메뉴 건너뛰기




Volumn 33, Issue 6, 2013, Pages 1114-1123

The COP9 signalosome interacts with and regulates interferon regulatory factor 5 protein stability

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; COP9 SIGNALOSOME; INTERFERON REGULATORY FACTOR 5; PROTEASOME; SMALL INTERFERING RNA; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UBIQUITIN;

EID: 84878780272     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00802-12     Document Type: Article
Times cited : (16)

References (86)
  • 1
    • 77449101221 scopus 로고    scopus 로고
    • Regulation of immunity and oncogenesis by the IRF transcription factor family
    • Savitsky D, Tamura T, Yanai H, Taniguchi T. 2010. Regulation of immunity and oncogenesis by the IRF transcription factor family. Cancer Immunol. Immunother. 59:489 -510.
    • (2010) Cancer Immunol. Immunother. , vol.59 , pp. 489-510
    • Savitsky, D.1    Tamura, T.2    Yanai, H.3    Taniguchi, T.4
  • 2
    • 0035968246 scopus 로고    scopus 로고
    • Virus-specific activation of a novel interferon regulatory factor, IRF-5, results in the induction of distinct interferon alpha genes
    • Barnes BJ, Moore PA, Pitha PM. 2001. Virus-specific activation of a novel interferon regulatory factor, IRF-5, results in the induction of distinct interferon alpha genes. J. Biol. Chem. 276:23382-23390.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23382-23390
    • Barnes, B.J.1    Moore, P.A.2    Pitha, P.M.3
  • 10
    • 0141919557 scopus 로고    scopus 로고
    • Interferon regulatory factor 5, a novel mediator of cell cycle arrest and cell death
    • Barnes BJ, Kellum MJ, Pinder KE, Frisancho JA, Pitha PM. 2003. Interferon regulatory factor 5, a novel mediator of cell cycle arrest and cell death. Cancer Res. 63:6424-6431.
    • (2003) Cancer Res. , vol.63 , pp. 6424-6431
    • Barnes, B.J.1    Kellum, M.J.2    Pinder, K.E.3    Frisancho, J.A.4    Pitha, P.M.5
  • 12
    • 59149091466 scopus 로고    scopus 로고
    • IRF-5 is a mediator of the death receptor-induced apoptotic signaling pathway
    • Hu G.Barnes BJ. 2009. IRF-5 is a mediator of the death receptor-induced apoptotic signaling pathway. J. Biol. Chem. 284:2767-2777.
    • (2009) J. Biol. Chem. , vol.284 , pp. 2767-2777
    • Hu, G.1    Barnes, B.J.2
  • 13
    • 23844463088 scopus 로고    scopus 로고
    • Signaling through IFN regulatory factor-5 sensitizes p53-deficient tumors to DNA damage-induced apoptosis and cell death
    • Hu G, Mancl ME, Barnes BJ. 2005. Signaling through IFN regulatory factor-5 sensitizes p53-deficient tumors to DNA damage-induced apoptosis and cell death. Cancer Res. 65:7403-7412.
    • (2005) Cancer Res. , vol.65 , pp. 7403-7412
    • Hu, G.1    Mancl, M.E.2    Barnes, B.J.3
  • 14
    • 0037171938 scopus 로고    scopus 로고
    • Identification of the interferon regulatory factor 5 gene (IRF-5) as a direct target for p53
    • Mori T, Anazawa Y, Iiizumi M, Fukuda S, Nakamura Y, Arakawa H. 2002. Identification of the interferon regulatory factor 5 gene (IRF-5) as a direct target for p53. Oncogene 21:2914 -2918.
    • (2002) Oncogene , vol.21 , pp. 2914-2918
    • Mori, T.1    Anazawa, Y.2    Iiizumi, M.3    Fukuda, S.4    Nakamura, Y.5    Arakawa, H.6
  • 15
    • 80155157544 scopus 로고    scopus 로고
    • Loss of interferon regulatory factor 5 (IRF5) expression in human ductal carcinoma correlates with disease stage and contributes to metastasis
    • R111 doi:10.1186/bcr3053
    • Bi X, Hameed M, Mirani N, Pimenta EM, Anari J, Barnes BJ. 2011. Loss of interferon regulatory factor 5 (IRF5) expression in human ductal carcinoma correlates with disease stage and contributes to metastasis. Breast Cancer Res. 13:R111. doi:10.1186/bcr3053.
    • (2011) Breast Cancer Res. , vol.13
    • Bi, X.1    Hameed, M.2    Mirani, N.3    Pimenta, E.M.4    Anari, J.5    Barnes, B.J.6
  • 17
    • 20444368020 scopus 로고    scopus 로고
    • Two discrete promoters regulate the alternatively spliced human interferon regulatory factor-5 isoforms. Multiple isoforms with distinct cell type-specific expression, localization, regulation, and function.
    • Mancl ME, Hu G, Sangster-Guity N, Olshalsky SL, Hoops K, Fitzgerald- Bocarsly P, Pitha PM, Pinder K, Barnes BJ. 2005. Two discrete promoters regulate the alternatively spliced human interferon regulatory factor-5 isoforms. Multiple isoforms with distinct cell type-specific expression, localization, regulation, and function. J. Biol. Chem. 280:21078 -21090.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21078-21090
    • Mancl, M.E.1    Hu, G.2    Sangster-Guity, N.3    Olshalsky, S.L.4    Hoops, K.5    Fitzgerald-Bocarsly, P.6    Pitha, P.M.7    Pinder, K.8    Barnes, B.J.9
  • 18
    • 57349121051 scopus 로고    scopus 로고
    • Functional regulation of MyD88-activated interferon regulatory factor 5 by K63-linked polyubiquitination
    • Balkhi MY, Fitzgerald KA, Pitha PM. 2008. Functional regulation of MyD88-activated interferon regulatory factor 5 by K63-linked polyubiquitination. Mol. Cell. Biol. 28:7296 -7308.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 7296-7308
    • Balkhi, M.Y.1    Fitzgerald, K.A.2    Pitha, P.M.3
  • 19
    • 0036311933 scopus 로고    scopus 로고
    • Multiple regulatory domains of IRF-5 control activation, cellular localization, and induction of chemokines that mediate recruitment of T lymphocytes
    • Barnes BJ, Kellum MJ, Field AE, Pitha PM. 2002. Multiple regulatory domains of IRF-5 control activation, cellular localization, and induction of chemokines that mediate recruitment of T lymphocytes. Mol. Cell. Biol. 22:5721-5740.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5721-5740
    • Barnes, B.J.1    Kellum, M.J.2    Field, A.E.3    Pitha, P.M.4
  • 20
    • 84857846174 scopus 로고    scopus 로고
    • Activation of interferon regulatory factor 5 by site specific phosphorylation
    • doi:10.1371/journal.pone.0033098.
    • Chang Foreman HC, Van Scoy S, Cheng TF, Reich NC. 2012. Activation of interferon regulatory factor 5 by site specific phosphorylation. PLoS One 7:e33098. doi:10.1371/journal.pone.0033098.
    • (2012) PLoS One , vol.7
    • Chang Foreman, H.C.1    Van Scoy, S.2    Cheng, T.F.3    Reich, N.C.4
  • 21
    • 33744906762 scopus 로고    scopus 로고
    • Differential activation of IFN regulatory factor (IRF)-3 and IRF-5 transcription factors during viral infection
    • Cheng TF, Brzostek S, Ando O, Van Scoy S, Kumar KP, Reich NC. 2006. Differential activation of IFN regulatory factor (IRF)-3 and IRF-5 transcription factors during viral infection. J. Immunol. 176:7462-7470.
    • (2006) J. Immunol. , vol.176 , pp. 7462-7470
    • Cheng, T.F.1    Brzostek, S.2    Ando, O.3    Van Scoy, S.4    Kumar, K.P.5    Reich, N.C.6
  • 22
    • 78650637976 scopus 로고    scopus 로고
    • Differential requirement of histone acetylase and deacetylase activities for IRF5-mediated proinflammatory cytokine expression
    • Feng D, Sangster-Guity N, Stone R, Korczeniewska J, Mancl ME, Fitzgerald-Bocarsly P, Barnes BJ. 2010. Differential requirement of histone acetylase and deacetylase activities for IRF5-mediated proinflammatory cytokine expression. J. Immunol. 185:6003- 6012.
    • (2010) J. Immunol. , vol.185 , pp. 6003-6012
    • Feng, D.1    Sangster-Guity, N.2    Stone, R.3    Korczeniewska, J.4    Mancl, M.E.5    Fitzgerald-Bocarsly, P.6    Barnes, B.J.7
  • 23
    • 0038608016 scopus 로고    scopus 로고
    • Virus-induced heterodimer formation between IRF-5 and IRF-7 modulates assembly of the IFNA enhanceosome in vivo and transcriptional activity of IFNA genes
    • Barnes BJ Field AE, Pitha-Rowe PM. 2003. Virus-induced heterodimer formation between IRF-5 and IRF-7 modulates assembly of the IFNA enhanceosome in vivo and transcriptional activity of IFNA genes. J. Biol. Chem. 278:16630 -16641.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16630-16641
    • Barnes, B.J.1    Field, A.E.2    Pitha-Rowe, P.M.3
  • 25
    • 13144305043 scopus 로고    scopus 로고
    • The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex
    • Wei N, Tsuge T, Serino G, Dohmae N, Takio K, Matsui M, Deng XW. 1998. The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex. Curr. Biol. 8:919- 922.
    • (1998) Curr. Biol. , vol.8 , pp. 919-922
    • Wei, N.1    Tsuge, T.2    Serino, G.3    Dohmae, N.4    Takio, K.5    Matsui, M.6    Deng, X.W.7
  • 26
    • 0030581153 scopus 로고    scopus 로고
    • The COP9 complex, a novel multisubunit nuclear regulator involved in light control of a plant developmental switch
    • Chamovitz DA, Wei N, Osterlund MT, von Arnim AG, Staub JM, Matsui M, Deng XW. 1996. The COP9 complex, a novel multisubunit nuclear regulator involved in light control of a plant developmental switch. Cell 86:115-121.
    • (1996) Cell , vol.86 , pp. 115-121
    • Chamovitz, D.A.1    Wei, N.2    Osterlund, M.T.3    von Arnim, A.G.4    Staub, J.M.5    Matsui, M.6    Deng, X.W.7
  • 27
    • 0028365625 scopus 로고
    • Arabidopsis COP9 is a component of a novel signaling complex mediating light control of development
    • Wei N, Chamovitz DA, Deng XW. 1994. Arabidopsis COP9 is a component of a novel signaling complex mediating light control of development. Cell 78:117-124.
    • (1994) Cell , vol.78 , pp. 117-124
    • Wei, N.1    Chamovitz, D.A.2    Deng, X.W.3
  • 28
    • 0032993486 scopus 로고    scopus 로고
    • Making sense of the COP9 signalosome. A regulatory protein complex conserved from Arabidopsis to human.
    • Wei N, Deng XW. 1999. Making sense of the COP9 signalosome. A regulatory protein complex conserved from Arabidopsis to human. Trends Genet. 15:98 -103.
    • (1999) Trends Genet. , vol.15 , pp. 98-103
    • Wei, N.1    Deng, X.W.2
  • 30
    • 0042665894 scopus 로고    scopus 로고
    • The COP9 signalosome is an essential regulator of development in the filamentous fungus Aspergillus nidulans
    • Busch S, Eckert SE, Krappmann S, Braus GH. 2003. The COP9 signalosome is an essential regulator of development in the filamentous fungus Aspergillus nidulans. Mol. Microbiol. 49:717-730.
    • (2003) Mol. Microbiol. , vol.49 , pp. 717-730
    • Busch, S.1    Eckert, S.E.2    Krappmann, S.3    Braus, G.H.4
  • 31
    • 34250215269 scopus 로고    scopus 로고
    • CIF-1, a shared subunit of the COP9/ signalosome and eukaryotic initiation factor 3 complexes, regulates MEL-26 levels in the Caenorhabditis elegans embryo
    • Luke-Glaser S, Roy M, Larsen B, Le Bihan T, Metalnikov P, Tyers M, Peter M, Pintard L. 2007. CIF-1, a shared subunit of the COP9/ signalosome and eukaryotic initiation factor 3 complexes, regulates MEL-26 levels in the Caenorhabditis elegans embryo. Mol. Cell. Biol. 27: 4526-4540.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4526-4540
    • Luke-Glaser, S.1    Roy, M.2    Larsen, B.3    Le Bihan, T.4    Metalnikov, P.5    Tyers, M.6    Peter, M.7    Pintard, L.8
  • 32
    • 0036472506 scopus 로고    scopus 로고
    • The COP9 signalosome: at the interface between signal transduction and ubiquitin-dependent proteolysis
    • Bech-Otschir D, Seeger M, Dubiel W. 2002. The COP9 signalosome: at the interface between signal transduction and ubiquitin-dependent proteolysis. J. Cell Sci. 115:467- 473.
    • (2002) J. Cell Sci. , vol.115 , pp. 467-473
    • Bech-Otschir, D.1    Seeger, M.2    Dubiel, W.3
  • 33
    • 0141426637 scopus 로고    scopus 로고
    • COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases
    • Cope GA, Deshaies RJ. 2003. COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases. Cell 114:663- 671. 34. Schwechheimer C. 2004. The COP9 signalosome (CSN): an evolutionary conserved proteolysis regulator in eukaryotic development. Biochim. Biophys. Acta 1695:45-54.
    • (2003) Cell , vol.114 , pp. 663-671
    • Cope, G.A.1    Deshaies, R.J.2
  • 34
    • 9644272422 scopus 로고    scopus 로고
    • The COP9 signalosome (CSN): an evolutionary conserved proteolysis regulator in eukaryotic development
    • Schwechheimer C. 2004. The COP9 signalosome (CSN): an evolutionary conserved proteolysis regulator in eukaryotic development. Biochim. Biophys. Acta 1695:45-54.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 45-54
    • Schwechheimer, C.1
  • 35
    • 0344583797 scopus 로고    scopus 로고
    • On again-off again: COP9 signalosome turns the key on protein degradation
    • von Arnim AG. 2003. On again-off again: COP9 signalosome turns the key on protein degradation. Curr. Opin. Plant Biol. 6:520 -529.
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 520-529
    • von Arnim, A.G.1
  • 37
    • 0345099331 scopus 로고    scopus 로고
    • The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases?
    • Wolf DA, Zhou C, Wee S. 2003. The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases? Nat. Cell Biol. 5:1029- 1033.
    • (2003) Nat.Cell Biol. , vol.5 , pp. 1029-1033
    • Wolf, D.A.1    Zhou, C.2    Wee, S.3
  • 38
    • 2442575650 scopus 로고    scopus 로고
    • The COP9 signalosome: mediating between kinase signaling and protein degradation
    • Harari-Steinberg O, Chamovitz DA. 2004. The COP9 signalosome: mediating between kinase signaling and protein degradation. Curr. Protein Pept. Sci. 5:185-189.
    • (2004) Curr. Protein Pept. Sci. , vol.5 , pp. 185-189
    • Harari-Steinberg, O.1    Chamovitz, D.A.2
  • 40
    • 33745218066 scopus 로고    scopus 로고
    • Jab1 induces the cytoplasmic localization and degradation of p53 in coordination with Hdm2
    • Oh W, Lee EW, Sung YH, Yang MR, Ghim J, Lee HW, Song J. 2006. Jab1 induces the cytoplasmic localization and degradation of p53 in coordination with Hdm2. J. Biol. Chem. 281:17457-17465.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17457-17465
    • Oh, W.1    Lee, E.W.2    Sung, Y.H.3    Yang, M.R.4    Ghim, J.5    Lee, H.W.6    Song, J.7
  • 41
    • 28744441667 scopus 로고    scopus 로고
    • Development of a method for screening short-lived proteins using green fluorescent protein
    • R81 doi:10.1186/gb-2004-5-10-r81
    • Jiang X, Coffino P, Li X. 2004. Development of a method for screening short-lived proteins using green fluorescent protein. Genome Biol. 5:R81. doi:10.1186/gb-2004-5-10-r81.
    • (2004) Genome Biol , vol.5
    • Jiang, X.1    Coffino, P.2    Li, X.3
  • 42
    • 84863275063 scopus 로고    scopus 로고
    • Interferon regulatory factor 5 activation in monocytes of systemic lupus erythematosus patients is triggered by circulating autoantigens independent of type I interferons
    • Stone RC, Feng D, Deng J, Singh S, Yang L, Fitzgerald-Bocarsly P, Eloranta ML, Ronnblom L, Barnes BJ. 2012. Interferon regulatory factor 5 activation in monocytes of systemic lupus erythematosus patients is triggered by circulating autoantigens independent of type I interferons. Arthritis Rheum. 64:788 -798.
    • (2012) Arthritis Rheum. , vol.64 , pp. 788-798
    • Stone, R.C.1    Feng, D.2    Deng, J.3    Singh, S.4    Yang, L.5    Fitzgerald-Bocarsly, P.6    Eloranta, M.L.7    Ronnblom, L.8    Barnes, B.J.9
  • 43
    • 77955714077 scopus 로고    scopus 로고
    • Reduced expression of plasma membrane calcium ATPase 2 and collapsin response mediator protein 1 promotes death of spinal cord neurons
    • Kurnellas MP, Li H, Jain MR, Giraud SN, Nicot AB, Ratnayake A, Heary RF, Elkabes S. 2010. Reduced expression of plasma membrane calcium ATPase 2 and collapsin response mediator protein 1 promotes death of spinal cord neurons. Cell Death Differ. 17:1501-1510.
    • (2010) Cell Death Differ. , vol.17 , pp. 1501-1510
    • Kurnellas, M.P.1    Li, H.2    Jain, M.R.3    Giraud, S.N.4    Nicot, A.B.5    Ratnayake, A.6    Heary, R.F.7    Elkabes, S.8
  • 44
    • 0037063336 scopus 로고    scopus 로고
    • Association of the mammalian proto-oncoprotein Int-6 with the three protein complexes eIF3, COP9 signalosome and 26S proteasome
    • Hoareau Alves K, Bochard V, Rety S, Jalinot P. 2002. Association of the mammalian proto-oncoprotein Int-6 with the three protein complexes eIF3, COP9 signalosome and 26S proteasome. FEBS Lett. 527:15-21.
    • (2002) FEBS Lett. , vol.527 , pp. 15-21
    • Hoareau Alves, K.1    Bochard, V.2    Rety, S.3    Jalinot, P.4
  • 46
    • 0035310470 scopus 로고    scopus 로고
    • Characterization of the interaction between the transcription factors human polyamine modulated factor (PMF-1) and NF-E2-related factor 2 (Nrf-2) in the transcriptional regulation of the spermidine/spermine N1- acetyltransferase (SSAT) gene
    • Wang Y, Devereux W, Stewart TM, Casero RA, Jr. 2001. Characterization of the interaction between the transcription factors human polyamine modulated factor (PMF-1) and NF-E2-related factor 2 (Nrf-2) in the transcriptional regulation of the spermidine/spermine N1- acetyltransferase (SSAT) gene. Biochem. J. 355:45- 49.
    • (2001) Biochem. J. , vol.355 , pp. 45-49
    • Wang, Y.1    Devereux, W.2    Stewart, T.M.3    Casero, R.A.4
  • 47
  • 48
    • 0037195929 scopus 로고    scopus 로고
    • Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1
    • Sun Y, Wilson MP, Majerus PW. 2002. Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1. J. Biol. Chem. 277:45759-45764.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45759-45764
    • Sun, Y.1    Wilson, M.P.2    Majerus, P.W.3
  • 49
    • 0035798638 scopus 로고    scopus 로고
    • Inositol 1,3,4- trisphosphate 5/6-kinase is a protein kinase that phosphorylates the transcription factors c-Jun and ATF-2
    • Wilson MP, Sun Y, Cao L, Majerus PW. 2001. Inositol 1,3,4- trisphosphate 5/6-kinase is a protein kinase that phosphorylates the transcription factors c-Jun and ATF-2. J. Biol. Chem. 276:40998-41004.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40998-41004
    • Wilson, M.P.1    Sun, Y.2    Cao, L.3    Majerus, P.W.4
  • 50
  • 52
    • 38849097142 scopus 로고    scopus 로고
    • Downregulation of COP9 signalosome subunits differentially affects the CSN complex and target protein stability
    • doi:10.1186/1471-2091-8-27
    • Peth A, Berndt C, Henke W, Dubiel W. 2007. Downregulation of COP9 signalosome subunits differentially affects the CSN complex and target protein stability. BMC Biochem. 8:27. doi:10.1186/1471-2091-8-27.
    • (2007) BMC Biochem , vol.8-27
    • Peth, A.1    Berndt, C.2    Henke, W.3    Dubiel, W.4
  • 54
    • 27644440307 scopus 로고    scopus 로고
    • Purification method of the COP9 signalosome from human erythrocytes
    • Hetfeld BK, Bech-Otschir D, Dubiel W. 2005. Purification method of the COP9 signalosome from human erythrocytes. Methods Enzymol. 398: 481-491.
    • (2005) Methods Enzymol. , vol.398 , pp. 481-491
    • Hetfeld, B.K.1    Bech-Otschir, D.2    Dubiel, W.3
  • 56
    • 33745823159 scopus 로고    scopus 로고
    • The ATM-mediated DNA-damage response: taking shape
    • Shiloh Y. 2006. The ATM-mediated DNA-damage response: taking shape. Trends Biochem. Sci. 31:402- 410.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 402-410
    • Shiloh, Y.1
  • 57
    • 11244272124 scopus 로고    scopus 로고
    • The Jab1/COP9 signalosome subcomplex is a downstream mediator of Bcr-Abl kinase activity and facilitates cell-cycle progression
    • Tomoda K, Kato JY, Tatsumi E, Takahashi T, Matsuo Y, Yoneda-Kato N. 2005. The Jab1/COP9 signalosome subcomplex is a downstream mediator of Bcr-Abl kinase activity and facilitates cell-cycle progression. Blood 105:775-783.
    • (2005) Blood , vol.105 , pp. 775-783
    • Tomoda, K.1    Kato, J.Y.2    Tatsumi, E.3    Takahashi, T.4    Matsuo, Y.5    Yoneda-Kato, N.6
  • 58
    • 0033545636 scopus 로고    scopus 로고
    • Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1
    • Tomoda K, Kubota Y, Kato J. 1999. Degradation of the cyclindependent- kinase inhibitor p27Kip1 is instigated by Jab1. Nature 398: 160-165.
    • (1999) Nature , vol.398 , pp. 160-165
    • Tomoda, K.1    Kubota, Y.2    Kato, J.3
  • 59
    • 18944367474 scopus 로고    scopus 로고
    • Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via COP9 signalosome subunit 3
    • Yoneda-Kato N, Tomoda K, Umehara M, Arata Y, Kato JY. 2005. Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via COP9 signalosome subunit 3. EMBO J. 24:1739 -1749.
    • (2005) EMBO J. , vol.24 , pp. 1739-1749
    • Yoneda-Kato, N.1    Tomoda, K.2    Umehara, M.3    Arata, Y.4    Kato, J.Y.5
  • 61
    • 0033557741 scopus 로고    scopus 로고
    • Assembly requirements of PU.1-Pip (IRF-4) activator comple xesP:inhibiting function in vivo using fused dimers
    • Brass AL, Zhu AQ, Singh H. 1999. Assembly requirements of PU.1-Pip (IRF-4) activator complexes: inhibiting function in vivo using fused dimers. EMBO J. 18:977-991.
    • (1999) EMBO J. , vol.18 , pp. 77-991
    • Brass, A.L.1    Zhu, A.Q.2    Singh, H.3
  • 62
    • 0032577707 scopus 로고    scopus 로고
    • PU. 1, interferon regulatory factor 1, and interferon consensus sequence-binding protein cooperate to increase gp91(phox) expression.
    • Eklund EA, Jalava A, Kakar R. 1998. PU.1, interferon regulatory factor 1, and interferon consensus sequence-binding protein cooperate to increase gp91(phox) expression. J. Biol. Chem. 273:13957-13965.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13957-13965
    • Eklund, E.A.1    Jalava, A.2    Kakar, R.3
  • 64
    • 0029067356 scopus 로고
    • Functional domain analysis of interferon consensus sequence binding protein (ICSBP) and its association with interferon regulatory factors
    • Sharf R, Azriel A, Lejbkowicz F, Winograd SS, Ehrlich R, Levi BZ. 1995. Functional domain analysis of interferon consensus sequence binding protein (ICSBP) and its association with interferon regulatory factors. J. Biol. Chem. 270:13063-13069.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13063-13069
    • Sharf, R.1    Azriel, A.2    Lejbkowicz, F.3    Winograd, S.S.4    Ehrlich, R.5    Levi, B.Z.6
  • 66
    • 33947606938 scopus 로고    scopus 로고
    • CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha
    • Schweitzer K, Bozko PM, Dubiel W, Naumann M. 2007. CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha. EMBO J. 26:1532- 1541.
    • (2007) EMBO J. , vol.26 , pp. 1532-1541
    • Schweitzer, K.1    Bozko, P.M.2    Dubiel, W.3    Naumann, M.4
  • 67
    • 76449101776 scopus 로고    scopus 로고
    • Control of NF-kappaB activation by the COP9 signalosome
    • Schweitzer K, Naumann M. 2010. Control of NF-kappaB activation by the COP9 signalosome. Biochem. Soc. Trans. 38:156 -161.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 156-161
    • Schweitzer, K.1    Naumann, M.2
  • 68
    • 0033544866 scopus 로고    scopus 로고
    • COP9 signalosome-directed c-Jun activation/stabilization is independent of JNK
    • Naumann M, Bech-Otschir D, Huang X, Ferrell K, Dubiel W. 1999. COP9 signalosome-directed c-Jun activation/stabilization is independent of JNK. J. Biol. Chem. 274:35297-35300.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35297-35300
    • Naumann, M.1    Bech-Otschir, D.2    Huang, X.3    Ferrell, K.4    Dubiel, W.5
  • 69
    • 70450173568 scopus 로고    scopus 로고
    • Mammalian COP9 signalosome
    • Kato JY, Yoneda-Kato N. 2009. Mammalian COP9 signalosome. Genes Cells 14:1209 -1225.
    • (2009) Genes Cells , vol.14 , pp. 1209-1225
    • Kato, J.Y.1    Yoneda-Kato, N.2
  • 70
    • 33749242814 scopus 로고    scopus 로고
    • Signalling platforms that modulate the inflammatory response: new targets for drug development
    • McCulloch CA, Downey GP, El-Gabalawy H. 2006. Signalling platforms that modulate the inflammatory response: new targets for drug development. Nat. Rev. Drug Discov. 5:864-876.
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 864-876
    • McCulloch, C.A.1    Downey, G.P.2    El-Gabalawy, H.3
  • 71
    • 33645216339 scopus 로고    scopus 로고
    • Cul4A and DDB1 associate with Skp2 to target p27Kip1 for proteolysis involving the COP9 signalosome
    • Bondar T, Kalinina A, Khair L, Kopanja D, Nag A, Bagchi S, Raychaudhuri P. 2006. Cul4A and DDB1 associate with Skp2 to target p27Kip1 for proteolysis involving the COP9 signalosome. Mol. Cell. Biol. 26:2531-2539.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2531-2539
    • Bondar, T.1    Kalinina, A.2    Khair, L.3    Kopanja, D.4    Nag, A.5    Bagchi, S.6    Raychaudhuri, P.7
  • 72
    • 35548940309 scopus 로고    scopus 로고
    • COP9 signalosome subunit 8 is essential for peripheral T cell homeostasis and antigen receptor-induced entry into the cell cycle from quiescence
    • Menon S, Chi H, Zhang H, Deng XW, Flavell RA, Wei N. 2007. COP9 signalosome subunit 8 is essential for peripheral T cell homeostasis and antigen receptor-induced entry into the cell cycle from quiescence. Nat. Immunol. 8:1236 -1245.
    • (2007) Nat. Immunol , vol.8 , pp. 1236-1245
    • Menon, S.1    Chi, H.2    Zhang, H.3    Deng, X.W.4    Flavell, R.A.5    Wei, N.6
  • 75
    • 13844259319 scopus 로고    scopus 로고
    • Small Jab1-containing subcomplex is regulated in an anchorage- and cell cycle-dependent manner, which is abrogated by ras transformation
    • Fukumoto A, Tomoda K, Kubota M, Kato JY, Yoneda-Kato N. 2005. Small Jab1-containing subcomplex is regulated in an anchorage- and cell cycle-dependent manner, which is abrogated by ras transformation. FEBS Lett. 579:1047-1054.
    • (2005) FEBS Lett , vol.579 , pp. 1047-1054
    • Fukumoto, A.1    Tomoda, K.2    Kubota, M.3    Kato, J.Y.4    Yoneda-Kato, N.5
  • 77
    • 0242525214 scopus 로고    scopus 로고
    • Radiationmediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint
    • Higa LA, Mihaylov IS, Banks DP, Zheng J, Zhang H. 2003. Radiationmediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint. Nat. Cell Biol. 5:1008 -1015.
    • (2003) Nat. Cell Biol , vol.5
    • Higa, L.A.1    Mihaylov, I.S.2    Banks, D.P.3    Zheng, J.4    Zhang, H.5
  • 78
    • 34447252157 scopus 로고    scopus 로고
    • Jab1 mediates protein degradation of the Rad9-Rad1-Hus1 checkpoint complex
    • Huang J, Yuan H, Lu C, Liu X, Cao X, Wan M. 2007. Jab1 mediates protein degradation of the Rad9-Rad1-Hus1 checkpoint complex. J. Mol. Biol. 371:514 -527.
    • (2007) J. Mol. Biol , vol.371
    • Huang, J.1    Yuan, H.2    Lu, C.3    Liu, X.4    Cao, X.5    Wan, M.6
  • 80
    • 34250333052 scopus 로고    scopus 로고
    • The subunit CSN6 of the COP9 signalosome is cleaved during apoptosis
    • da Silva Correia J, Miranda Y, Leonard N, Ulevitch RJ. 2007. The subunit CSN6 of the COP9 signalosome is cleaved during apoptosis. J. Biol. Chem. 282:12557-12565.
    • (2007) J. Biol. Chem , vol.282 , pp. 12557-12565
    • da Silva Correia, J.1    Miranda, Y.2    Leonard, N.3    Ulevitch, R.J.4
  • 81
    • 38649109469 scopus 로고    scopus 로고
    • The COP9 signalosome-mediated deneddylation is stimulated by caspases during apoptosis
    • Hetfeld BK, Peth A, Sun XM, Henklein P, Cohen GM, Dubiel W. 2008. The COP9 signalosome-mediated deneddylation is stimulated by caspases during apoptosis. Apoptosis 13:187-195.
    • (2008) Apoptosis , vol.13 , pp. 187-195
    • Hetfeld, B.K.1    Peth, A.2    Sun, X.M.3    Henklein, P.4    Cohen, G.M.5    Dubiel, W.6
  • 82
    • 66749097742 scopus 로고    scopus 로고
    • Analysis of the role of COP9 Signalosome (CSN) subunits in K562; the first link between CSN and autophagy
    • doi:10.1186/1471-2121-10-31
    • Pearce C, Hayden RE, Bunce CM, Khanim FL. 2009. Analysis of the role of COP9 Signalosome (CSN) subunits in K562; the first link between CSN and autophagy. BMC Cell Biol. 10:31. doi:10.1186/1471-2121-10-31.
    • (2009) BMC Cell Biol , vol.10 , pp. 31
    • Pearce, C.1    Hayden, R.E.2    Bunce, C.M.3    Khanim, F.L.4
  • 83
  • 85
    • 79955957425 scopus 로고    scopus 로고
    • Plant homologue constitutive photomorphogenesis 9 (COP9) signalosome subunit CSN5 regulates innate immune responses in macrophages
    • Deng Z, Pardi R, Cheadle W, Xiang X, Zhang S, Shah SV, Grizzle W, Miller D, Mountz J, Zhang HG. 2011. Plant homologue constitutive photomorphogenesis 9 (COP9) signalosome subunit CSN5 regulates innate immune responses in macrophages. Blood 117:4796-4804.
    • (2011) Blood , vol.117 , pp. 4796-4804
    • Deng, Z.1    Pardi, R.2    Cheadle, W.3    Xiang, X.4    Zhang, S.5    Shah, S.V.6    Grizzle, W.7    Miller, D.8    Mountz, J.9    Zhang, H.G.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.