메뉴 건너뛰기




Volumn 1, Issue , 2007, Pages 348-369

The COP9 Signalosome: Its Possible Role in the Ubiquitin System

Author keywords

Architecture of the CSN; Association of CSN with other protein complexes; Biochemical activities associated with the CSN; Biological functions of the CSN; COP9 signalosome; Discovery of the CSN; Protein degradation

Indexed keywords


EID: 84889615514     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527619320.ch13     Document Type: Chapter
Times cited : (4)

References (100)
  • 2
    • 0028365625 scopus 로고
    • Arabidopsis COP9 is a component of a novel signaling complex mediating light control of development
    • Wei, N., Chamovitz, D. A., Deng, X. W. Arabidopsis COP9 is a component of a novel signaling complex mediating light control of development. Cell 1994, 78, 117-124.
    • (1994) Cell , vol.78 , pp. 117-124
    • Wei, N.1    Chamovitz, D.A.2    Deng, X.W.3
  • 3
    • 0032993486 scopus 로고    scopus 로고
    • Making sense of the COP9 signalosome. A regulatory protein complex conserved from Arabidopsis to human
    • Wei, N., Deng, X. W. Making sense of the COP9 signalosome. A regulatory protein complex conserved from Arabidopsis to human. Trends Genet. 1999, 15, 98-103.
    • (1999) Trends Genet. , vol.15 , pp. 98-103
    • Wei, N.1    Deng, X.W.2
  • 4
    • 0037480420 scopus 로고    scopus 로고
    • The COP9 signalosome: regulating plant development through the control of proteolysis
    • Serino, G., Deng, X. W. The COP9 signalosome: regulating plant development through the control of proteolysis. Annu. Rev. Plant Biol. 2003, 54, 165-182.
    • (2003) Annu. Rev. Plant Biol. , vol.54 , pp. 165-182
    • Serino, G.1    Deng, X.W.2
  • 6
    • 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, X. W. The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex. Curr. Biol. 1998, 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
  • 7
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • Glickman, M. H., Rubin, D. M., Coux, O., Wefes, I., Pfeifer, G., Cjeka, Z., Baumeister, W., Fried, V. A., Finley, D. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 1998, 94, 615-623.
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 8
    • 0035478483 scopus 로고    scopus 로고
    • COP9 signalosome revisited: a novel mediator of protein degradation
    • Schwechheimer, C., Deng, X. W. COP9 signalosome revisited: a novel mediator of protein degradation. Trends Cell Biol. 2001, 11, 420-426.
    • (2001) Trends Cell Biol. , vol.11 , pp. 420-426
    • Schwechheimer, C.1    Deng, X.W.2
  • 10
    • 0141557809 scopus 로고    scopus 로고
    • Disruption of the COP9 signalosome Csn2 subunit in mice causes deficient cell proliferation, accumulation of p53 and cyclin E, and early embryonic death
    • Lykke-Andersen, K., Schaefer, L., Menon, S., Deng, X. W., Miller, J. B., Wei, N. Disruption of the COP9 signalosome Csn2 subunit in mice causes deficient cell proliferation, accumulation of p53 and cyclin E, and early embryonic death. Mol. Cell. Biol. 2003, 23, 6790-6797.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6790-6797
    • Lykke-Andersen, K.1    Schaefer, L.2    Menon, S.3    Deng, X.W.4    Miller, J.B.5    Wei, N.6
  • 11
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • Groisman, R., Polanowska, J., Kuraoka, I., Sawada, J., Saijo, M., Drapkin, R., Kisselev, A. F., Tanaka, K., Nakatani, Y. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 2003, 113, 357-367.
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3    Sawada, J.4    Saijo, M.5    Drapkin, R.6    Kisselev, A.F.7    Tanaka, K.8    Nakatani, Y.9
  • 12
    • 0038185375 scopus 로고    scopus 로고
    • Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and-independent mechanisms
    • Liu, C., Powell, K. A., Mundt, K., Wu, L., Carr, A. M., Caspari, T. Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and-independent mechanisms. Genes Dev. 2003, 17, 1130-1140.
    • (2003) Genes Dev. , vol.17 , pp. 1130-1140
    • Liu, C.1    Powell, K.A.2    Mundt, K.3    Wu, L.4    Carr, A.M.5    Caspari, T.6
  • 13
    • 0035576892 scopus 로고    scopus 로고
    • The constitutive photomorphogenesis 9 signalosome directs vascular endothelial growth factor production in tumor cells
    • Pollmann, C., Huang, X., Mall, J., Bech-Otschir, D., Naumann, M., Dubiel, W. The constitutive photomorphogenesis 9 signalosome directs vascular endothelial growth factor production in tumor cells. Cancer Res. 2001, 61, 8416-8421.
    • (2001) Cancer Res. , vol.61 , pp. 8416-8421
    • Pollmann, C.1    Huang, X.2    Mall, J.3    Bech-Otschir, D.4    Naumann, M.5    Dubiel, W.6
  • 14
    • 0034521740 scopus 로고    scopus 로고
    • The roles of photoreceptor systems and the COP1-targeted destabilization of HY5 in light control of Arabidopsis seedling development
    • Osterlund, M. T., Wei, N., Deng, X. W. The roles of photoreceptor systems and the COP1-targeted destabilization of HY5 in light control of Arabidopsis seedling development. Plant Physiol. 2000, 124, 1520-1524.
    • (2000) Plant Physiol. , vol.124 , pp. 1520-1524
    • Osterlund, M.T.1    Wei, N.2    Deng, X.W.3
  • 15
    • 0029761277 scopus 로고    scopus 로고
    • A new group of conserved coactivators that increase the specificity of AP-1 transcription factors
    • Claret, F. X., Hibi, M., Dhut, S., Toda, T., Karin, M. A new group of conserved coactivators that increase the specificity of AP-1 transcription factors. Nature 1996, 383, 453-457.
    • (1996) Nature , vol.383 , pp. 453-457
    • Claret, F.X.1    Hibi, M.2    Dhut, S.3    Toda, T.4    Karin, M.5
  • 16
    • 0028876893 scopus 로고
    • Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor
    • Lee, J. W., Choi, H. S., Gyuris, J., Brent, R., Moore, D. D. Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol. Endocrinol. 1995, 9, 243-254.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 243-254
    • Lee, J.W.1    Choi, H.S.2    Gyuris, J.3    Brent, R.4    Moore, D.D.5
  • 17
    • 0032133073 scopus 로고    scopus 로고
    • Characterization and purification of the mammalian COP9 complex, a conserved nuclear regulator initially identified as a repressor of photomorphogenesis in higher plants
    • Wei, N., Deng, X. W. Characterization and purification of the mammalian COP9 complex, a conserved nuclear regulator initially identified as a repressor of photomorphogenesis in higher plants. Photochem. Photobiol. 1998, 68, 237-241.
    • (1998) Photochem. Photobiol. , vol.68 , pp. 237-241
    • Wei, N.1    Deng, X.W.2
  • 19
    • 0034725525 scopus 로고    scopus 로고
    • Electron microscopy and subunit-subunit interaction studies reveal a first architecture of COP9 signalosome
    • Kapelari, B., Bech-Otschir, D., Hegerl, R., Schade, R., Dumdey, R., Dubiel, W. Electron microscopy and subunit-subunit interaction studies reveal a first architecture of COP9 signalosome. J. Mol. Biol. 2000, 300, 1169-1178.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1169-1178
    • Kapelari, B.1    Bech-Otschir, D.2    Hegerl, R.3    Schade, R.4    Dumdey, R.5    Dubiel, W.6
  • 21
    • 0029860455 scopus 로고    scopus 로고
    • Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11), suppress G-protein-and mitogenactivated protein kinase-mediated signal transduction in yeast and mammalian cells
    • Spain, B. H., Bowdish, K. S., Pacal, A. R., Staub, S. F., Koo, D., Chang, C. Y., Xie, W., Colicelli, J. Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11), suppress G-protein-and mitogenactivated protein kinase-mediated signal transduction in yeast and mammalian cells. Mol. Cell. Biol. 1996, 16, 6698-6706.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6698-6706
    • Spain, B.H.1    Bowdish, K.S.2    Pacal, A.R.3    Staub, S.F.4    Koo, D.5    Chang, C.Y.6    Xie, W.7    Colicelli, J.8
  • 22
    • 0035808382 scopus 로고    scopus 로고
    • The subunit 1 of the COP9 signalosome suppresses gene expression through its N-terminal domain and incorporates into the complex through the PCI domain
    • Tsuge, T., Matsui, M., Wei, N. The subunit 1 of the COP9 signalosome suppresses gene expression through its N-terminal domain and incorporates into the complex through the PCI domain. J. Mol. Biol. 2001, 305, 1-9.
    • (2001) J. Mol. Biol. , vol.305 , pp. 1-9
    • Tsuge, T.1    Matsui, M.2    Wei, N.3
  • 23
    • 0036178019 scopus 로고    scopus 로고
    • CSN1 N-terminal-dependent activity is required for Arabidopsis development but not for Rub1/Nedd8 deconjugation of cullins: a structurefunction study of CSN1 subunit of COP9 signalosome
    • Wang, X., Kang, D., Feng, S., Serino, G., Schwechheimer, C., Wei, N. CSN1 N-terminal-dependent activity is required for Arabidopsis development but not for Rub1/Nedd8 deconjugation of cullins: a structurefunction study of CSN1 subunit of COP9 signalosome. Mol. Biol. Cell 2002, 13, 646-655.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 646-655
    • Wang, X.1    Kang, D.2    Feng, S.3    Serino, G.4    Schwechheimer, C.5    Wei, N.6
  • 24
    • 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, M. P., Majerus, P. W. Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1. J. Biol. Chem. 2002, 277, 45759-45764.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45759-45764
    • Sun, Y.1    Wilson, M.P.2    Majerus, P.W.3
  • 25
    • 0032514947 scopus 로고    scopus 로고
    • The Arabidopsis homologue of an eIF3 complex subunit associates with the COP9 complex
    • Karniol, B., Yahalom, A., Kwok, S., Tsuge, T., Matsui, M., Deng, X. W., Chamovitz, D. A. The Arabidopsis homologue of an eIF3 complex subunit associates with the COP9 complex. FEBS Lett. 1998, 439, 173-179.
    • (1998) FEBS Lett. , vol.439 , pp. 173-179
    • Karniol, B.1    Yahalom, A.2    Kwok, S.3    Tsuge, T.4    Matsui, M.5    Deng, X.W.6    Chamovitz, D.A.7
  • 26
    • 0033534648 scopus 로고    scopus 로고
    • Characterization of two subunits of Arabidopsis 19S proteasome regulatory complex and its possible interaction with the COP9 complex
    • Kwok, S. F., Staub, J. M., Deng, X. W. Characterization of two subunits of Arabidopsis 19S proteasome regulatory complex and its possible interaction with the COP9 complex. J. Mol. Biol. 1999, 285, 85-95.
    • (1999) J. Mol. Biol. , vol.285 , pp. 85-95
    • Kwok, S.F.1    Staub, J.M.2    Deng, X.W.3
  • 28
    • 0037117417 scopus 로고    scopus 로고
    • The COP9 signalosome inhibits p27(kip1) degradation and impedes G1-S phase progression via deneddylation of SCF Cul1
    • Yang, X., Menon, S., Lykke-Andersen, K., Tsuge, T., Di, X., Wang, X., Rodriguez-Suarez, R. J., Zhang, H., Wei, N. The COP9 signalosome inhibits p27(kip1) degradation and impedes G1-S phase progression via deneddylation of SCF Cul1. Curr. Biol. 2002, 12, 667-672.
    • (2002) Curr. Biol. , vol.12 , pp. 667-672
    • Yang, X.1    Menon, S.2    Lykke-Andersen, K.3    Tsuge, T.4    Di, X.5    Wang, X.6    Rodriguez-Suarez, R.J.7    Zhang, H.8    Wei, N.9
  • 29
    • 0034671924 scopus 로고    scopus 로고
    • Interaction between interferon consensus sequence-binding protein and COP9/signalosome subunit CSN2 (Trip15). A possible link between interferon regulatory factor signaling and the COP9/signalosome
    • Cohen, H., Azriel, A., Cohen, T., Meraro, D., Hashmueli, S., Bech-Otschir, D., Kraft, R., Dubiel, W., Levi, B. Z. Interaction between interferon consensus sequence-binding protein and COP9/signalosome subunit CSN2 (Trip15). A possible link between interferon regulatory factor signaling and the COP9/signalosome. J. Biol. Chem. 2000, 275, 39081-39089.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39081-39089
    • Cohen, H.1    Azriel, A.2    Cohen, T.3    Meraro, D.4    Hashmueli, S.5    Bech-Otschir, D.6    Kraft, R.7    Dubiel, W.8    Levi, B.Z.9
  • 30
    • 0034677882 scopus 로고    scopus 로고
    • Interaction of the corepressor Alien with DAX-1 is abrogated by mutations of DAX-1 involved in adrenal hypoplasia congenita
    • Altincicek, B., Tenbaum, S. P., Dressel, U., Thormeyer, D., Renkawitz, R., Baniahmad, A. Interaction of the corepressor Alien with DAX-1 is abrogated by mutations of DAX-1 involved in adrenal hypoplasia congenita. J. Biol. Chem. 2000, 275, 7662-7667.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7662-7667
    • Altincicek, B.1    Tenbaum, S.P.2    Dressel, U.3    Thormeyer, D.4    Renkawitz, R.5    Baniahmad, A.6
  • 32
    • 0035874621 scopus 로고    scopus 로고
    • CSN3 interacts with IKKgamma and inhibits TNF-but not IL-1-induced NF-kappaB activation
    • Hong, X., Xu, L., Li, X., Zhai, Z., Shu, H. CSN3 interacts with IKKgamma and inhibits TNF-but not IL-1-induced NF-kappaB activation. FEBS Lett. 2001, 499, 133-136.
    • (2001) FEBS Lett. , vol.499 , pp. 133-136
    • Hong, X.1    Xu, L.2    Li, X.3    Zhai, Z.4    Shu, H.5
  • 33
    • 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. Association of the mammalian proto-oncoprotein Int-6 with the three protein complexes eIF3, COP9 signalosome and 26S proteasome. FEBS Lett. 2002, 527, 15-21.
    • (2002) FEBS Lett. , vol.527 , pp. 15-21
    • Hoareau Alves, K.1    Bochard, V.2    Rety, S.3    Jalinot, P.4
  • 34
    • 0036500015 scopus 로고    scopus 로고
    • Arabidopsis COP10 is a ubiquitinconjugating enzyme variant that acts together with COP1 and the COP9 signalosome in repressing photomorphogenesis
    • Suzuki, G., Yanagawa, Y., Kwok, S. F., Matsui, M., Deng, X. W. Arabidopsis COP10 is a ubiquitinconjugating enzyme variant that acts together with COP1 and the COP9 signalosome in repressing photomorphogenesis. Genes Dev. 2002, 16, 554-559.
    • (2002) Genes Dev. , vol.16 , pp. 554-559
    • Suzuki, G.1    Yanagawa, Y.2    Kwok, S.F.3    Matsui, M.4    Deng, X.W.5
  • 35
    • 0035794541 scopus 로고    scopus 로고
    • COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system
    • Bech-Otschir, D., Kraft, R., Huang, X., Henklein, P., Kapelari, B., Pollmann, C., Dubiel, W. COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. EMBO J. 2001, 20, 1630-1639.
    • (2001) EMBO J. , vol.20 , pp. 1630-1639
    • Bech-Otschir, D.1    Kraft, R.2    Huang, X.3    Henklein, P.4    Kapelari, B.5    Pollmann, C.6    Dubiel, W.7
  • 36
    • 0033545636 scopus 로고    scopus 로고
    • Degradation of the cyclin-dependentkinase inhibitor p27Kip1 is instigated by Jab1
    • Tomoda, K., Kubota, Y., Kato, J. Degradation of the cyclin-dependentkinase inhibitor p27Kip1 is instigated by Jab1. Nature 1999, 398, 160-165.
    • (1999) Nature , vol.398 , pp. 160-165
    • Tomoda, K.1    Kubota, Y.2    Kato, J.3
  • 37
    • 0034607465 scopus 로고    scopus 로고
    • p38JAB1 binds to the intracellular precursor of the lutropin/choriogonadotropin receptor and promotes its degradation
    • Li, S., Liu, X., Ascoli, M. p38JAB1 binds to the intracellular precursor of the lutropin/choriogonadotropin receptor and promotes its degradation. J. Biol. Chem. 2000, 275, 13386-13393.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13386-13393
    • Li, S.1    Liu, X.2    Ascoli, M.3
  • 38
    • 0036198412 scopus 로고    scopus 로고
    • Jab1 antagonizes TGF-beta signaling by inducing Smad4 degradation
    • Wan, M., Cao, X., Wu, Y., Bai, S., Wu, L., Shi, X., Wang, N. Jab1 antagonizes TGF-beta signaling by inducing Smad4 degradation. EMBO Rep. 2002, 3, 171-176.
    • (2002) EMBO Rep. , vol.3 , pp. 171-176
    • Wan, M.1    Cao, X.2    Wu, Y.3    Bai, S.4    Wu, L.5    Shi, X.6    Wang, N.7
  • 40
    • 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. The COP9 signalosome: at the interface between signal transduction and ubiquitin-dependent proteolysis. J. Cell Sci. 2002, 115, 467-473.
    • (2002) J. Cell Sci. , vol.115 , pp. 467-473
    • Bech-Otschir, D.1    Seeger, M.2    Dubiel, W.3
  • 41
    • 4644308739 scopus 로고    scopus 로고
    • Ubiquitindependent degradation of Id1 and Id3 is mediated by the COP9 signalosome
    • Berse, M., Bounpheng, M. A., Huang, X., Christy, B. A., Pollmann, C., Dubiel, W. Ubiquitindependent degradation of Id1 and Id3 is mediated by the COP9 signalosome. J. Mol. Biol. 2004, 343, 361-370.
    • (2004) J. Mol. Biol. , vol.343 , pp. 361-370
    • Berse, M.1    Bounpheng, M.A.2    Huang, X.3    Christy, B.A.4    Pollmann, C.5    Dubiel, W.6
  • 44
    • 0034611731 scopus 로고    scopus 로고
    • Integrin LFA-1 interacts with the transcriptional coactivator JAB1 to modulate AP-1 activity
    • Bianchi, E., Denti, S., Granata, A., Bossi, G., Geginat, J., Villa, A., Rogge, L., Pardi, R. Integrin LFA-1 interacts with the transcriptional coactivator JAB1 to modulate AP-1 activity. Nature 2000, 404, 617-621.
    • (2000) Nature , vol.404 , pp. 617-621
    • Bianchi, E.1    Denti, S.2    Granata, A.3    Bossi, G.4    Geginat, J.5    Villa, A.6    Rogge, L.7    Pardi, R.8
  • 48
    • 0036434142 scopus 로고    scopus 로고
    • The GLH proteins, Caenorhabditis elegans P granule components, associate with CSN-5 and KGB-1, proteins necessary for fertility, and with ZYX-1, a predicted cytoskeletal protein
    • Smith, P., Leung-Chiu, W. M., Montgomery, R., Orsborn, A., Kuznicki, K., Gressman-Coberly, E., Mutapcic, L., Bennett, K. The GLH proteins, Caenorhabditis elegans P granule components, associate with CSN-5 and KGB-1, proteins necessary for fertility, and with ZYX-1, a predicted cytoskeletal protein. Dev. Biol. 2002, 251, 333-347.
    • (2002) Dev. Biol. , vol.251 , pp. 333-347
    • Smith, P.1    Leung-Chiu, W.M.2    Montgomery, R.3    Orsborn, A.4    Kuznicki, K.5    Gressman-Coberly, E.6    Mutapcic, L.7    Bennett, K.8
  • 50
    • 0035098524 scopus 로고    scopus 로고
    • JAB1/CSN5 and the COP9 signalosome. A complex situation
    • Chamovitz, D. A., Segal, D. JAB1/CSN5 and the COP9 signalosome. A complex situation. EMBO Rep. 2001, 2, 96-101.
    • (2001) EMBO Rep. , vol.2 , pp. 96-101
    • Chamovitz, D.A.1    Segal, D.2
  • 51
    • 0037127256 scopus 로고    scopus 로고
    • The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex
    • Tomoda, K., Kubota, Y., Arata, Y., Mori, S., Maeda, M., Tanaka, T., Yoshida, M., Yoneda-Kato, N., Kato, J. Y. The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex. J. Biol. Chem. 2002, 277, 2302-2310.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2302-2310
    • Tomoda, K.1    Kubota, Y.2    Arata, Y.3    Mori, S.4    Maeda, M.5    Tanaka, T.6    Yoshida, M.7    Yoneda-Kato, N.8    Kato, J.Y.9
  • 53
    • 0032584088 scopus 로고    scopus 로고
    • HIV-1 Vpr interacts with a human 34-kDa mov34 homologue, a cellular factor linked to the G2/M phase transition of the mammalian cell cycle
    • Mahalingam, S., Ayyavoo, V., Patel, M., Kieber-Emmons, T., Kao, G. D., Muschel, R. J., Weiner, D. B. HIV-1 Vpr interacts with a human 34-kDa mov34 homologue, a cellular factor linked to the G2/M phase transition of the mammalian cell cycle. Proc. Natl. Acad. Sci. USA 1998, 95, 3419-3424.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3419-3424
    • Mahalingam, S.1    Ayyavoo, V.2    Patel, M.3    Kieber-Emmons, T.4    Kao, G.D.5    Muschel, R.J.6    Weiner, D.B.7
  • 56
    • 0037126632 scopus 로고    scopus 로고
    • Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome
    • Fu, H., Reis, N., Lee, Y., Glickman, M. H., Vierstra, R. D. Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome. EMBO J. 2001, 20, 7096-7107.
    • (2001) EMBO J. , vol.20 , pp. 7096-7107
    • Fu, H.1    Reis, N.2    Lee, Y.3    Glickman, M.H.4    Vierstra, R.D.5
  • 57
    • 0037103765 scopus 로고    scopus 로고
    • Polyaminemodulated factor 1 binds to the human homologue of the 7a subunit of the Arabidopsis COP9 signalosome: implications in gene expression
    • Wang, Y., Devereux, W., Stewart, T. M., Casero, R. A., Jr. Polyaminemodulated factor 1 binds to the human homologue of the 7a subunit of the Arabidopsis COP9 signalosome: implications in gene expression. Biochem. J. 2002, 366, 79-86.
    • (2002) Biochem. J. , vol.366 , pp. 79-86
    • Wang, Y.1    Devereux, W.2    Stewart, T.M.3    Casero Jr., R.A.4
  • 58
    • 0032104227 scopus 로고    scopus 로고
    • The PCI domain: a common theme in three multiprotein complexes
    • Hofmann, K., Bucher, P. The PCI domain: a common theme in three multiprotein complexes. Trends Biochem. Sci. 1998, 23, 204-205.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 204-205
    • Hofmann, K.1    Bucher, P.2
  • 59
    • 0035206221 scopus 로고    scopus 로고
    • PCI complexes: pretty complex interactions in diverse signaling pathways
    • Kim, T., Hofmann, K., von Arnim, A. G., Chamovitz, D. A. PCI complexes: pretty complex interactions in diverse signaling pathways. Trends Plant Sci. 2001, 6, 379-386.
    • (2001) Trends Plant Sci. , vol.6 , pp. 379-386
    • Kim, T.1    Hofmann, K.2    Von Arnim, A.G.3    Chamovitz, D.A.4
  • 63
    • 34248350363 scopus 로고    scopus 로고
    • MPN{thorn}, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function
    • Maytal-Kivity, V., Reis, N., Hofmann, K., Glickman, M. H. MPN{thorn}, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function. BMC BioChem. 2002, 3, 28.
    • (2002) BMC BioChem. , vol.3 , pp. 28
    • Maytal-Kivity, V.1    Reis, N.2    Hofmann, K.3    Glickman, M.H.4
  • 64
    • 0141706654 scopus 로고    scopus 로고
    • Structure of the Jab1/MPN domain and its implications for proteasome function
    • Tran, H. J., Allen, M. D., Lowe, J., Bycroft, M. Structure of the Jab1/MPN domain and its implications for proteasome function. Biochemistry 2003, 42, 11460-11465.
    • (2003) Biochemistry , vol.42 , pp. 11460-11465
    • Tran, H.J.1    Allen, M.D.2    Lowe, J.3    Bycroft, M.4
  • 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. COP9 signalosome-directed c-Jun activation/stabilization is independent of JNK. J. Biol. Chem. 1999, 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
    • 0033133454 scopus 로고    scopus 로고
    • Arabidopsis FUSCA5 encodes a novel phosphoprotein that is a component of the COP9 complex
    • Karniol, B., Malec, P., Chamovitz, D. A. Arabidopsis FUSCA5 encodes a novel phosphoprotein that is a component of the COP9 complex. Plant Cell 1999, 11, 839-848.
    • (1999) Plant Cell , vol.11 , pp. 839-848
    • Karniol, B.1    Malec, P.2    Chamovitz, D.A.3
  • 70
    • 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, M. P., Sun, Y., Cao, L., Majerus, P. W. 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. 2001, 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
  • 71
    • 0037509945 scopus 로고    scopus 로고
    • Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p
    • Zhou, C., Wee, S., Rhee, E., Naumann, M., Dubiel, W., Wolf, D. A. Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p. Mol. Cell 2003, 11, 927-938.
    • (2003) Mol. Cell , vol.11 , pp. 927-938
    • Zhou, C.1    Wee, S.2    Rhee, E.3    Naumann, M.4    Dubiel, W.5    Wolf, D.A.6
  • 72
    • 0345099331 scopus 로고    scopus 로고
    • The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases?
    • Wolf, D. A., Zhou, C., Wee, S. The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases? Nat. Cell Biol. 2003, 5, 1029-1033.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1029-1033
    • Wolf, D.A.1    Zhou, C.2    Wee, S.3
  • 73
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • Geyer, R., Wee, S., Anderson, S., Yates, J., Wolf, D. A. BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases. Mol. Cell 2003, 12, 783-790.
    • (2003) Mol. Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Anderson, S.3    Yates, J.4    Wolf, D.A.5
  • 74
    • 0033995119 scopus 로고    scopus 로고
    • Proteolysis and the cell cycle: with this RING I do thee destroy
    • Tyers, M., Jorgensen, P. Proteolysis and the cell cycle: with this RING I do thee destroy. Curr. Opin. Genet. Dev. 2000, 10, 54-64.
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 54-64
    • Tyers, M.1    Jorgensen, P.2
  • 75
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCFlike modular ubiquitin ligase containing CUL-3
    • Xu, L., Wei, Y., Reboul, J., Vaglio, P., Shin, T. H., Vidal, M., Elledge, S. J., Harper, J. W. BTB proteins are substrate-specific adaptors in an SCFlike modular ubiquitin ligase containing CUL-3. Nature 2003, 425, 316-321.
    • (2003) Nature , vol.425 , pp. 316-321
    • Xu, L.1    Wei, Y.2    Reboul, J.3    Vaglio, P.4    Shin, T.H.5    Vidal, M.6    Elledge, S.J.7    Harper, J.W.8
  • 78
    • 0035808429 scopus 로고    scopus 로고
    • Arabidopsis eIF3e (INT-6) associates with both eIF3c and the COP9 signalosome subunit CSN7
    • Yahalom, A., Kim, T. H., Winter, E., Karniol, B., von Arnim, A. G., Chamovitz, D. A. Arabidopsis eIF3e (INT-6) associates with both eIF3c and the COP9 signalosome subunit CSN7. J. Biol. Chem. 2001, 276, 334-340.
    • (2001) J. Biol. Chem. , vol.276 , pp. 334-340
    • Yahalom, A.1    Kim, T.H.2    Winter, E.3    Karniol, B.4    Von Arnim, A.G.5    Chamovitz, D.A.6
  • 80
    • 0242390528 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6 interact with the eIF3 core complex by binding to cognate eIF3b subunits
    • Shalev, A., Valasek, L., Pise-Masison, C. A., Radonovich, M., Phan, L., Clayton, J., He, H., Brady, J. N., Hinnebusch, A. G., Asano, K. Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6 interact with the eIF3 core complex by binding to cognate eIF3b subunits. J. Biol. Chem. 2001, 276, 34948-34957.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34948-34957
    • Shalev, A.1    Valasek, L.2    Pise-Masison, C.A.3    Radonovich, M.4    Phan, L.5    Clayton, J.6    He, H.7    Brady, J.N.8    Hinnebusch, A.G.9    Asano, K.10
  • 81
    • 0036000003 scopus 로고    scopus 로고
    • Sum1, a component of the fission yeast eIF3 translation initiation complex, is rapidly relocalized during environmental stress and interacts with components of the 26S proteasome
    • Dunand-Sauthier, I., Walker, C., Wilkinson, C., Gordon, C., Crane, R., Norbury, C., Humphrey, T. Sum1, a component of the fission yeast eIF3 translation initiation complex, is rapidly relocalized during environmental stress and interacts with components of the 26S proteasome. Mol. Biol. Cell 2002, 13, 1626-1640.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1626-1640
    • Dunand-Sauthier, I.1    Walker, C.2    Wilkinson, C.3    Gordon, C.4    Crane, R.5    Norbury, C.6    Humphrey, T.7
  • 82
    • 0037462417 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe Int6 and Ras homologs regulate cell division and mitotic fidelity via the proteasome
    • Yen, H. C., Gordon, C., Chang, E. C. Schizosaccharomyces pombe Int6 and Ras homologs regulate cell division and mitotic fidelity via the proteasome. Cell 2003, 112, 207-217.
    • (2003) Cell , vol.112 , pp. 207-217
    • Yen, H.C.1    Gordon, C.2    Chang, E.C.3
  • 83
    • 0037447245 scopus 로고    scopus 로고
    • Protein homeostasis: a degrading role for Int6/eIF3e
    • von Arnim, A. G., Chamovitz, D. A. Protein homeostasis: a degrading role for Int6/eIF3e. Curr. Biol. 2003, 13, R323-325.
    • (2003) Curr. Biol. , vol.13
    • Von Arnim, A.G.1    Chamovitz, D.A.2
  • 84
    • 0038686677 scopus 로고    scopus 로고
    • Evidence for a physical association of the COP9 signalosome, the proteasome, and specific SCF E3 ligases in vivo
    • Peng, Z., Shen, Y., Feng, S., Wang, X., Chitteti, B. N., Vierstra, R. D., Deng, X. W. Evidence for a physical association of the COP9 signalosome, the proteasome, and specific SCF E3 ligases in vivo. Curr. Biol. 2003, 13, R504-505.
    • (2003) Curr. Biol. , vol.13
    • Peng, Z.1    Shen, Y.2    Feng, S.3    Wang, X.4    Chitteti, B.N.5    Vierstra, R.D.6    Deng, X.W.7
  • 85
    • 1542713819 scopus 로고    scopus 로고
    • The COP9 signalosome: an alternative lid for the 26S proteasome?
    • Li, L., Deng, X. W. The COP9 signalosome: an alternative lid for the 26S proteasome? Trends Cell Biol. 2003, 13, 507-509.
    • (2003) Trends Cell Biol. , vol.13 , pp. 507-509
    • Li, L.1    Deng, X.W.2
  • 86
    • 0141426637 scopus 로고    scopus 로고
    • COP9 signalosome: a multifunctional regulator of SCF and other cullinbased ubiquitin ligases
    • Cope, G. A., Deshaies, R. J. COP9 signalosome: a multifunctional regulator of SCF and other cullinbased ubiquitin ligases. Cell 2003, 114, 663-671.
    • (2003) Cell , vol.114 , pp. 663-671
    • Cope, G.A.1    Deshaies, R.J.2
  • 88
    • 0036904663 scopus 로고    scopus 로고
    • UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis
    • Xie, Y., Varshavsky, A. UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis. Nat Cell Biol. 2002, 4, 1003-1007.
    • (2002) Nat Cell Biol. , vol.4 , pp. 1003-1007
    • Xie, Y.1    Varshavsky, A.2
  • 89
    • 0242298321 scopus 로고    scopus 로고
    • Tatbinding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel-Lindau protein
    • Corn, P. G., McDonald, E. R., 3rd, Herman, J. G., El-Deiry, W. S. Tatbinding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel-Lindau protein. Nat. Genet. 2003, 35, 229-237.
    • (2003) Nat. Genet. , vol.35 , pp. 229-237
    • Corn, P.G.1    McDonald III, E.R.2    Herman, J.G.3    El-Deiry, W.S.4
  • 90
    • 0036848655 scopus 로고    scopus 로고
    • CSN5/Jab1 mutations affect axis formation in the Drosophila oocyte by activating a meiotic checkpoint
    • Doronkin, S., Djagaeva, I., Beckendorf, S. K. CSN5/Jab1 mutations affect axis formation in the Drosophila oocyte by activating a meiotic checkpoint. Development 2002, 129, 5053-5064.
    • (2002) Development , vol.129 , pp. 5053-5064
    • Doronkin, S.1    Djagaeva, I.2    Beckendorf, S.K.3
  • 91
    • 0242525214 scopus 로고    scopus 로고
    • Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint
    • Higa, L. A., Mihaylov, I. S., Banks, D. P., Zheng, J., Zhang, H. Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint. Nat Cell Biol. 2003, 5, 1008-1015.
    • (2003) Nat Cell Biol. , vol.5 , pp. 1008-1015
    • Higa, L.A.1    Mihaylov, I.S.2    Banks, D.P.3    Zheng, J.4    Zhang, H.5
  • 92
    • 18744411246 scopus 로고    scopus 로고
    • Conservation of the COP9/signalosome in budding yeast
    • Wee, S., Hetfeld, B., Dubiel, W., Wolf, D. A. Conservation of the COP9/signalosome in budding yeast. BMC Genet. 2002, 3, 15.
    • (2002) BMC Genet. , vol.3 , pp. 15
    • Wee, S.1    Hetfeld, B.2    Dubiel, W.3    Wolf, D.A.4
  • 95
    • 0037351609 scopus 로고    scopus 로고
    • Analysis of the mutational effects of the COP/DET/FUS loci on genome expression profiles reveals their overlapping yet not identical roles in regulating Arabidopsis seedling development
    • Ma, L., Zhao, H., Deng, X. W. Analysis of the mutational effects of the COP/DET/FUS loci on genome expression profiles reveals their overlapping yet not identical roles in regulating Arabidopsis seedling development. Development 2003, 130, 969-981.
    • (2003) Development , vol.130 , pp. 969-981
    • Ma, L.1    Zhao, H.2    Deng, X.W.3
  • 96
    • 0036801543 scopus 로고    scopus 로고
    • Multiple ubiquitin ligasemediated processes require COP9 signalosome and AXR1 function
    • Schwechheimer, C., Serino, G., Deng, X. W. Multiple ubiquitin ligasemediated processes require COP9 signalosome and AXR1 function. Plant Cell 2002, 14, 2553-2563.
    • (2002) Plant Cell , vol.14 , pp. 2553-2563
    • Schwechheimer, C.1    Serino, G.2    Deng, X.W.3
  • 97
    • 0038752574 scopus 로고    scopus 로고
    • The COP9 signalosome interacts physically with SCF COI1 and modulates jasmonate responses
    • Feng, S., Ma, L., Wang, X., Xie, D., Dinesh-Kumar, S. P., Wei, N., Deng, X. W. The COP9 signalosome interacts physically with SCF COI1 and modulates jasmonate responses. Plant Cell 2003, 15, 1083-1094.
    • (2003) Plant Cell , vol.15 , pp. 1083-1094
    • Feng, S.1    Ma, L.2    Wang, X.3    Xie, D.4    Dinesh-Kumar, S.P.5    Wei, N.6    Deng, X.W.7
  • 98
    • 0038414526 scopus 로고    scopus 로고
    • The COP9 signalosome interacts with SCF UFO and participates in Arabidopsis flower development
    • Wang, X., Feng, S., Nakayama, N., Crosby, W. L., Irish, V., Deng, X. W., Wei, N. The COP9 signalosome interacts with SCF UFO and participates in Arabidopsis flower development. Plant Cell 2003, 15, 1071-1082.
    • (2003) Plant Cell , vol.15 , pp. 1071-1082
    • Wang, X.1    Feng, S.2    Nakayama, N.3    Crosby, W.L.4    Irish, V.5    Deng, X.W.6    Wei, N.7
  • 100
    • 0035924693 scopus 로고    scopus 로고
    • The Id proteins and angiogenesis
    • Benezra, R., Rafii, S., Lyden, D. The Id proteins and angiogenesis. Oncogene 2001, 20, 8334-8341.
    • (2001) Oncogene , vol.20 , pp. 8334-8341
    • Benezra, R.1    Rafii, S.2    Lyden, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.