of glycogen phosphorylase by phosphorylation Protein Sci. 3 1994 1726 1730
    • (1994) Protein Sci. , vol.3 , pp. 1726-1730
    • Johnson, L.N.1    Barford, D.2
  • 20
    • 57049114930 scopus 로고    scopus 로고
    • Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: Role of disordered phosphorylation loops
    • M. Kato, R.M. Wynn, J.L. Chuang, S.C. Tso, M. Machius, J. Li, and D.T. Chuang Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops Structure 16 2008 1849 1859
    • (2008) Structure , vol.16 , pp. 1849-1859
    • Kato, M.1    Wynn, R.M.2    Chuang, J.L.3    Tso, S.C.4    MacHius, M.5    Li, J.6    Chuang, D.T.7
  • 21
    • 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
    • G. Klaiman, N. Champagne, and A.C. LeBlanc 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 2009 592 601
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 592-601
    • Klaiman, G.1    Champagne, N.2    Leblanc, A.C.3
  • 22
    • 69449095860 scopus 로고    scopus 로고
    • Caspases and kinases in a death grip
    • M. Kurokawa, and S. Kornbluth Caspases and kinases in a death grip Cell 138 2009 838 854
    • (2009) Cell , vol.138 , pp. 838-854
    • Kurokawa, M.1    Kornbluth, S.2
  • 23
    • 79959367758 scopus 로고    scopus 로고
    • Phosphorylation of caspase-7 by p21-activated protein kinase (PAK)2 inhibits chemotherapeutic drugs-induced apoptosis of breast cancer cell lines
    • X. Li, W. Wen, K. Liu, F. Zhu, M. Malakhova, C. Peng, T. Li, H.G. Kim, W. Ma, and Y.Y. Cho Phosphorylation of caspase-7 by p21-activated protein kinase (PAK)2 inhibits chemotherapeutic drugs-induced apoptosis of breast cancer cell lines J. Biol. Chem. 286 2011 22291 22299
    • (2011) J. Biol. Chem. , vol.286 , pp. 22291-22299
    • Li, X.1    Wen, W.2    Liu, K.3    Zhu, F.4    Malakhova, M.5    Peng, C.6    Li, T.7    Kim, H.G.8    Ma, W.9    Cho, Y.Y.10
  • 24
    • 77950012622 scopus 로고    scopus 로고
    • The regulatory crosstalk between kinases and proteases in cancer
    • C. López-Otín, and T. Hunter The regulatory crosstalk between kinases and proteases in cancer Nat. Rev. Cancer 10 2010 278 292
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 278-292
    • López-Otín, C.1    Hunter, T.2
  • 25
    • 0031554904 scopus 로고    scopus 로고
    • Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen
    • M. Podobnik, R. Kuhelj, V. Turk, and D. Turk Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen J. Mol. Biol. 271 1997 774 788
    • (1997) J. Mol. Biol. , vol.271 , pp. 774-788
    • Podobnik, M.1    Kuhelj, R.2    Turk, V.3    Turk, D.4
  • 26
    • 0035859944 scopus 로고    scopus 로고
    • A novel exosite on coagulation factor VIIa and its molecular interactions with a new class of peptide inhibitors
    • M. Roberge, L. Santell, M.S. Dennis, C. Eigenbrot, M.A. Dwyer, and R.A. Lazarus A novel exosite on coagulation factor VIIa and its molecular interactions with a new class of peptide inhibitors Biochemistry 40 2001 9522 9531
    • (2001) Biochemistry , vol.40 , pp. 9522-9531
    • Roberge, M.1    Santell, L.2    Dennis, M.S.3    Eigenbrot, C.4    Dwyer, M.A.5    Lazarus, R.A.6
  • 28
    • 14844323968 scopus 로고    scopus 로고
    • XIAP inhibits caspase-3 and -7 using two binding sites: Evolutionarily conserved mechanism of IAPs
    • F.L. Scott, J.B. Denault, S.J. Riedl, H. Shin, M. Renatus, and G.S. Salvesen XIAP inhibits caspase-3 and -7 using two binding sites: evolutionarily conserved mechanism of IAPs EMBO J. 24 2005 645 655
    • (2005) EMBO J. , vol.24 , pp. 645-655
    • Scott, F.L.1    Denault, J.B.2    Riedl, S.J.3    Shin, H.4    Renatus, M.5    Salvesen, G.S.6
  • 31
    • 0036470319 scopus 로고    scopus 로고
    • Reprieval from execution: The molecular basis of caspase inhibition
    • H.R. Stennicke, C.A. Ryan, and G.S. Salvesen Reprieval from execution: the molecular basis of caspase inhibition Trends Biochem. Sci. 27 2002 94 101
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 94-101
    • Stennicke, H.R.1    Ryan, C.A.2    Salvesen, G.S.3
  • 33
    • 79955097644 scopus 로고    scopus 로고
    • Caspase-6 latent state stability relies on helical propensity
    • S. Vaidya, and J.A. Hardy Caspase-6 latent state stability relies on helical propensity Biochemistry 50 2011 3282 3287
    • (2011) Biochemistry , vol.50 , pp. 3282-3287
    • Vaidya, S.1    Hardy, J.A.2
  • 34
    • 79151469464 scopus 로고    scopus 로고
    • Substrate-induced conformational changes occur in all cleaved forms of caspase-6
    • S. Vaidya, E.M. Velázquez-Delgado, G. Abbruzzese, and J.A. Hardy Substrate-induced conformational changes occur in all cleaved forms of caspase-6 J. Mol. Biol. 406 2011 75 91
    • (2011) J. Mol. Biol. , vol.406 , pp. 75-91
    • Vaidya, S.1    Velázquez-Delgado, E.M.2    Abbruzzese, G.3    Hardy, J.A.4
  • 35
    • 78049347657 scopus 로고    scopus 로고
    • Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation
    • X.J. Wang, Q. Cao, X. Liu, K.T. Wang, W. Mi, Y. Zhang, L.F. Li, A.C. LeBlanc, and X.D. Su Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation EMBO Rep. 11 2010 841 847
    • (2010) EMBO Rep. , vol.11 , pp. 841-847
    • Wang, X.J.1    Cao, Q.2    Liu, X.3    Wang, K.T.4    Mi, W.5    Zhang, Y.6    Li, L.F.7    Leblanc, A.C.8    Su, X.D.9
  • 36
    • 67650070345 scopus 로고    scopus 로고
    • L2′ loop is critical for caspase-7 active site formation
    • W.A. Witkowski, and J.A. Hardy L2′ loop is critical for caspase-7 active site formation Protein Sci. 18 2009 1459 1468
    • (2009) Protein Sci. , vol.18 , pp. 1459-1468
    • Witkowski, W.A.1    Hardy, J.A.2
  • 37
    • 79960687487 scopus 로고    scopus 로고
    • A designed redox-controlled caspase
    • W.A. Witkowski, and J.A. Hardy A designed redox-controlled caspase Protein Sci. 20 2011 1421 1431
    • (2011) Protein Sci. , vol.20 , pp. 1421-1431
    • Witkowski, W.A.1    Hardy, J.A.2
  • 38
    • 9944259021 scopus 로고    scopus 로고
    • Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation
    • R.M. Wynn, M. Kato, M. Machius, J.L. Chuang, J. Li, D.R. Tomchick, and D.T. Chuang Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation Structure 12 2004 2185 2196
    • (2004) Structure , vol.12 , pp. 2185-2196
    • Wynn, R.M.1    Kato, M.2    MacHius, M.3    Chuang, J.L.4    Li, J.5    Tomchick, D.R.6    Chuang, D.T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.