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Volumn 52, Issue 3, 2010, Pages 195-203

Proteasomes and their role in transcriptional regulation

Author keywords

DNA damage; Post translational modifications; Proteasome; Transcription

Indexed keywords

ATP DEPENDENT 26S PROTEASE; PROTEASOME;

EID: 77952061595     PISSN: 00413771     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (9)

References (84)
  • 1
    • 35748950163 scopus 로고    scopus 로고
    • Damage-Induced Ubiquitylation of Human RNA Polymerase II by the Ubiquitin Ligase Nedd4, but Not Cockayne Syndrome Proteins or BRCA1
    • DOI 10.1016/j.molcel.2007.10.008, PII S1097276507006715
    • Anindya R., Aygun O., Svejstrup J. Q. 2007. Damage-induced ubiquitylation of human RNA polymerase II by the ubiquitin ligase Nedd4, but not cockayne syndrome proteins or BRCA1. Mol. Cell. 28: 386-397. (Pubitemid 350047546)
    • (2007) Molecular Cell , vol.28 , Issue.3 , pp. 386-397
    • Anindya, R.1    Aygun, O.2    Svejstrup, J.Q.3
  • 2
    • 13244275245 scopus 로고    scopus 로고
    • A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73
    • DOI 10.1101/gad.319905
    • Asher G., Tsvetkov P., Kahana C., Shaul Y. 2005. A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73. Genes Develop. 19: 316-321. (Pubitemid 40189294)
    • (2005) Genes and Development , vol.19 , Issue.3 , pp. 316-321
    • Asher, G.1    Tsvetkov, P.2    Kahana, C.3    Shaul, Y.4
  • 4
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • DOI 10.1016/S0092-8674(00)80929-0
    • Baumeister W., Walz J., Zuhl F., Seemuller E. 1998. The proteasome: paradigm of a self-compartmentalizing protease. Cell. 92: 367-380. (Pubitemid 28093014)
    • (1998) Cell , vol.92 , Issue.3 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 5
    • 0029143239 scopus 로고
    • Nuclear multicatalytic proteinase alpha subunit RRC3: Differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment
    • Benedict C. M., Ren L., Clawson G. A. 1995. Nuclear multicatalytic proteinase alpha subunit RRC3: differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment. Biochemistry. 34: 9587-9598.
    • (1995) Biochemistry , vol.34 , pp. 9587-9598
    • Benedict, C.M.1    Ren, L.2    Clawson, G.A.3
  • 6
    • 0035863064 scopus 로고    scopus 로고
    • Gamma-Interferon decreases the level of 26 S proteasomes and changes the pattern of phosphorylation
    • DOI 10.1042/0264-6021:3530291
    • Bose S., Brooks P., Mason G. G., Rivett A. J. 2001. Gamma-Interferon decreases the level of 26S proteasomes and changes the pattern of phosphorylation. Biochem. J. 353: 291-297. (Pubitemid 32096938)
    • (2001) Biochemical Journal , vol.353 , Issue.2 , pp. 291-297
    • Bose, S.1    Brooks, P.2    Mason, G.G.F.3    Rivett, A.J.4
  • 8
    • 1542344946 scopus 로고    scopus 로고
    • Phosphorylation of 20S proteasome alpha subunit C8 (alpha7) stabilizes the 26S proteasome and plays a role in the regulation of proteasome complexes by gamma-interferon
    • DOI 10.1042/BJ20031122
    • Bose S., Stratford F. L., Broadfoot K. I., Mason G. G., Rivett A. J. 2004. Phosphorylation of 20S proteasome alpha subunit C8 (alpha7) stabilizes the 26S proteasome and plays a role in the regulation of proteasome complexes by gamma-interferon. Biochem. J. 378: 177-184. (Pubitemid 38299555)
    • (2004) Biochemical Journal , vol.378 , Issue.1 , pp. 177-184
    • Bose, S.1    Stratford, F.L.L.2    Broadfoot, K.I.3    Mason, G.G.F.4    Rivett, A.J.5
  • 9
    • 0034647563 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of the proapoptotic active form of bid. A functional consequence on apoptosis induction
    • DOI 10.1074/jbc.M001083200
    • Breitschopf K., Zeiher A. M., Dimmeler S. 2000. Ubiquitin-mediated degradation of the proapoptotic active form of bid. A functional consequence on apoptosis induction. J. Biol. Chem. 275: 21 648-21 652. (Pubitemid 30481872)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.28 , pp. 21648-21652
    • Breitschopf, K.1    Zeiher, A.M.2    Dimmeler, S.3
  • 10
    • 0029876795 scopus 로고    scopus 로고
    • Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis
    • DOI 10.1021/bi952540s
    • Castano J. G., Mahillo E., Arizti P., Arribas J. 1996. Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis. Biochemistry. 35: 3782-3789. (Pubitemid 26102167)
    • (1996) Biochemistry , vol.35 , Issue.12 , pp. 3782-3789
    • Castano, J.G.1    Mahillo, E.2    Arizti, P.3    Arribas, J.4
  • 11
    • 65249083913 scopus 로고    scopus 로고
    • Ubiquitin in NF-kappaB signaling
    • Chiu Y. H., Zhao M., Chen Z. J. 2009. Ubiquitin in NF-kappaB signaling. Chem. Rev. 109: 1549-1560.
    • (2009) Chem. Rev. , vol.109 , pp. 1549-1560
    • Chiu, Y.H.1    Zhao, M.2    Chen, Z.J.3
  • 12
    • 33644867538 scopus 로고    scopus 로고
    • The proteasome: A utility tool for transcription?
    • Collins G. A., Tansey W. P. 2006. The proteasome: a utility tool for transcription? Curr. Opin. Genet. Develop. 16: 197-202.
    • (2006) Curr. Opin. Genet. Develop. , vol.16 , pp. 197-202
    • Collins, G.A.1    Tansey, W.P.2
  • 14
    • 35548937755 scopus 로고    scopus 로고
    • Biting the hand that feeds: Rpn4-dependent feedback regulation of proteasome function
    • DOI 10.1016/j.bbamcr.2007.05.015, PII S0167488907001462
    • Dohmen R. J., Willers I., Marques A. J. 2007. Biting the hand that feeds: Rpn4-dependent feedback regulation of proteasome function. Biochim. biophys. acta. 1773: 1599-1604. (Pubitemid 350018910)
    • (2007) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1773 , Issue.11 , pp. 1599-1604
    • Dohmen, R.J.1    Willers, I.2    Marques, A.J.3
  • 15
    • 1242271997 scopus 로고    scopus 로고
    • Proteasomal ATPases Link Ubiquitylation of Histone H2B to Methylation of Histone H3
    • DOI 10.1016/S1097-2765(04)00026-7
    • Ezhkova E., Tansey W. P. 2004. Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3. Mol. Cell. 13: 435-442. (Pubitemid 38229815)
    • (2004) Molecular Cell , vol.13 , Issue.3 , pp. 435-442
    • Ezhkova, E.1    Tansey, W.P.2
  • 16
    • 0035143449 scopus 로고    scopus 로고
    • Polo-like kinase interacts with proteasomes and regulates their activity
    • Feng Y., Longo D. L., Ferris D. K. 2001. Polo-like kinase interacts with proteasomes and regulates their activity. Cell Growth Differ. 12: 29-37. (Pubitemid 32107510)
    • (2001) Cell Growth and Differentiation , vol.12 , Issue.1 , pp. 29-37
    • Feng, Y.1    Longo, D.L.2    Ferris, D.K.3
  • 17
    • 0035947238 scopus 로고    scopus 로고
    • The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II
    • DOI 10.1016/S1097-2765(01)00250-7
    • Ferdous A., Gonzalez F., Sun L., Kodadek T., Johnston S. A. 2001. The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II. Mol. Cell. 7: 981-991. (Pubitemid 32525745)
    • (2001) Molecular Cell , vol.7 , Issue.5 , pp. 981-991
    • Ferdous, A.1    Gonzalez, F.2    Sun, L.3    Kodadek, T.4    Johnston, S.A.5
  • 18
    • 0037159223 scopus 로고    scopus 로고
    • A nonproteolytic function of the 19S regulatory subunit of the 26S proteasome is required for efficient activated transcription by human RNA polymerase II
    • DOI 10.1021/bi020425t
    • Ferdous A., Kodadek T., Johnston S. A. 2002. A nonproteolytic function of the 19S regulatory subunit of the 26S proteasome is required for efficient activated transcription by human RNA polymerase II. Biochemistry. 41: 12 798-12 805. (Pubitemid 35192508)
    • (2002) Biochemistry , vol.41 , Issue.42 , pp. 12798-12805
    • Ferdous, A.1    Kodadek, T.2    Johnston, S.A.3
  • 19
    • 33846132939 scopus 로고    scopus 로고
    • The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promoters
    • DOI 10.1101/gad.1493207
    • Ferdous A., Sikder D., Gillette T., Nalley K., Kodadek T., Johnston S. A. 2007. The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promoters. Genes Develop. 21: 112-123. (Pubitemid 46089712)
    • (2007) Genes and Development , vol.21 , Issue.1 , pp. 112-123
    • Ferdous, A.1    Sikder, D.2    Gillette, T.3    Nalley, K.4    Kodadek, T.5    Johnston, S.A.6
  • 20
    • 0036683779 scopus 로고    scopus 로고
    • In vivo and in vitro phosphorylation of Candida albicans 20S proteasome
    • DOI 10.1016/S0003-9861(02)00248-5, PII S0003986102002485
    • Fernandez-Murray P., Pardo P. S., Zelada A. M., Passeron S. 2002. In vivo and in vitro phosphorylation of Candida albicans 20S proteasome. Arch. Biochem. Biophys. 404: 116-125. (Pubitemid 34876287)
    • (2002) Archives of Biochemistry and Biophysics , vol.404 , Issue.1 , pp. 116-125
    • Fernandez Murray, P.1    Pardo, P.S.2    Zelada, A.M.3    Passeron, S.4
  • 21
    • 0030948085 scopus 로고    scopus 로고
    • SUG1, a putative transcriptional mediator and subunit of the PA700 proteasome regulatory complex, is a DNA helicase
    • DOI 10.1074/jbc.272.11.7122
    • Fraser R. A., Rossignol M., Heard D. J., Egly J. M., Chambon P. 1997. SUG1, a putative transcriptional mediator and subunit of the PA700 proteasome regulatory complex, is a DNA helicase. J. Biol. Chem. 272: 7122-7126. (Pubitemid 27166417)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.11 , pp. 7122-7126
    • Fraser, R.A.1    Rossignol, M.2    Heard, D.J.3    Egly, J.-M.4    Chambon, P.5
  • 22
    • 34249811193 scopus 로고    scopus 로고
    • The 20S proteasome isolated from Alzheimer's disease brain shows post-translational modifications but unchanged proteolytic activity
    • Gillardon F., Kloss A., Berg M., Neumann M., Mechtler K., Hengerer B., Dahlmann B. 2007. The 20S proteasome isolated from Alzheimer's disease brain shows post-translational modifications but unchanged proteolytic activity. J. Neurochem. 101: 1483-1490.
    • (2007) J. Neurochem , vol.101 , pp. 1483-1490
    • Gillardon, F.1    Kloss, A.2    Berg, M.3    Neumann, M.4    Mechtler, K.5    Hengerer, B.6    Dahlmann, B.7
  • 24
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman M. H., Ciechanover A. 2002. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82: 373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 25
    • 0037134015 scopus 로고    scopus 로고
    • Recruitment of a 19S proteasome subcomplex to an activated promoter
    • Gonzalez F., Delahodde A., Kodadek T., Johnston S. A. 2002. Recruitment of a 19S proteasome subcomplex to an activated promoter. Science. 296: 548-550.
    • (2002) Science , vol.296 , pp. 548-550
    • Gonzalez, F.1    Delahodde, A.2    Kodadek, T.3    Johnston, S.A.4
  • 26
    • 3242683251 scopus 로고    scopus 로고
    • P38 MAPK mediates TNF-induced apoptosis in endothelial cells via phosphorylation and downregulation of Bcl-x(L)
    • Grethe S., Ares M. P., Andersson T., Porn-Ares M. I. 2004. p38 MAPK mediates TNF-induced apoptosis in endothelial cells via phosphorylation and downregulation of Bcl-x(L). Exp. Cell Res. 298: 632-642.
    • (2004) Exp. Cell Res. , vol.298 , pp. 632-642
    • Grethe, S.1    Ares, M.P.2    Andersson, T.3    Porn-Ares, M.I.4
  • 28
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., Oren M. 1997. Mdm2 promotes the rapid degradation of p53. Nature. 387: 296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 29
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden M. S., Ghosh S. 2008. Shared principles in NF-kappaB signaling. Cell. 132: 344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 30
    • 36849069924 scopus 로고    scopus 로고
    • Inhibition of paclitaxel-induced proteasome activation influences paclitaxel cytotoxicity in breast cancer cells in a sequence-dependent manner
    • Hernandez-Vargas H., von Kobbe C., Sanchez-Estevez C., Julian-Tendero M., Palacios J., Moreno-Bueno G. 2007. Inhibition of paclitaxel-induced proteasome activation influences paclitaxel cytotoxicity in breast cancer cells in a sequence-dependent manner. Cell Cycle. 6: 2662-2668.
    • (2007) Cell Cycle , vol.6 , pp. 2662-2668
    • Hernandez-Vargas, H.1    Von Kobbe, C.2    Sanchez-Estevez, C.3    Julian-Tendero, M.4    Palacios, J.5    Moreno-Bueno, G.6
  • 31
    • 26444512037 scopus 로고    scopus 로고
    • The oncoprotein gankyrin negatively regulates both p53 and RB by enhancing proteasomal degradation
    • Higashitsuji H., Liu Y., Mayer R. J., Fujita J. 2005. The oncoprotein gankyrin negatively regulates both p53 and RB by enhancing proteasomal degradation. Cell Cycle. 4: 1335-1337. (Pubitemid 41437115)
    • (2005) Cell Cycle , vol.4 , Issue.10 , pp. 1335-1337
    • Higashitsuji, H.1    Liu, Y.2    Mayer, R.J.3    Fujita, J.4
  • 32
    • 5644266525 scopus 로고    scopus 로고
    • Identification of a protein kinase which phosphorylates a subunit of the 26S proteasome and changes in its activity during meiotic cell cycle in goldfish oocytes
    • Horiguchi R., Yoshikuni M., Tokumoto M., Nagahama Y., Tokumoto T. 2005. Identification of a protein kinase which phosphorylates a subunit of the 26S proteasome and changes in its activity during meiotic cell cycle in goldfish oocytes. Cell Signal. 17: 205-215.
    • (2005) Cell Signal , vol.17 , pp. 205-215
    • Horiguchi, R.1    Yoshikuni, M.2    Tokumoto, M.3    Nagahama, Y.4    Tokumoto, T.5
  • 33
    • 33847753121 scopus 로고    scopus 로고
    • Degradation of NFAT5, a transcriptional regulator of osmotic stress-related genes, is a critical event for doxorubicin-induced cytotoxicity in cardiac myocytes
    • Ito T., Fujio Y., Takahashi K., Azuma J. 2007. Degradation of NFAT5, a transcriptional regulator of osmotic stress-related genes, is a critical event for doxorubicin-induced cytotoxicity in cardiac myocytes. J. Biol. Chem. 282: 1152-1160.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1152-1160
    • Ito, T.1    Fujio, Y.2    Takahashi, K.3    Azuma, J.4
  • 34
    • 0036177305 scopus 로고    scopus 로고
    • Electrophoretic analysis of phosphorylation of the yeast 20S proteasome
    • Iwafune Y., Kawasaki H., Hirano H. 2002. Electrophoretic analysis of phosphorylation of the yeast 20S proteasome. Electrophoresis. 23: 329-338.
    • (2002) Electrophoresis , vol.23 , pp. 329-338
    • Iwafune, Y.1    Kawasaki, H.2    Hirano, H.3
  • 35
    • 5344237367 scopus 로고    scopus 로고
    • Identification of three phosphorylation sites in the alpha7 subunit of the yeast 20S proteasome in vivo using mass spectrometry
    • Iwafune Y., Kawasaki H., Hirano H. 2004. Identification of three phosphorylation sites in the alpha7 subunit of the yeast 20S proteasome in vivo using mass spectrometry. Arch. Biochem. Biophys. 431: 9-15.
    • (2004) Arch. Biochem. Biophys. , vol.431 , pp. 9-15
    • Iwafune, Y.1    Kawasaki, H.2    Hirano, H.3
  • 36
    • 2642560445 scopus 로고    scopus 로고
    • Proteasomal degradation of RPN4 via two distinct mechanisms, ubiquitin-dependent and -independent
    • Ju D., Xie Y. 2004. Proteasomal degradation of RPN4 via two distinct mechanisms, ubiquitin-dependent and -independent. J. Biol. Chem. 279: 23 851-23 854.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23851-23854
    • Ju, D.1    Xie, Y.2
  • 37
    • 27744492409 scopus 로고    scopus 로고
    • Mechanisms of protein degradation: An odyssey with ODC
    • Kahana C., Asher G., Shaul Y. 2005. Mechanisms of protein degradation: an odyssey with ODC. Cell Cycle. 4: 1461-1464.
    • (2005) Cell Cycle , vol.4 , pp. 1461-1464
    • Kahana, C.1    Asher, G.2    Shaul, Y.3
  • 38
    • 34347327136 scopus 로고    scopus 로고
    • Proteasome activity modulates chromatin modifications and RNA polymerase II phosphorylation to enhance glucocorticoid receptor-mediated transcription
    • Kinyamu H. K., Archer T. K. 2007. Proteasome activity modulates chromatin modifications and RNA polymerase II phosphorylation to enhance glucocorticoid receptor-mediated transcription. Mol. Cell. Biol. 27: 4891-4904.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4891-4904
    • Kinyamu, H.K.1    Archer, T.K.2
  • 39
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol
    • Kisselev A. F., Akopian T. N., Castillo V., Goldberg A. L. 1999. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol. Cell. 4: 395-402.
    • (1999) Cell , Issue.4 , pp. 395-402
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 40
    • 18844407814 scopus 로고    scopus 로고
    • BRCA1/BARD1 inhibition of mRNA 3' processing involves targeted degradation of RNA polymerase II
    • Kleiman F. E., Wu-Baer F., Fonseca D., Kaneko S., Baer R., Manley J. L. 2005. BRCA1/BARD1 inhibition of mRNA 3' processing involves targeted degradation of RNA polymerase II. Genes Develop. 19: 1227-1237.
    • (2005) Genes Develop , vol.19 , pp. 1227-1237
    • Kleiman, F.E.1    Wu-Baer, F.2    Fonseca, D.3    Kaneko, S.4    Baer, R.5    Manley, J.L.6
  • 41
    • 33750023437 scopus 로고    scopus 로고
    • Keeping transcriptional activators under control
    • Kodadek T., Sikder D., Nalley K. 2006. Keeping transcriptional activators under control. Cell. 127: 261-264.
    • (2006) Cell , vol.127 , pp. 261-264
    • Kodadek, T.1    Sikder, D.2    Nalley, K.3
  • 43
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat M. H., Jones S. N., Vousden K. H. 1997. Regulation of p53 stability by Mdm2. Nature. 387: 299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 44
    • 2942715351 scopus 로고    scopus 로고
    • VP16 and ubiquitin; Binding of P-TEFb via its activation domain and ubiquitin facilitates elongation of transcription of target genes
    • Kurosu T., Peterlin B. M. 2004. VP16 and ubiquitin; binding of P-TEFb via its activation domain and ubiquitin facilitates elongation of transcription of target genes. Curr. Biol. 14: 1112-1116.
    • (2004) Curr. Biol. , Issue.14 , pp. 1112-1116
    • Kurosu, T.1    Peterlin, B.M.2
  • 45
    • 27544486193 scopus 로고    scopus 로고
    • The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators
    • Lee D., Ezhkova E., Li B., Pattenden S. G., Tansey W. P., Workman J. L. 2005. The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators. Cell. 123: 423-436.
    • (2005) Cell , Issue.123 , pp. 423-436
    • Lee, D.1    Ezhkova, E.2    Li, B.3    Pattenden, S.G.4    Tansey, W.P.5    Workman, J.L.6
  • 46
    • 27744495040 scopus 로고    scopus 로고
    • A putative stimulatory role for activator turnover in gene expression
    • Lipford J. R., Smith G. T., Chi Y., Deshaies R. J. 2005. A putative stimulatory role for activator turnover in gene expression. Nature. 438: 113-116.
    • (2005) Nature , vol.438 , pp. 113-116
    • Lipford, J.R.1    Smith, G.T.2    Chi, Y.3    Deshaies, R.J.4
  • 47
    • 57349171307 scopus 로고    scopus 로고
    • A therapeutic dose of doxorubicin activates ubiquitin-proteasome system-mediated proteolysis by acting on both the ubiquitination apparatus and proteasome
    • Liu J., Zheng H., Tang M., Ryu Y. C., Wang X. 2008. A therapeutic dose of doxorubicin activates ubiquitin-proteasome system-mediated proteolysis by acting on both the ubiquitination apparatus and proteasome. Amer. J. Physiol. Heart Circ. Physiol. 295: H2541-2550.
    • (2008) Amer. J. Physiol. Heart Circ. Physiol. , vol.295
    • Liu, J.1    Zheng, H.2    Tang, M.3    Ryu, Y.C.4    Wang, X.5
  • 48
    • 0027267492 scopus 로고
    • Copurification of casein kinase II with 20S proteasomes and phosphorylation of a 30-kDa proteasome subunit
    • Ludemann R., Lerea K. M., Etlinger J. D. 1993. Copurification of casein kinase II with 20S proteasomes and phosphorylation of a 30-kDa proteasome subunit. J. Biol. Chem. 268: 17 413-17 417.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17413-17417
    • Ludemann, R.1    Lerea, K.M.2    Etlinger, J.D.3
  • 49
    • 0033004441 scopus 로고    scopus 로고
    • Rpn4p acts as a transcription factor by binding to PACE, a nonamer box found upstream of 26S proteasomal and other genes in yeast
    • Mannhaupt G., Schnall R., Karpov V., Vetter I., Feldmann H. 1999. Rpn4p acts as a transcription factor by binding to PACE, a nonamer box found upstream of 26S proteasomal and other genes in yeast. FEBS Lett. 450: 27-34.
    • (1999) FEBS Lett , vol.450 , pp. 27-34
    • Mannhaupt, G.1    Schnall, R.2    Karpov, V.3    Vetter, I.4    Feldmann, H.5
  • 50
    • 0029892643 scopus 로고    scopus 로고
    • Phosphorylation of proteasomes in mammalian cells. Identification of two phosphorylated subunits and the effect of phosphorylation on activity
    • Mason G. G., Hendil K. B., Rivett A. J. 1996. Phosphorylation of proteasomes in mammalian cells. Identification of two phosphorylated subunits and the effect of phosphorylation on activity. Eur. J. Biochem. 238: 453-462.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 453-462
    • Mason, G.G.1    Hendil, K.B.2    Rivett, A.J.3
  • 51
    • 0036678959 scopus 로고    scopus 로고
    • Role and function of the 26S proteasome in proliferation and apoptosis
    • Naujokat C., Hoffmann S. 2002. Role and function of the 26S proteasome in proliferation and apoptosis. Lab. Invest. 82: 965-980.
    • (2002) Lab. Invest. , vol.82 , pp. 965-980
    • Naujokat, C.1    Hoffmann, S.2
  • 52
    • 0032518167 scopus 로고    scopus 로고
    • In vivo and in vitro phosphorylation of the alpha 7/PRS1 subunit of Saccharomyces cerevisiae 20S proteasome: In vitro phosphorylation by protein kinase CK2 is absolutely dependent on polylysine
    • Pardo P. S., Murray P. F., Walz K., Franco L., Passeron S. 1998. In vivo and in vitro phosphorylation of the alpha 7/PRS1 subunit of Saccharomyces cerevisiae 20S proteasome: in vitro phosphorylation by protein kinase CK2 is absolutely dependent on polylysine. Arch. Biochem. Biophys. 349: 397-401.
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 397-401
    • Pardo, P.S.1    Murray, P.F.2    Walz, K.3    Franco, L.4    Passeron, S.5
  • 53
    • 0034460132 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of the coactivator p300 impairs cardiac transcription
    • Poizat C., Sartorelli V., Chung G., Kloner R. A., Kedes L. 2000. Proteasome-mediated degradation of the coactivator p300 impairs cardiac transcription. Mol. Cell. Biol. 20: 8643-8654.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8643-8654
    • Poizat, C.1    Sartorelli, V.2    Chung, G.3    Kloner, R.A.4    Kedes, L.5
  • 54
  • 55
    • 9644302406 scopus 로고    scopus 로고
    • Productive RUPture: Activation of transcription factors by proteasomal processing
    • Rape M., Jentsch S. 2004. Productive RUPture: activation of transcription factors by proteasomal processing. Biochim. biophys. acta. 1695: 209-213.
    • (2004) Biochim. Biophys. Acta. , vol.1695 , pp. 209-213
    • Rape, M.1    Jentsch, S.2
  • 56
    • 3142691854 scopus 로고    scopus 로고
    • DNA damage-induced Def-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro
    • Reid J., Svejstrup J. Q. 2004. DNA damage-induced Def-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro. J. Biol. Chem. 279: 29 875-29 878.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29875-29878
    • Reid, J.1    Svejstrup, J.Q.2
  • 57
    • 0035070697 scopus 로고    scopus 로고
    • Regulation of proteasome complexes by gamma-interferon and phosphorylation
    • Rivett A. J., Bose S., Brooks P., Broadfoot K. I. 2001. Regulation of proteasome complexes by gamma-interferon and phosphorylation. Biochimie. 83: 363-366.
    • (2001) Biochimie , Issue.83 , pp. 363-366
    • Rivett, A.J.1    Bose, S.2    Brooks, P.3    Broadfoot, K.I.4
  • 58
    • 0029132743 scopus 로고
    • Phosphorylation of proteasome substrate by a protein kinase associated with the 26S proteasome is linked to the ATP-dependent proteolysis of the 26S proteasome
    • Satoh K., Nishikawa T., Yokosawa H., Sawada H. 1995. Phosphorylation of proteasome substrate by a protein kinase associated with the 26S proteasome is linked to the ATP-dependent proteolysis of the 26S proteasome. Biochem. Biophys. Res. Commun. 213: 7-14.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 7-14
    • Satoh, K.1    Nishikawa, T.2    Yokosawa, H.3    Sawada, H.4
  • 59
    • 0035895354 scopus 로고    scopus 로고
    • Assembly of the 26S proteasome is regulated by phosphorylation of the p45/Rpt6 ATPase subunit
    • Satoh K., Sasajima H., Nyoumura K.I., Yokosawa H., Sawada H. 2001. Assembly of the 26S proteasome is regulated by phosphorylation of the p45/Rpt6 ATPase subunit. Biochemistry. 40: 314-319.
    • (2001) Biochemistry , vol.40 , pp. 314-319
    • Satoh, K.1    Sasajima, H.2    Nyoumura, K.I.3    Yokosawa, H.4    Sawada, H.5
  • 60
    • 28444437051 scopus 로고    scopus 로고
    • MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein
    • Sdek P., Ying H., Chang D. L., Qiu W., Zheng H., Touitou R., Allday M. J., Xiao Z. X. 2005. MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein. Mol. Cell. 20: 699-708.
    • (2005) Mol. Cell. , vol.20 , pp. 699-708
    • Sdek, P.1    Ying, H.2    Chang, D.L.3    Qiu, W.4    Zheng, H.5    Touitou, R.6    Allday, M.J.7    Xiao, Z.X.8
  • 61
    • 13944252067 scopus 로고    scopus 로고
    • The life cycle of C-myc: From synthesis to degradation
    • Sears R. C. 2004. The life cycle of C-myc: from synthesis to degradation. Cell Cycle. 3: 1133-1137.
    • (2004) Cell Cycle , vol.3 , pp. 1133-1137
    • Sears, R.C.1
  • 62
    • 33748753648 scopus 로고    scopus 로고
    • Widespread, but non-identical, association of proteasomal 19 and 20S proteins with yeast chromatin
    • Sikder D., Johnston S. A., Kodadek T. 2006. Widespread, but non-identical, association of proteasomal 19 and 20S proteins with yeast chromatin. J. Biol. Chem. 281: 27 346-27 355.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27346-27355
    • Sikder, D.1    Johnston, S.A.2    Kodadek, T.3
  • 63
    • 20444428382 scopus 로고    scopus 로고
    • Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest
    • Somesh B. P., Reid J., Liu W. F., Sogaard T. M., Erdjument-Bromage H., Tempst P., Svejstrup J. Q. 2005. Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell. 121: 913-923.
    • (2005) Cell , vol.121 , pp. 913-923
    • Somesh, B.P.1    Reid, J.2    Liu, W.F.3    Sogaard, T.M.4    Erdjument-Bromage, H.5    Tempst, P.6    Svejstrup, J.Q.7
  • 64
    • 33947720525 scopus 로고    scopus 로고
    • Communication between distant sites in RNA polymerase II through ubiquitylation factors and the polymerase CTD
    • Somesh B. P., Sigurdsson S., Saeki H., Erdjument-Bromage H., Tempst P., Svejstrup J. Q. 2007. Communication between distant sites in RNA polymerase II through ubiquitylation factors and the polymerase CTD. Cell. 129: 57-68.
    • (2007) Cell , vol.129 , pp. 57-68
    • Somesh, B.P.1    Sigurdsson, S.2    Saeki, H.3    Erdjument-Bromage, H.4    Tempst, P.5    Svejstrup, J.Q.6
  • 65
    • 0033591451 scopus 로고    scopus 로고
    • An N-terminal region of Sp1 targets its proteasome-dependent degradation in vitro
    • Su K., Roos M. D., Yang X., Han I., Paterson A. J., Kudlow J. E. 1999. An N-terminal region of Sp1 targets its proteasome-dependent degradation in vitro. J. Biol. Chem. 274: 15194-15202.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15194-15202
    • Su, K.1    Roos, M.D.2    Yang, X.3    Han, I.4    Paterson, A.J.5    Kudlow, J.E.6
  • 66
    • 33644993615 scopus 로고    scopus 로고
    • The proteasomal ATPase complex is required for stress-induced transcription in yeast
    • Sulahian R., Sikder D., Johnston S. A., Kodadek T. 2006. The proteasomal ATPase complex is required for stress-induced transcription in yeast. Nucl. Acids Res. 34: 1351-1357.
    • (2006) Nucl. Acids Res. , vol.34 , pp. 1351-1357
    • Sulahian, R.1    Sikder, D.2    Johnston, S.A.3    Kodadek, T.4
  • 67
    • 0036384370 scopus 로고    scopus 로고
    • Physical association of the APIS complex and general transcription factors
    • Sun L., Johnston S. A., Kodadek T. 2002. Physical association of the APIS complex and general transcription factors. Biochem. Biophys. Res. Commun. 296: 991-999.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 991-999
    • Sun, L.1    Johnston, S.A.2    Kodadek, T.3
  • 68
    • 33845645536 scopus 로고    scopus 로고
    • The proteasome restricts permissive transcription at tissue-specific gene loci in embryonic stem cells
    • Szutorisz H., Georgiou A., Tora L., Dillon N. 2006. The proteasome restricts permissive transcription at tissue-specific gene loci in embryonic stem cells. Cell. 127: 1375-1388.
    • (2006) Cell , vol.127 , pp. 1375-1388
    • Szutorisz, H.1    Georgiou, A.2    Tora, L.3    Dillon, N.4
  • 69
    • 3242705721 scopus 로고    scopus 로고
    • Death, destruction, and the proteasome
    • Tansey W. P. 2004. Death, destruction, and the proteasome. N. Engl. J. Med. 351: 393-394.
    • (2004) N. Engl. J. Med. , vol.351 , pp. 393-394
    • Tansey, W.P.1
  • 70
    • 3242880721 scopus 로고    scopus 로고
    • Post-translationally modified S12, absent in transformed breast epithelial cells, is not associated with the 26S proteasome and is induced by proteasome inhibitor
    • Thompson H. G., Harris J. W., Brody J. P. 2004. Post-translationally modified S12, absent in transformed breast epithelial cells, is not associated with the 26S proteasome and is induced by proteasome inhibitor. Int. J. Cancer. 111: 338-347.
    • (2004) Int. J. Cancer. , vol.111 , pp. 338-347
    • Thompson, H.G.1    Harris, J.W.2    Brody, J.P.3
  • 71
    • 33947595988 scopus 로고    scopus 로고
    • Changes in composition and activities of 26S proteasomes under the action of doxorubicin-apoptosis inductor of erythroleukemic K562 cells
    • Tsimokha A. S., Mittenberg A. G., Kulichkova V. A., Kozhukharova I. V., Gause L. N., Konstantinova I. M. 2007. Changes in composition and activities of 26S proteasomes under the action of doxorubicin-apoptosis inductor of erythroleukemic K562 cells. Cell. Biol. Int. 31: 338-348.
    • (2007) Cell. Biol. Int. , Issue.31 , pp. 338-348
    • Tsimokha, A.S.1    Mittenberg, A.G.2    Kulichkova, V.A.3    Kozhukharova, I.V.4    Gause, L.N.5    Konstantinova, I.M.6
  • 72
    • 0030751344 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of a proteasome subunit from rice and carrot cells
    • Umeda M., Fujii N., Manabe Y., Uchimiya H. 1997. Molecular and biochemical characterization of a proteasome subunit from rice and carrot cells. Mol. Gen. Genet. 255: 19-27.
    • (1997) Mol. Gen. Genet. , vol.255 , pp. 19-27
    • Umeda, M.1    Fujii, N.2    Manabe, Y.3    Uchimiya, H.4
  • 73
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., Baumeister W. 1999. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68: 1015-1068.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 75
    • 33947380146 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the affinity-purified human 26S proteasome complex
    • Wang X., Chen C. F., Baker P. R., Chen P. L., Kaiser P., Huang L. 2007. Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry. 46: 3553-3565.
    • (2007) Biochemistry , vol.46 , pp. 3553-3565
    • Wang, X.1    Chen, C.F.2    Baker, P.R.3    Chen, P.L.4    Kaiser, P.5    Huang, L.6
  • 78
    • 0035853037 scopus 로고    scopus 로고
    • RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: A negative feedback circuit
    • Xie Y., Varshavsky A. 2001. RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit. Proc. Nat. Acad. Sci. USA. 98: 3056-3061.
    • (2001) Proc. Nat. Acad. Sci. USA , vol.98 , pp. 3056-3061
    • Xie, Y.1    Varshavsky, A.2
  • 79
    • 33644770294 scopus 로고    scopus 로고
    • Targeting retinoblastoma protein for degradation by proteasomes
    • Ying H., Xiao Z. X. 2006. Targeting retinoblastoma protein for degradation by proteasomes. Cell Cycle. 5: 506-508.
    • (2006) Cell Cycle , vol.5 , pp. 506-508
    • Ying, H.1    Xiao, Z.X.2
  • 80
    • 34547953209 scopus 로고    scopus 로고
    • Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6
    • Zhang F., Hu Y., Huang P., Toleman C. A., Paterson A. J., Kudlow J. E. 2007. Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6. J. Biol. Chem. 282: 22 460-22 471.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22460-22471
    • Zhang, F.1    Hu, Y.2    Huang, P.3    Toleman, C.A.4    Paterson, A.J.5    Kudlow, J.E.6
  • 81
    • 33748947865 scopus 로고    scopus 로고
    • The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription
    • Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R., Sun X., Shang Y. 2006. The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription. EMBO J. 25: 4223-4233.
    • (2006) EMBO J , vol.25 , pp. 4223-4233
    • Zhang, H.1    Sun, L.2    Liang, J.3    Yu, W.4    Zhang, Y.5    Wang, Y.6    Chen, Y.7    Li, R.8    Sun, X.9    Shang, Y.10
  • 82
    • 69249099667 scopus 로고    scopus 로고
    • S-glutathionylation of the Rpn2 regulatory subunit inhibits 26S proteasomal function
    • Zmijewski J. W., Banerjee S., Abraham E. 2009. S-glutathionylation of the Rpn2 regulatory subunit inhibits 26S proteasomal function. J. Biol. Chem. 284: 22 213-22 221.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22213-22221
    • Zmijewski, J.W.1    Banerjee, S.2    Abraham, E.3
  • 84
    • 33845652273 scopus 로고    scopus 로고
    • Keeping the noise down in ES cells
    • Zwaka T. P. 2006. Keeping the noise down in ES cells. Cell. 127: 1301-1302.
    • (2006) Cell , vol.127 , pp. 1301-1302
    • Zwaka, T.P.1


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