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Volumn 309, Issue 3, 2003, Pages 520-527

Identification of a Bcl-XL binding region within the ATPase domain of Apaf-1

Author keywords

Apaf 1; Apoptosis; Bcl XL; CED 4; CED 9; Direct binding; Immunoprecipitation; Two hybrid system

Indexed keywords

ADENOSINE TRIPHOSPHATASE; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; COMPLEMENTARY DNA; PROTEIN; PROTEIN BCL XL; PROTEIN CED 4; UNCLASSIFIED DRUG; APAF1 PROTEIN, HUMAN; BCL2L1 PROTEIN, HUMAN; CAENORHABDITIS ELEGANS PROTEIN; CALCIUM BINDING PROTEIN; CED 4 PROTEIN, C ELEGANS; CED-4 PROTEIN, C ELEGANS; PROTEIN BCL 2; PROTEIN BCL X;

EID: 0042330448     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.08.030     Document Type: Article
Times cited : (12)

References (47)
  • 1
    • 0022497852 scopus 로고
    • Genetic control of programmed cell death in the nematode C. elegans
    • Ellis H.M., Horvitz H.R. Genetic control of programmed cell death in the nematode C. elegans. Cell. 44:1986;817-829.
    • (1986) Cell , vol.44 , pp. 817-829
    • Ellis, H.M.1    Horvitz, H.R.2
  • 2
    • 0026582702 scopus 로고
    • Caenorhabditis elegans gene ced-9 protects cells from programmed cell death
    • Hengartner M.O., Ellis R.E., Horvitz H.R. Caenorhabditis elegans gene ced-9 protects cells from programmed cell death. Nature. 356:1992;494-499.
    • (1992) Nature , vol.356 , pp. 494-499
    • Hengartner, M.O.1    Ellis, R.E.2    Horvitz, H.R.3
  • 3
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • Yuan J., Shaham S., Ledoux S., Ellis H.M., Horvitz H.R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell. 75:1993;641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 5
    • 0031194404 scopus 로고    scopus 로고
    • Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3- induced apoptosis
    • Seshagiri S., Miller L.K. Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3- induced apoptosis. Curr. Biol. 7:1997;455-460.
    • (1997) Curr. Biol. , vol.7 , pp. 455-460
    • Seshagiri, S.1    Miller, L.K.2
  • 6
    • 0031019739 scopus 로고    scopus 로고
    • Interaction between the C. elegans cell-death regulators CED-9 and CED-4
    • Spector M.S., Desnoyers S., Hoeppner D.J., Hengartner M.O. Interaction between the C. elegans cell-death regulators CED-9 and CED-4. Nature. 385:1997;653-656.
    • (1997) Nature , vol.385 , pp. 653-656
    • Spector, M.S.1    Desnoyers, S.2    Hoeppner, D.J.3    Hengartner, M.O.4
  • 7
    • 0031034997 scopus 로고    scopus 로고
    • Interaction of CED-4 with CED-3 and CED-9: A molecular framework for cell death
    • Chinnaiyan A.M., O'Rourke K., Lane B.R., Dixit V.M. Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death. Science. 275:1997;1122-1126.
    • (1997) Science , vol.275 , pp. 1122-1126
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Lane, B.R.3    Dixit, V.M.4
  • 8
    • 0031020227 scopus 로고    scopus 로고
    • Interaction and regulation of subcellular localization of CED-4 by CED-9
    • Wu D., Wallen H.D., Nunez G. Interaction and regulation of subcellular localization of CED-4 by CED-9. Science. 275:1997;1126-1129.
    • (1997) Science , vol.275 , pp. 1126-1129
    • Wu, D.1    Wallen, H.D.2    Nunez, G.3
  • 11
    • 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
    • Zou H., Henzel W.J., Liu X., Lutschg A., Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell. 90:1997;405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 12
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams J.M., Cory S. The Bcl-2 protein family: arbiters of cell survival. Science. 281:1998;1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 13
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X., Kim C.N., Yang J., Jemmerson R., Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell. 86:1996;147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 16
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 91:1997;479-489.
    • (1997) Cell , vol.91 , 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
  • 18
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1 · cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou H., Li Y., Liu X., Wang X. An APAF-1. · cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9 J. Biol. Chem. 274:1999;11549-11556.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 19
    • 0033529634 scopus 로고    scopus 로고
    • Caspase activation involves the formation of the aposome, a large (∼700 kDa) caspase-activating complex
    • Cain K., Brown D.G., Langlais C., Cohen G.M. Caspase activation involves the formation of the aposome, a large (∼700. kDa) caspase-activating complex J. Biol. Chem. 274:1999;22686-22692.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22686-22692
    • Cain, K.1    Brown, D.G.2    Langlais, C.3    Cohen, G.M.4
  • 20
    • 0034105784 scopus 로고    scopus 로고
    • Apaf-1 oligomerizes into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexes
    • Cain K., Bratton S.B., Langlais C., Walker G., Brown D.G., Sun X.M., Cohen G.M. Apaf-1 oligomerizes into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexes. J. Biol. Chem. 275:2000;6067-6070.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6067-6070
    • Cain, K.1    Bratton, S.B.2    Langlais, C.3    Walker, G.4    Brown, D.G.5    Sun, X.M.6    Cohen, G.M.7
  • 22
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R.M., Bossy-Wetzel E., Green D.R., Newmeyer D.D. The release of cytochrome. c from mitochondria: a primary site for Bcl-2 regulation of apoptosis Science. 275:1997;1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 23
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., Reed J.C. Mitochondria and apoptosis. Science. 281:1998;1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 26
    • 0033578303 scopus 로고    scopus 로고
    • Bcl-2 family members do not inhibit apoptosis by binding the caspase activator apaf-1
    • Moriishi K., Huang D.C.S., Cory S., Adams J.M. Bcl-2 family members do not inhibit apoptosis by binding the caspase activator apaf-1. Proc. Natl. Acad. Sci. USA. 96:1999;9683-9688.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9683-9688
    • Moriishi, K.1    Huang, D.C.S.2    Cory, S.3    Adams, J.M.4
  • 29
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:1982;945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 30
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A., McDonnell J.M., Korsmeyer S.J. BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 13:1999;1899-1911.
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 31
    • 0031442184 scopus 로고    scopus 로고
    • Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy
    • Iwahashi H., Eguchi Y., Yasuhara N., Hanafusa T., Matsuzawa Y., Tsujimoto Y. Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy. Nature. 390:1997;413-417.
    • (1997) Nature , vol.390 , pp. 413-417
    • Iwahashi, H.1    Eguchi, Y.2    Yasuhara, N.3    Hanafusa, T.4    Matsuzawa, Y.5    Tsujimoto, Y.6
  • 32
    • 0001003612 scopus 로고    scopus 로고
    • Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members
    • Hsu S.Y., Kaipia A., McGee E., Lomeli M., Hsueh A.J. Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members. Proc. Natl. Acad. Sci. USA. 94:1997;12401-12406.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12401-12406
    • Hsu, S.Y.1    Kaipia, A.2    McGee, E.3    Lomeli, M.4    Hsueh, A.J.5
  • 33
    • 0344348821 scopus 로고    scopus 로고
    • Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis
    • Hu Y., Benedict M.A., Ding L., Nunez G. Role of cytochrome. c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis EMBO J. 18:1999;3586-3595.
    • (1999) EMBO J. , vol.18 , pp. 3586-3595
    • Hu, Y.1    Benedict, M.A.2    Ding, L.3    Nunez, G.4
  • 34
    • 0034708504 scopus 로고    scopus 로고
    • Expression and functional analysis of Apaf-1 isoforms. Extra WD-40 repeat is required for cytochrome c binding and regulated activation of procaspase-9
    • Benedict M.A., Hu Y., Inohara N., Nunez G. Expression and functional analysis of Apaf-1 isoforms. Extra WD-40 repeat is required for cytochrome. c binding and regulated activation of procaspase-9 J. Biol. Chem. 275:2000;8461-8468.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8461-8468
    • Benedict, M.A.1    Hu, Y.2    Inohara, N.3    Nunez, G.4
  • 36
    • 0033193863 scopus 로고    scopus 로고
    • Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an evolutionarily conserved death pathway
    • Rodriguez A., Oliver H., Zou H., Chen P., Wang X., Abrams J.M. Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an evolutionarily conserved death pathway. Nat. Cell Biol. 1:1999;272-279.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 272-279
    • Rodriguez, A.1    Oliver, H.2    Zou, H.3    Chen, P.4    Wang, X.5    Abrams, J.M.6
  • 37
    • 0033231548 scopus 로고    scopus 로고
    • HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis
    • Zhou L., Song Z., Tittel J., Steller H. HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis. Mol. Cell. 4:1999;745-755.
    • (1999) Mol. Cell , vol.4 , pp. 745-755
    • Zhou, L.1    Song, Z.2    Tittel, J.3    Steller, H.4
  • 38
    • 0033231614 scopus 로고    scopus 로고
    • Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator
    • Kanuka H., Sawamoto K., Inohara N., Matsuno K., Okano H., Miura M. Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator. Mol. Cell. 4:1999;757-769.
    • (1999) Mol. Cell , vol.4 , pp. 757-769
    • Kanuka, H.1    Sawamoto, K.2    Inohara, N.3    Matsuno, K.4    Okano, H.5    Miura, M.6
  • 41
    • 0035895992 scopus 로고    scopus 로고
    • Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-κB
    • Ogura Y., Inohara N., Benito A., Chen F.F., Yamaoka S., Nunez G. Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-κB. J. Biol. Chem. 276:2000;4812-4818.
    • (2000) J. Biol. Chem. , vol.276 , pp. 4812-4818
    • Ogura, Y.1    Inohara, N.2    Benito, A.3    Chen, F.F.4    Yamaoka, S.5    Nunez, G.6
  • 42
    • 0035937775 scopus 로고    scopus 로고
    • Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins
    • Hlaing T., Guo R.F., Dilley K.A., Loussia J.M., Morrish T.A., Shi M.M., Vincenz C., Ward P.A. Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins. J. Biol. Chem. 276:2001;9230-9238.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9230-9238
    • Hlaing, T.1    Guo, R.F.2    Dilley, K.A.3    Loussia, J.M.4    Morrish, T.A.5    Shi, M.M.6    Vincenz, C.7    Ward, P.A.8
  • 43
    • 0035854790 scopus 로고    scopus 로고
    • L blocks transforming growth factor-β1-induced apoptosis by inhibiting cytochrome c release and not by directly antagonizing Apaf-1-dependent caspase activation in prostate epithelial cells
    • L blocks transforming growth factor-β1-induced apoptosis by inhibiting cytochrome. c release and not by directly antagonizing Apaf-1-dependent caspase activation in prostate epithelial cells J. Biol. Chem. 276:2001;26614-26621.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26614-26621
    • Chipuk, J.E.1    Bhat, M.2    Hsing, A.Y.3    Ma, J.4    Danielpour, D.5
  • 47
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • Acehan D., Jiang X., Morgan D.G., Heuser J.E., Wang X., Akey C.W. Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation. Mol. Cell. 9:2002;423-432.
    • (2002) Mol. Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6


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