메뉴 건너뛰기




Volumn 586, Issue 11, 2012, Pages 1612-1616

X-linked inhibitor of apoptosis protein mediates neddylation by itself but does not function as a NEDD8-E3 ligase for caspase-7

Author keywords

Caspase 7; E3 ligase; NEDD8; Ubiquitin; XIAP

Indexed keywords

CASPASE 7; NEDD8 PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; X LINKED INHIBITOR OF APOPTOSIS;

EID: 84861623915     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.04.056     Document Type: Article
Times cited : (16)

References (33)
  • 3
    • 2642689658 scopus 로고    scopus 로고
    • Proteases to die for
    • V. Cryns, and J. Yuan Proteases to die for Genes Dev. 12 1998 1551 1570
    • (1998) Genes Dev. , vol.12 , pp. 1551-1570
    • Cryns, V.1    Yuan, J.2
  • 4
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • N.A. Thornberry, and Y. Lazebnik Caspases: enemies within Science 281 1998 1312 1316
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 5
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • W.C. Earnshaw, L.M. Martins, and S.H. Kaufmann Mammalian caspases: structure, activation, substrates, and functions during apoptosis Annu. Rev. Biochem. 68 1999 383 424
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 6
    • 0037184113 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro
    • M. MacFarlane, W. Merrison, S.B. Bratton, and G.M. Cohen Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro J. Biol. Chem. 277 2002 36611 36616
    • (2002) J. Biol. Chem. , vol.277 , pp. 36611-36616
    • MacFarlane, M.1    Merrison, W.2    Bratton, S.B.3    Cohen, G.M.4
  • 7
    • 17044368875 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis functions as ubiquitin ligase toward mature caspase-9 and cytosolic Smac/DIABLO
    • Y. Morizane, R. Honda, K. Fukami, and H. Yasuda X-linked inhibitor of apoptosis functions as ubiquitin ligase toward mature caspase-9 and cytosolic Smac/DIABLO J. Biochem. 137 2005 125 132
    • (2005) J. Biochem. , vol.137 , pp. 125-132
    • Morizane, Y.1    Honda, R.2    Fukami, K.3    Yasuda, H.4
  • 8
    • 3042555866 scopus 로고    scopus 로고
    • Smac/Diablo antagonizes ubiquitin ligase activity of inhibitor of apoptosis proteins
    • E.M. Creagh, B.M. Murphy, P.J. Duriez, C.S. Duckett, and S.J. Martin Smac/Diablo antagonizes ubiquitin ligase activity of inhibitor of apoptosis proteins J. Biol. Chem. 279 2004 26906 26914
    • (2004) J. Biol. Chem. , vol.279 , pp. 26906-26914
    • Creagh, E.M.1    Murphy, B.M.2    Duriez, P.J.3    Duckett, C.S.4    Martin, S.J.5
  • 9
    • 0035902601 scopus 로고    scopus 로고
    • Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death
    • Y. Suzuki, Y. Nakabayashi, and R. Takahashi Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death Proc. Natl. Acad. Sci. U S A 98 2001 8662 8667
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 10
    • 0041842553 scopus 로고    scopus 로고
    • Preservation of caspase-3 subunits from degradation contributes to apoptosis evoked by lactacystin: Any single lysine or lysine pair of the small subunit is sufficient for ubiquitination
    • L. Chen, L. Smith, Z. Wang, and J.B. Smith Preservation of caspase-3 subunits from degradation contributes to apoptosis evoked by lactacystin: any single lysine or lysine pair of the small subunit is sufficient for ubiquitination Mol. Pharmacol. 64 2003 334 345
    • (2003) Mol. Pharmacol. , vol.64 , pp. 334-345
    • Chen, L.1    Smith, L.2    Wang, Z.3    Smith, J.B.4
  • 11
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • Y. Yang, S. Fang, J.P. Jensen, A.M. Weissman, and J.D. Ashwell Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli Science 288 2000 874 877
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 12
    • 0027165193 scopus 로고
    • Cloning of a cDNA which encodes a novel ubiquitin-like protein
    • S. Kumar, Y. Yoshida, and M. Noda Cloning of a cDNA which encodes a novel ubiquitin-like protein Biochem. Biophys. Res. Commun. 195 1993 393 399
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 393-399
    • Kumar, S.1    Yoshida, Y.2    Noda, M.3
  • 13
    • 0030695339 scopus 로고    scopus 로고
    • Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein
    • T. Kamitani, K. Kito, H.P. Nguyen, and E.T. Yeh Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein J. Biol. Chem. 272 1997 28557 28562
    • (1997) J. Biol. Chem. , vol.272 , pp. 28557-28562
    • Kamitani, T.1    Kito, K.2    Nguyen, H.P.3    Yeh, E.T.4
  • 15
    • 0033597126 scopus 로고    scopus 로고
    • Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway
    • L. Gong, and E.T. Yeh Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway J. Biol. Chem. 274 1999 12036 12042
    • (1999) J. Biol. Chem. , vol.274 , pp. 12036-12042
    • Gong, L.1    Yeh, E.T.2
  • 20
    • 1842591241 scopus 로고    scopus 로고
    • Nedd8 on cullin: Building an expressway to protein destruction
    • Z.Q. Pan, A. Kentsis, D.C. Dias, K. Yamoah, and K. Wu Nedd8 on cullin: building an expressway to protein destruction Oncogene 23 2004 1985 1997
    • (2004) Oncogene , vol.23 , pp. 1985-1997
    • Pan, Z.Q.1    Kentsis, A.2    Dias, D.C.3    Yamoah, K.4    Wu, K.5
  • 21
    • 3142570737 scopus 로고    scopus 로고
    • Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity
    • D.P. Xirodimas, M.K. Saville, J.C. Bourdon, R.T. Hay, and D.P. Lane Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity Cell 118 2004 83 97
    • (2004) Cell , vol.118 , pp. 83-97
    • Xirodimas, D.P.1    Saville, M.K.2    Bourdon, J.C.3    Hay, R.T.4    Lane, D.P.5
  • 22
    • 1842557655 scopus 로고    scopus 로고
    • PVHL modification by NEDD8 is required for fibronectin matrix assembly and suppression of tumor development
    • N.H. Stickle, J. Chung, J.M. Klco, R.P. Hill, W.G. Kaelin Jr., and M. Ohh PVHL modification by NEDD8 is required for fibronectin matrix assembly and suppression of tumor development Mol. Cell. Biol. 24 2004 3251 3261
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3251-3261
    • Stickle, N.H.1    Chung, J.2    Klco, J.M.3    Hill, R.P.4    Kaelin, Jr.W.G.5    Ohh, M.6
  • 23
    • 33845920314 scopus 로고    scopus 로고
    • Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function
    • I.R. Watson, A. Blanch, D.C. Lin, M. Ohh, and M.S. Irwin Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function J. Biol. Chem. 281 2006 34096 34103
    • (2006) J. Biol. Chem. , vol.281 , pp. 34096-34103
    • Watson, I.R.1    Blanch, A.2    Lin, D.C.3    Ohh, M.4    Irwin, M.S.5
  • 24
    • 33749173298 scopus 로고    scopus 로고
    • Neddylation of a breast cancer-associated protein recruits a class III histone deacetylase that represses NFkappaB-dependent transcription
    • F. Gao, J. Cheng, T. Shi, and E.T. Yeh Neddylation of a breast cancer-associated protein recruits a class III histone deacetylase that represses NFkappaB-dependent transcription Nat. Cell Biol. 8 2006 1171 1177
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1171-1177
    • Gao, F.1    Cheng, J.2    Shi, T.3    Yeh, E.T.4
  • 26
    • 70449697971 scopus 로고    scopus 로고
    • Regulation of nucleolar signalling to p53 through NEDDylation of L11
    • A. Sundqvist, G. Liu, A. Mirsaliotis, and D.P. Xirodimas Regulation of nucleolar signalling to p53 through NEDDylation of L11 Embo Rep. 10 2009 1132 1139
    • (2009) Embo Rep. , vol.10 , pp. 1132-1139
    • Sundqvist, A.1    Liu, G.2    Mirsaliotis, A.3    Xirodimas, D.P.4
  • 27
    • 79953170581 scopus 로고    scopus 로고
    • Hypoxia-inducible factor α subunit stabilization by NEDD8 conjugation is reactive oxygen species-dependent
    • J.H. Ryu, S.H. Li, H.S. Park, J.W. Park, B. Lee, and Y.S. Chun Hypoxia-inducible factor α subunit stabilization by NEDD8 conjugation is reactive oxygen species-dependent J. Biol. Chem. 286 2011 6963 6970
    • (2011) J. Biol. Chem. , vol.286 , pp. 6963-6970
    • Ryu, J.H.1    Li, S.H.2    Park, H.S.3    Park, J.W.4    Lee, B.5    Chun, Y.S.6
  • 28
    • 77951073143 scopus 로고    scopus 로고
    • NUB1 promotes cytoplasmic localization of p53 through cooperation of the NEDD8 and ubiquitin pathways
    • G. Liu, and D.P. Xirodimas NUB1 promotes cytoplasmic localization of p53 through cooperation of the NEDD8 and ubiquitin pathways Oncogene 29 2010 2252 2261
    • (2010) Oncogene , vol.29 , pp. 2252-2261
    • Liu, G.1    Xirodimas, D.P.2
  • 30
    • 84862908377 scopus 로고    scopus 로고
    • Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes
    • R. Hjerpe, Y. Thomas, J. Chen, A. Zemla, S. Curran, N. Shpiro, L.R. Dick, and T. Kurz Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes Biochem. J. 441 2012 927 936
    • (2012) Biochem. J. , vol.441 , pp. 927-936
    • Hjerpe, R.1    Thomas, Y.2    Chen, J.3    Zemla, A.4    Curran, S.5    Shpiro, N.6    Dick, L.R.7    Kurz, T.8
  • 31
    • 12544256390 scopus 로고    scopus 로고
    • Nuclear translocation of caspase-3 is dependent on its proteolytic activation and recognition of a substrate-like protein(s)
    • S. Kamada, U. Kikkawa, Y. Tsujimoto, and T. Hunter Nuclear translocation of caspase-3 is dependent on its proteolytic activation and recognition of a substrate-like protein(s) J. Biol. Chem. 280 2005 857 860
    • (2005) J. Biol. Chem. , vol.280 , pp. 857-860
    • Kamada, S.1    Kikkawa, U.2    Tsujimoto, Y.3    Hunter, T.4
  • 32
    • 79953321047 scopus 로고    scopus 로고
    • Contribution of caspase(s) to the cell cycle regulation at mitotic phase
    • T. Hashimoto, U. Kikkawa, and S. Kamada Contribution of caspase(s) to the cell cycle regulation at mitotic phase PLoS ONE 6 2011 e18449
    • (2011) PLoS ONE , vol.6 , pp. 18449
    • Hashimoto, T.1    Kikkawa, U.2    Kamada, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.