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Volumn 331, Issue 4, 2005, Pages 1007-1015

Caspase recruitment domain of procaspase-2 could be a target for SUMO-1 modification through Ubc9

Author keywords

Apoptosis; Caspase 2; Dot like structure; Nuclear localization; SUMO 1; Ubc9

Indexed keywords

CASPASE; CYSTEINE PROTEINASE; PROCASPASE 2; PROTEIN SUBUNIT; PROTEIN UBC9; SUMO 1 PROTEIN; UNCLASSIFIED DRUG;

EID: 18844450183     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.04.019     Document Type: Article
Times cited : (18)

References (47)
  • 1
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • M.P. Boldin, T.M. Goncharov, Y.V. Goltsev, and D. Wallach Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death Cell 85 1996 803 815
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 3
    • 0030954209 scopus 로고    scopus 로고
    • The CARD domain: A new apoptotic signalling motif
    • K. Hofmann, P. Bucher, and J. Tschopp The CARD domain: a new apoptotic signalling motif Trends Biochem. Sci. 22 1997 155 156
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 155-156
    • Hofmann, K.1    Bucher, P.2    Tschopp, J.3
  • 4
    • 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
    • H. Zou, W.J. Henzel, X. Liu, A. Lutschg, and X. Wang 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
  • 5
    • 0031615875 scopus 로고    scopus 로고
    • Autoproteolytic activation of pro-caspases by oligomerization
    • X. Yang, H.Y. Chang, and D. Baltimore Autoproteolytic activation of pro-caspases by oligomerization Mol. Cell 1 1998 319 325
    • (1998) Mol. Cell , vol.1 , pp. 319-325
    • Yang, X.1    Chang, H.Y.2    Baltimore, D.3
  • 6
    • 0032548842 scopus 로고    scopus 로고
    • Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal
    • D.A. Martin, R.M. Siegel, L. Zheng, and M.J. Lenardo Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal J. Biol. Chem. 273 1998 4345 4349
    • (1998) J. Biol. Chem. , vol.273 , pp. 4345-4349
    • Martin, D.A.1    Siegel, R.M.2    Zheng, L.3    Lenardo, M.J.4
  • 8
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • M. Enari, H. Sakahira, H. Yokoyama, K. Okawa, A. Iwamatsu, and S. Nagata A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD Nature 391 1998 43 50
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 9
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • H. Sakahira, M. Enari, and S. Nagata Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis Nature 391 1998 96 99
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 10
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Y.A. Lazebnik, S.H. Kaufmann, S. Desnoyers, G.G. Poirier, and W.C. Earnshaw Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE Nature 371 1994 346 347
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 11
    • 0031106612 scopus 로고    scopus 로고
    • Apoptosis: Alive and kicking in 1997
    • L.M. Martins, and W.C. Earnshaw Apoptosis: alive and kicking in 1997 Trends Cell Biol. 7 1997 111 114
    • (1997) Trends Cell Biol. , vol.7 , pp. 111-114
    • Martins, L.M.1    Earnshaw, W.C.2
  • 13
    • 0033539067 scopus 로고    scopus 로고
    • Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation
    • S. Sahara, M. Aoto, Y. Eguchi, N. Imamoto, Y. Yoneda, and Y. Tsujimoto Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation Nature 401 1999 168 173
    • (1999) Nature , vol.401 , pp. 168-173
    • Sahara, S.1    Aoto, M.2    Eguchi, Y.3    Imamoto, N.4    Yoneda, Y.5    Tsujimoto, Y.6
  • 14
    • 0029832173 scopus 로고    scopus 로고
    • Cleavage of CPP32 by granzyme B represents a critical role for granzyme B in the induction of target cell DNA fragmentation
    • A.J. Darmon, T.J. Ley, D.W. Nicholson, and R.C. Bleackley Cleavage of CPP32 by granzyme B represents a critical role for granzyme B in the induction of target cell DNA fragmentation J. Biol. Chem. 271 1996 21709 21712
    • (1996) J. Biol. Chem. , vol.271 , pp. 21709-21712
    • Darmon, A.J.1    Ley, T.J.2    Nicholson, D.W.3    Bleackley, R.C.4
  • 15
    • 9344261615 scopus 로고    scopus 로고
    • The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism
    • S.J. Martin, G.P. Amarante-Mendes, L. Shi, T.H. Chuang, C.A. Casiano, G.A. O'Brien, P. Fitzgerald, E.M. Tan, G.M. Bokoch, A.H. Greenberg, and D.R. Green The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism EMBO J. 15 1996 2407 2416
    • (1996) EMBO J. , vol.15 , pp. 2407-2416
    • Martin, S.J.1    Amarante-Mendes, G.P.2    Shi, L.3    Chuang, T.H.4    Casiano, C.A.5    O'Brien, G.A.6    Fitzgerald, P.7    Tan, E.M.8    Bokoch, G.M.9    Greenberg, A.H.10    Green, D.R.11
  • 17
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new 'death' adaptor molecule
    • H. Duan, and V.M. Dixit RAIDD is a new 'death' adaptor molecule Nature 385 1997 86 89
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 18
    • 0032515191 scopus 로고    scopus 로고
    • Hypoxia induces apoptosis in human neuroblastoma SK-N-MC cells by caspase activation accompanying cytochrome c release from mitochondria
    • R. Araya, T. Uehara, and Y. Nomura Hypoxia induces apoptosis in human neuroblastoma SK-N-MC cells by caspase activation accompanying cytochrome c release from mitochondria FEBS Lett. 439 1998 168 172
    • (1998) FEBS Lett. , vol.439 , pp. 168-172
    • Araya, R.1    Uehara, T.2    Nomura, Y.3
  • 19
    • 0032955601 scopus 로고    scopus 로고
    • Caspase activation accompanying cytochrome c release from mitochondria is possibly involved in nitric oxide-induced neuronal apoptosis in SH-SY5Y cells
    • T. Uehara, Y. Kikuchi, and Y. Nomura Caspase activation accompanying cytochrome c release from mitochondria is possibly involved in nitric oxide-induced neuronal apoptosis in SH-SY5Y cells J. Neurochem. 72 1999 196 205
    • (1999) J. Neurochem. , vol.72 , pp. 196-205
    • Uehara, T.1    Kikuchi, Y.2    Nomura, Y.3
  • 20
    • 0032719378 scopus 로고    scopus 로고
    • Possible involvement of cytochrome c release and sequential activation of caspases in ceramide-induced apoptosis in SK-N-MC cells
    • A. Ito, T. Uehara, A. Tokumitsu, Y. Okuma, and Y. Nomura Possible involvement of cytochrome c release and sequential activation of caspases in ceramide-induced apoptosis in SK-N-MC cells Biochim. Biophys. Acta 1452 1999 263 274
    • (1999) Biochim. Biophys. Acta , vol.1452 , pp. 263-274
    • Ito, A.1    Uehara, T.2    Tokumitsu, A.3    Okuma, Y.4    Nomura, Y.5
  • 21
    • 0034634441 scopus 로고    scopus 로고
    • Mechanism of nitric oxide-induced apoptosis in human neuroblastoma SH-SY5Y cells
    • R. Moriya, T. Uehara, and Y. Nomura Mechanism of nitric oxide-induced apoptosis in human neuroblastoma SH-SY5Y cells FEBS Lett. 484 2000 252 260
    • (2000) FEBS Lett. , vol.484 , pp. 252-260
    • Moriya, R.1    Uehara, T.2    Nomura, Y.3
  • 23
    • 0035576737 scopus 로고    scopus 로고
    • A new RING for SUMO: Wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases
    • P.K. Jackson A new RING for SUMO: wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases Genes Dev. 15 2001 3053 3058
    • (2001) Genes Dev. , vol.15 , pp. 3053-3058
    • Jackson, P.K.1
  • 24
    • 0036237383 scopus 로고    scopus 로고
    • Versatile protein tag, SUMO: Its enzymology and biological function
    • K.I. Kim, S.H. Baek, and C.H. Chung Versatile protein tag, SUMO: its enzymology and biological function J. Cell Physiol. 191 2002 257 268
    • (2002) J. Cell Physiol. , vol.191 , pp. 257-268
    • Kim, K.I.1    Baek, S.H.2    Chung, C.H.3
  • 25
    • 0037295721 scopus 로고    scopus 로고
    • Modification with SUMO. a role in transcriptional regulation
    • A. Verger, J. Perdomo, and M. Crossley Modification with SUMO. A role in transcriptional regulation EMBO Rep. 4 2003 137 142
    • (2003) EMBO Rep. , vol.4 , pp. 137-142
    • Verger, A.1    Perdomo, J.2    Crossley, M.3
  • 27
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1
    • T. Sternsdorf, K. Jensen, and H. Will Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1 J Cell Biol. 139 1997 1621 1634
    • (1997) J Cell Biol. , vol.139 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 28
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • J.M. Desterro, M.S. Rodriguez, and R.T. Hay SUMO-1 modification of IκBα inhibits NF-κB activation Mol. Cell 2 1998 233 239
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 29
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • S. Muller, M.J. Matunis, and A. Dejean Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus EMBO J. 17 1998 61 70
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 31
    • 0344299239 scopus 로고    scopus 로고
    • Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption
    • S. Muller, and A. Dejean Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption J. Virol. 73 1999 5137 5143
    • (1999) J. Virol. , vol.73 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 32
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • R. Mahajan, C. Delphin, T. Guan, L. Gerace, and F. Melchior A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2 Cell 88 1997 97 107
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 33
    • 0032498541 scopus 로고    scopus 로고
    • SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex
    • M.J. Matunis, J. Wu, and G. Blobel SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex J. Cell Biol. 140 1998 499 509
    • (1998) J. Cell Biol. , vol.140 , pp. 499-509
    • Matunis, M.J.1    Wu, J.2    Blobel, G.3
  • 34
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • S. Zhong, P. Salomoni, and P.P. Pandolfi The transcriptional role of PML and the nuclear body Nat. Cell Biol. 2 2000 E85 E90
    • (2000) Nat. Cell Biol. , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 38
    • 0034737397 scopus 로고    scopus 로고
    • Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity
    • A. Ito, T. Uehara, and Y. Nomura Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity FEBS Lett. 470 2000 360 364
    • (2000) FEBS Lett. , vol.470 , pp. 360-364
    • Ito, A.1    Uehara, T.2    Nomura, Y.3
  • 39
    • 0032985374 scopus 로고    scopus 로고
    • Transient nuclear factor κb (NF-κB) activation stimulated by interleukin-1β may be partly dependent on proteasome activity, but not phosphorylation and ubiquitination of the IκBα molecule, in C6 glioma cells
    • T. Uehara, J. Matsuno, M. Kaneko, T. Nishiya, M. Fujimuro, H. Yokosawa, and Y. Nomura Transient nuclear factor κB (NF-κB) activation stimulated by interleukin-1β may be partly dependent on proteasome activity, but not phosphorylation and ubiquitination of the IκBα molecule, in C6 glioma cells J. Biol. Chem. 274 1999 15875 15882
    • (1999) J. Biol. Chem. , vol.274 , pp. 15875-15882
    • Uehara, T.1    Matsuno, J.2    Kaneko, M.3    Nishiya, T.4    Fujimuro, M.5    Yokosawa, H.6    Nomura, Y.7
  • 40
    • 0034615941 scopus 로고    scopus 로고
    • Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death
    • S. Tanaka, T. Uehara, and Y. Nomura Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death J. Biol. Chem. 275 2000 10388 10393
    • (2000) J. Biol. Chem. , vol.275 , pp. 10388-10393
    • Tanaka, S.1    Uehara, T.2    Nomura, Y.3
  • 41
    • 0037144597 scopus 로고    scopus 로고
    • Role of ubiquitin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death
    • H.S. Ko, T. Uehara, and Y. Nomura Role of ubiquitin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death J. Biol. Chem. 277 2002 35386 35392
    • (2002) J. Biol. Chem. , vol.277 , pp. 35386-35392
    • Ko, H.S.1    Uehara, T.2    Nomura, Y.3
  • 42
    • 0032080337 scopus 로고    scopus 로고
    • Characterization of a second member of the sentrin family of ubiquitin-like proteins
    • T. Kamitani, K. Kito, H.P. Nguyen, T. Fukuda-Kamitani, and E.T. Yeh Characterization of a second member of the sentrin family of ubiquitin-like proteins J. Biol. Chem. 273 1998 11349 11353
    • (1998) J. Biol. Chem. , vol.273 , pp. 11349-11353
    • Kamitani, T.1    Kito, K.2    Nguyen, H.P.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 43
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif
    • A. Minty, X. Dumont, M. Kaghad, and D. Caput Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif J. Biol. Chem. 275 2000 36316 36323
    • (2000) J. Biol. Chem. , vol.275 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3    Caput, D.4
  • 44
    • 0032567759 scopus 로고    scopus 로고
    • Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association
    • R. Mahajan, L. Gerace, and F. Melchior Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association J. Cell Biol. 140 1998 259 270
    • (1998) J. Cell Biol. , vol.140 , pp. 259-270
    • Mahajan, R.1    Gerace, L.2    Melchior, F.3
  • 45
    • 0347790260 scopus 로고    scopus 로고
    • Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1
    • Y.H. Kim, C.Y. Choi, and Y. Kim Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1 Proc. Natl. Acad. Sci. USA 96 1999 12350 12355
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12350-12355
    • Kim, Y.H.1    Choi, C.Y.2    Kim, Y.3
  • 46
    • 0035298087 scopus 로고    scopus 로고
    • Comprehensive studies on subcellular localizations and cell death-inducing activities of eight GFP-tagged apoptosis-related caspases
    • Y. Shikama, M.U.T. Miyashita, and M. Yamada Comprehensive studies on subcellular localizations and cell death-inducing activities of eight GFP-tagged apoptosis-related caspases Exp. Cell Res. 264 2001 315 325
    • (2001) Exp. Cell Res. , vol.264 , pp. 315-325
    • Shikama, Y.1    Miyashita, M.U.T.2    Yamada, M.3
  • 47
    • 0032544397 scopus 로고    scopus 로고
    • Prodomain-dependent nuclear localization of the caspase-2 (Nedd2) precursor. a novel function for a caspase prodomain
    • P.A. Colussi, N.L. Harvey, and S. Kumar Prodomain-dependent nuclear localization of the caspase-2 (Nedd2) precursor. A novel function for a caspase prodomain J. Biol. Chem. 273 1998 24535 24542
    • (1998) J. Biol. Chem. , vol.273 , pp. 24535-24542
    • Colussi, P.A.1    Harvey, N.L.2    Kumar, S.3


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