메뉴 건너뛰기




Volumn 49, Issue 9, 2010, Pages 1923-1930

Novel small molecules relieve prothymosin α-mediated inhibition of apoptosome formation by blocking its interaction with Apaf-1

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS; APOPTOSOMES; CASPASE-3; CASPASE-3 ACTIVATION; CYTOCHROME C; HELA CELL; HETERONUCLEAR; HIGH-THROUGHPUT SCREENING; HUMAN CANCER; IN-VITRO; MECHANISM OF ACTION; NUCLEAR PROTEINS; PROCASPASE; QUANTUM CORRELATIONS; SMALL MOLECULES; STRESS-INDUCED; TARGET PROTEINS;

EID: 77749259049     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi9022329     Document Type: Article
Times cited : (26)

References (39)
  • 1
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson, C. B. (1995) Apoptosis in the Pathogenesis and Treatment of Disease. Science 267, 1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 2
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen, G. S., and Dixit, V. M. (1997) Caspases: Intracellular signaling by proteolysis. Cell 91, 443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 3
    • 0033383556 scopus 로고    scopus 로고
    • Death by design: Mechanism and control of apoptosis
    • DOI 10.1016/S0968-0004(99)01485-1, PII S0968000499014851
    • Song, Z. W., and Steiler, H. (1999) Death by design: Mechanism and control, of apoptosis. Trends Biochem. Sci. 24, M49-M52. (Pubitemid 30009425)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.12
    • Song, Z.1    Steller, H.2
  • 4
    • 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. J., Morgan, D. G., Heuser, J. E., Wang, X. D., 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
  • 5
    • 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. S., Lutschg, A., and Wang, X. D. (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
  • 6
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • 6. Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., and Wang, X. D. (1997) Cytochrome c and dATPdependent formation of Apaf-l/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489. (Pubitemid 27508237)
    • (1997) Cell , vol.91 , Issue.4 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 7
    • 0032509354 scopus 로고    scopus 로고
    • WD-40 repeat region regulates Apaf-1. self-association and procaspase-9 activation
    • Hu, Y. M., Ding, L. Y., Spencer, D. M., and Nunez, G. (1998) WD-40 repeat region regulates Apaf-1. self-association and procaspase-9 activation. J. Biol. Chem. 273, 33489-33494.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33489-33494
    • Hu, Y.M.1    Ding, L.Y.2    Spencer, D.M.3    Nunez, G.4
  • 8
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1·cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou, H., Li, Y. C., Liu, H. S., and Wang, X. D. (1999) An APAF-1 center dot cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J. Biol. Chem. 274, 11549-11.556. (Pubitemid 129518401)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.17 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 9
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • DOI 10.1038/35004029
    • Goldstein, J. C., Waterhouse, N. J., Juin, P., Evan, G. I., and Green, D. R. (2000) The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant, Nat. Cell Biol. 2,156-162. (Pubitemid 30781130)
    • (2000) Nature Cell Biology , vol.2 , Issue.3 , pp. 156-162
    • Goldstein, J.C.1    Waterhouse, N.J.2    Juin, P.3    Evan, G.I.4    Green, D.R.5
  • 10
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. D. (2001) The expanding role of mitochondria in apoptosis. Genes Dev. 15, 2922-2933.
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.D.1
  • 11
    • 0034613302 scopus 로고    scopus 로고
    • Cytochrome c promotescaspase9 activation by inducing nucleotide binding to Apaf-1
    • Jiang, X. J., and Wang, X. D. (2000) Cytochrome c promotescaspase9 activation by inducing nucleotide binding to Apaf-1. J. Biol. Chem. 275, 31199-31203.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31199-31203
    • Jiang, X.J.1    Wang, X.D.2
  • 12
    • 27644505459 scopus 로고    scopus 로고
    • Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1
    • DOI 10.1073/pnas.0507900102
    • Kim, H. E., Du, F. H., Fang, M., and Wang, X. D. (2005) Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1. Proc. Natl. Acad. Sci. U.S.A. 102, 17545-17550. (Pubitemid 41803534)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.49 , pp. 17545-17550
    • Kim, H.-E.1    Du, F.2    Fang, M.3    Wang, X.4
  • 13
    • 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
  • 14
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry, N. A., and Lazebnik, Y. (1998) Caspases: Enemies within. Science 281, 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 15
    • 0033783289 scopus 로고    scopus 로고
    • Fifteen years of prothymosin a: Contradictory past and new horizons
    • Pineiro, A., Cordero, O. J., and Nogueira, M. (2000) Fifteen years of prothymosin a: Contradictory past and new horizons. Peptides 21, 1433-1446.
    • (2000) Peptides , vol.21 , pp. 1433-1446
    • Pineiro, A.1    Cordero, O.J.2    Nogueira, M.3
  • 17
    • 0024340627 scopus 로고
    • The expression of prothymosin α gene in T lymphocytes and leukemic lymphoid cells is tied to lymphocyte proliferation
    • Gomezmarquez, J., Segade, F., Dosil, M., Pichel, J. G., Bustelo, X. R., and Freire, M. (1989) The Expression, of Prothymosin α-Gene in Lymphocytes-T and Leukemic Lymphoid-Cells Is Tied to Lymphocyte-Proliferation. J. Biol. Chem. 264, 8451-8454. (Pubitemid 19151549)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.15 , pp. 8451-8454
    • Gomez-Marquez, J.1    Segade, F.2    Dosil, M.3    Pichel, J.G.4    Bustelo, X.R.5    Freire, M.6
  • 19
    • 0033942157 scopus 로고    scopus 로고
    • Modulation of histone acetyltransferase activity through interaction of Epstein-Barr nuclear antigen 3C with prothymosin a
    • Cotter, M. A., and Robertson, E. S. (2000) Modulation of histone acetyltransferase activity through interaction of Epstein-Barr nuclear antigen 3C with prothymosin a. Mol. Cell. Biol. 20, 5722-5735.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5722-5735
    • Cotter, M.A.1    Robertson, E.S.2
  • 20
    • 0036245548 scopus 로고    scopus 로고
    • Prothymosin α interacts with the CREB-binding protein and potentiates transcription
    • DOI 10.1093/embo-reports/kvf071
    • Karetsou, Z., Kretsovali, A., Murphy, C., Tsolas, O., and Papamarcaki, T. (2002) Prothymosin a interacts with the CREB-binding protein and potentiates transcription. EMBO Rep. 3, 361-366. (Pubitemid 34467607)
    • (2002) EMBO Reports , vol.3 , Issue.4 , pp. 361-366
    • Karetsou, Z.1    Kretsovali, A.2    Murphy, C.3    Tsolas, O.4    Papamarcaki, T.5
  • 22
    • 8844283395 scopus 로고    scopus 로고
    • Prothymosin α associates with the oncoprotein SET and is involved in chromatin decondensation
    • DOI 10.1016/j.febslet.2004.09.091, PII S0014579304013092
    • Karetsou, Z., Marts, G., Tavoulari, S., Christoforidis, S., Wilm, M., Grass, C., and Papamarcaki, T. (2004) Prothymosin a associates with the oncoprotein SET and is involved in chromatin decondensation. FEBS Lett. 577, 496-500. (Pubitemid 39535337)
    • (2004) FEBS Letters , vol.577 , Issue.3 , pp. 496-500
    • Karetsou, Z.1    Martic, G.2    Tavoulari, S.3    Christoforidis, S.4    Wilm, M.5    Gruss, C.6    Papamarcaki, T.7
  • 25
    • 0037428217 scopus 로고    scopus 로고
    • Distinctive roles of PHAP proteins and prothymosin-α in a death regulatory pathway
    • DOI 10.1126/science.1076807
    • Jiang, X, J., Kim, H. E., Shu, H. J., Zhao, Y. M., Zhang, H. C., Kofron, J., Donnelly, J., Burns, D., Ng, S. C., Rosenberg, S., and Wang, X. D. (2003) Distinctive roles of PHAP proteins and prothymosin-a in a death regulatory pathway. Science 299, 223-226. (Pubitemid 36125203)
    • (2003) Science , vol.299 , Issue.5604 , pp. 223-226
    • Jiang, X.1    Kim, H.-E.2    Shu, H.3    Zhao, Y.4    Zhang, H.5    Kofron, J.6    Donnelly, J.7    Burns, D.8    Ng, S.-C.9    Rosenberg, S.10    Wang, X.11
  • 26
    • 43049147998 scopus 로고    scopus 로고
    • PHAPI, CAS, and Hsp70 promote apoptosome formation by preventing Apaf-1 aggregation and enhancing nucleotide exchange on Apaf-1
    • Kim, H. E., Jiang, X. J., Du, F. H., and Wang, X. D. (2008) PHAPI, CAS, and Hsp70 promote apoptosome formation by preventing Apaf-1 aggregation and enhancing nucleotide exchange on Apaf-1. Mol- Cell 30, 239-247.
    • (2008) Mol- Cell , vol.30 , pp. 239-247
    • Kim, H.E.1    Jiang, X.J.2    Du, F.H.3    Wang, X.D.4
  • 27
    • 36048990877 scopus 로고    scopus 로고
    • Effects of zinc binding on the structure and dynamics of the intrinsically disordered protein prothymosin α: Evidence for metalation as an entropic switch
    • DOI 10.1021/bi7014822
    • Yi, S. L., Boys, B. L., Brickenden, A., Konermann, L., and Choy, W. Y. (2007) Effects of zinc binding on the structure and dynamics of the intrinsically disordered protein prothymosin a: Evidence for metalation as an entropie switch, Biochemistry 46,13120-13130. (Pubitemid 350089907)
    • (2007) Biochemistry , vol.46 , Issue.45 , pp. 13120-13130
    • Yi, S.1    Boys, B.L.2    Brickenden, A.3    Konermann, L.4    Choy, W.-Y.5
  • 28
    • 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. S., Kim, C. N., Yang, J., Jemmerson, R., and Wang, X. D. (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
  • 31
    • 0030716768 scopus 로고    scopus 로고
    • The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
    • DOI 10.1038/40159
    • Matilla, A., Koshy, B. T., Cummings, C., Isobe, T., Orr, H. T., and Zoghbi, H. Y. (1997) The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1. Nature 389, 974-978. (Pubitemid 27485689)
    • (1997) Nature , vol.389 , Issue.6654 , pp. 974-978
    • Matilla, A.1    Koshy, B.T.2    Cummings, C.J.3    Isobe, T.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 32
    • 0031401988 scopus 로고    scopus 로고
    • Cloning and characterization of a new silver-stainable protein SSP29, a member of the LRR family
    • Zhu, L. J., Perlaky, L., Henning, D., and Valdez, B. C. (1997) Cloning and characterization of a new silver-stainable protein SSP29, a member of the LRR family. Biol. Mol. Biol. Int. 42, 927-935. (Pubitemid 28297584)
    • (1997) Biochemistry and Molecular Biology International , vol.42 , Issue.5 , pp. 927-935
    • Zhu, L.1    Perlaky, L.2    Henning, D.3    Valdez, B.C.4
  • 34
    • 0033575254 scopus 로고    scopus 로고
    • Identification of sequences required for inhibition of oncogene-mediated transformation by pp32
    • Brody, J. R., Kadkol, S. S., Mahmoud, M. A., Rebel, J. M. J., and Pasternack, G. R. (1999) Identification of sequences required for inhibition of oncogene-mediated transformation by pp32. J. Biol. Chem. 274, 20053-20055. (Pubitemid 129519464)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.29 , pp. 20053-20055
    • Brody, J.R.1    Kadkol, S.S.2    Mahmoud, M.A.3    Rebel, J.M.J.4    Pasternack, G.R.5
  • 35
    • 0029665228 scopus 로고    scopus 로고
    • 1(PP2A), a novel potent heat-stable inhibitor protein of protein phosphatase 2A
    • DOI 10.1021/bi960581y
    • Li, M., Makkinje, A., and Damuni, Z. (1996) Molecular identification of I-1(PP2A), a novel potent heat-stable inhibitor protein of protein phosphatase 2A. Biochemistry 35, 6998-7002. (Pubitemid 26182088)
    • (1996) Biochemistry , vol.35 , Issue.22 , pp. 6998-7002
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 36
    • 0035846894 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein
    • DOI 10.1016/S0092-8674(01)00196-9
    • Seo, S. B., McNamara, P., Heo, S., Turner, A., Lane, W. S., and Chakravarti, D. (2001) Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein, Cell 104, 119-130. (Pubitemid 32144977)
    • (2001) Cell , vol.104 , Issue.1 , pp. 119-130
    • Seo, S.-B.1    McNamara, P.2    Heo, S.3    Turner, A.4    Lane, W.S.5    Chakravarti, D.6
  • 39
    • 0026099022 scopus 로고
    • The MYC protein activates transcription of the α-prothymosin gene
    • Eilers, M., Schirm, S., and Bishop, J. M. (1991) The Myc Protein Activates Transcription of the α-Prothymosin Gene. EMBO J. 10, 133-141. (Pubitemid 21905275)
    • (1991) EMBO Journal , vol.10 , Issue.1 , pp. 133-141
    • Eilers, M.1    Schirm, S.2    Bishop, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.