메뉴 건너뛰기




Volumn 120, Issue 6, 2005, Pages 887-899

The F box protein Dsg1/Mdm30 is a transcriptional coactivator that stimulates Gal4 turnover and cotranscriptional mRNA processing

Author keywords

[No Author keywords available]

Indexed keywords

F BOX PROTEIN; MESSENGER RNA; RNA; RNA POLYMERASE II; TRANSCRIPTION FACTOR; UBIQUITIN;

EID: 17644386183     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2004.12.025     Document Type: Article
Times cited : (147)

References (45)
  • 1
    • 0030978351 scopus 로고    scopus 로고
    • Beta-catenin is a target for the ubiquitin-proteasome pathway
    • H. Aberle, A. Bauer, J. Stappert, A. Kispert, and R. Kemler Beta-catenin is a target for the ubiquitin-proteasome pathway EMBO J. 16 1997 3797 3804
    • (1997) EMBO J. , vol.16 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 2
    • 1542334001 scopus 로고    scopus 로고
    • Phosphorylation of serine 2 within the RNA polymerase II C-terminal domain couples transcription and 3′ end processing
    • S.H. Ahn, M. Kim, and S. Buratowski Phosphorylation of serine 2 within the RNA polymerase II C-terminal domain couples transcription and 3′ end processing Mol. Cell 13 2004 67 76
    • (2004) Mol. Cell , vol.13 , pp. 67-76
    • Ahn, S.H.1    Kim, M.2    Buratowski, S.3
  • 3
    • 0021288735 scopus 로고
    • Isolation and characterization of a pleiotropic glucose repression resistant mutant of Saccharomyces cerevisiae
    • R.B. Bailey, and A. Woodword Isolation and characterization of a pleiotropic glucose repression resistant mutant of Saccharomyces cerevisiae Mol. Gen. Genet. 193 1984 507 512
    • (1984) Mol. Gen. Genet. , vol.193 , pp. 507-512
    • Bailey, R.B.1    Woodword, A.2
  • 4
    • 1542710344 scopus 로고    scopus 로고
    • Nuclear retinoid receptors and the transcription of retinoid-target genes
    • J. Bastien, and C. Rochette-Egly Nuclear retinoid receptors and the transcription of retinoid-target genes Gene 328 2004 1 16
    • (2004) Gene , vol.328 , pp. 1-16
    • Bastien, J.1    Rochette-Egly, C.2
  • 5
  • 6
    • 0035893314 scopus 로고    scopus 로고
    • Opposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser 2 of the RNA polymerase II C-terminal domain
    • E.J. Cho, M.S. Kobor, M. Kim, J. Greenblatt, and S. Buratowski Opposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser 2 of the RNA polymerase II C-terminal domain Genes Dev. 15 2001 3319 3329
    • (2001) Genes Dev. , vol.15 , pp. 3319-3329
    • Cho, E.J.1    Kobor, M.S.2    Kim, M.3    Greenblatt, J.4    Buratowski, S.5
  • 8
    • 0036252704 scopus 로고    scopus 로고
    • T7 RNA polymerase-directed transcripts are processed in yeast and link 3′ end formation to mRNA nuclear export
    • K. Dower, and M. Rosbash T7 RNA polymerase-directed transcripts are processed in yeast and link 3′ end formation to mRNA nuclear export RNA 8 2002 686 697
    • (2002) RNA , vol.8 , pp. 686-697
    • Dower, K.1    Rosbash, M.2
  • 9
    • 0037188922 scopus 로고    scopus 로고
    • Yph1p, an ORC-interacting protein: Potential links between cell proliferation control, DNA replication, and ribosome biogenesis
    • Y.C. Du, and B. Stillman Yph1p, an ORC-interacting protein: potential links between cell proliferation control, DNA replication, and ribosome biogenesis Cell 109 2002 835 848
    • (2002) Cell , vol.109 , pp. 835-848
    • Du, Y.C.1    Stillman, B.2
  • 10
    • 0038037754 scopus 로고    scopus 로고
    • Mdm30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast
    • S. Fritz, N. Weinbach, and B. Westermann Mdm30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast Mol. Biol. Cell 14 2003 2303 2313
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2303-2313
    • Fritz, S.1    Weinbach, N.2    Westermann, B.3
  • 11
    • 0032834055 scopus 로고    scopus 로고
    • EIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • A.C. Gingras, B. Raught, and N. Sonenberg eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation Annu. Rev. Biochem. 68 1999 913 963
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 12
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Y. Haupt, R. Maya, A. Kazaz, and M. Oren Mdm2 promotes the rapid degradation of p53 Nature 387 1997 296 299
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 13
    • 0032110627 scopus 로고    scopus 로고
    • Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin-dependent kinases
    • C.J. Hengartner, V.E. Myer, S.M. Liao, C.J. Wilson, S.S. Koh, and R.A. Young Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin-dependent kinases Mol. Cell 2 1998 43 53
    • (1998) Mol. Cell , vol.2 , pp. 43-53
    • Hengartner, C.J.1    Myer, V.E.2    Liao, S.M.3    Wilson, C.J.4    Koh, S.S.5    Young, R.A.6
  • 14
    • 0033000483 scopus 로고    scopus 로고
    • GAL4 is regulated by the RNA polymerase II holoenzyme-associated cyclin-dependent protein kinase SRB10/CDK8
    • M. Hirst, M.S. Kobor, N. Kuriakose, J. Greenblatt, and I. Sadowski GAL4 is regulated by the RNA polymerase II holoenzyme-associated cyclin-dependent protein kinase SRB10/CDK8 Mol. Cell 3 1999 673 678
    • (1999) Mol. Cell , vol.3 , pp. 673-678
    • Hirst, M.1    Kobor, M.S.2    Kuriakose, N.3    Greenblatt, J.4    Sadowski, I.5
  • 15
    • 0842265974 scopus 로고    scopus 로고
    • Regulation of RNA polymerase II transcription by sequence-specific DNA binding factors
    • J.T. Kadonaga Regulation of RNA polymerase II transcription by sequence-specific DNA binding factors Cell 116 2004 247 257
    • (2004) Cell , vol.116 , pp. 247-257
    • Kadonaga, J.T.1
  • 16
    • 0141557763 scopus 로고    scopus 로고
    • Bur1 kinase is required for efficient transcription elongation by RNA polymerase II
    • M.C. Keogh, V. Podolny, and S. Buratowski Bur1 kinase is required for efficient transcription elongation by RNA polymerase II Mol. Cell. Biol. 23 2003 7005 7018
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7005-7018
    • Keogh, M.C.1    Podolny, V.2    Buratowski, S.3
  • 17
    • 1542290655 scopus 로고    scopus 로고
    • Transitions in RNA polymerase II elongation complexes at the 3′ ends of genes
    • M. Kim, S.H. Ahn, N.J. Krogan, J.F. Greenblatt, and S. Buratowski Transitions in RNA polymerase II elongation complexes at the 3′ ends of genes EMBO J. 23 2004 354 364
    • (2004) EMBO J. , vol.23 , pp. 354-364
    • Kim, M.1    Ahn, S.H.2    Krogan, N.J.3    Greenblatt, J.F.4    Buratowski, S.5
  • 18
    • 0037073061 scopus 로고    scopus 로고
    • Regulation of transcription elongation by phosphorylation
    • M.S. Kobor, and J. Greenblatt Regulation of transcription elongation by phosphorylation Biochim. Biophys. Acta 1577 2002 261 275
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 261-275
    • Kobor, M.S.1    Greenblatt, J.2
  • 19
    • 0034307008 scopus 로고    scopus 로고
    • Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription
    • P. Komarnitsky, E.J. Cho, and S. Buratowski Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription Genes Dev. 14 2000 2452 2460
    • (2000) Genes Dev. , vol.14 , pp. 2452-2460
    • Komarnitsky, P.1    Cho, E.J.2    Buratowski, S.3
  • 21
    • 0141729263 scopus 로고    scopus 로고
    • Diverse roles for ubiquitin-dependent proteolysis in transcriptional activation
    • J.R. Lipford, and R.J. Deshaies Diverse roles for ubiquitin-dependent proteolysis in transcriptional activation Nat. Cell Biol. 5 2003 845 850
    • (2003) Nat. Cell Biol. , vol.5 , pp. 845-850
    • Lipford, J.R.1    Deshaies, R.J.2
  • 22
    • 0842347413 scopus 로고    scopus 로고
    • Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex
    • Y. Liu, C. Kung, J. Fishburn, A.Z. Ansari, K.M. Shokat, and S. Hahn Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex Mol. Cell. Biol. 24 2004 1721 1735
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1721-1735
    • Liu, Y.1    Kung, C.2    Fishburn, J.3    Ansari, A.Z.4    Shokat, K.M.5    Hahn, S.6
  • 23
    • 0026731557 scopus 로고
    • Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II
    • H. Lu, L. Zawel, L. Fisher, J.M. Egly, and D. Reinberg Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II Nature 358 1992 641 645
    • (1992) Nature , vol.358 , pp. 641-645
    • Lu, H.1    Zawel, L.2    Fisher, L.3    Egly, J.M.4    Reinberg, D.5
  • 24
    • 0031761689 scopus 로고    scopus 로고
    • Characterization of three related glucose repressors and genes they regulate in Saccharomyces cerevisiae
    • L.L. Lutfiyya, V.R. Iyer, J. DeRisi, M.J. DeVit, P.O. Brown, and M. Johnston Characterization of three related glucose repressors and genes they regulate in Saccharomyces cerevisiae Genetics 150 1998 1377 1391
    • (1998) Genetics , vol.150 , pp. 1377-1391
    • Lutfiyya, L.L.1    Iyer, V.R.2    Derisi, J.3    Devit, M.J.4    Brown, P.O.5    Johnston, M.6
  • 25
    • 0023643078 scopus 로고
    • The carboxy-terminal 30 amino acids of GAL4 are recognized by GAL80
    • J. Ma, and M. Ptashne The carboxy-terminal 30 amino acids of GAL4 are recognized by GAL80 Cell 50 1987 137 142
    • (1987) Cell , vol.50 , pp. 137-142
    • Ma, J.1    Ptashne, M.2
  • 26
    • 2442681755 scopus 로고    scopus 로고
    • Functional interactions of RNA-capping enzyme with factors that positively and negatively regulate promoter escape by RNA polymerase II
    • S.S. Mandal, C. Chu, T. Wada, H. Handa, A.J. Shatkin, and D. Reinberg Functional interactions of RNA-capping enzyme with factors that positively and negatively regulate promoter escape by RNA polymerase II Proc. Natl. Acad. Sci. USA 101 2004 7572 7577
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7572-7577
    • Mandal, S.S.1    Chu, C.2    Wada, T.3    Handa, H.4    Shatkin, A.J.5    Reinberg, D.6
  • 27
    • 0037041395 scopus 로고    scopus 로고
    • An extensive network of coupling among gene expression machines
    • T. Maniatis, and R. Reed An extensive network of coupling among gene expression machines Nature 416 2002 499 506
    • (2002) Nature , vol.416 , pp. 499-506
    • Maniatis, T.1    Reed, R.2
  • 29
    • 0033571527 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of transcriptional activators correlates with activation domain potency in vivo
    • E. Molinari, M. Gilman, and S. Natesan Proteasome-mediated degradation of transcriptional activators correlates with activation domain potency in vivo EMBO J. 18 1999 6439 6447
    • (1999) EMBO J. , vol.18 , pp. 6439-6447
    • Molinari, E.1    Gilman, M.2    Natesan, S.3
  • 30
    • 0345016384 scopus 로고    scopus 로고
    • Isw1 chromatin remodeling ATPase coordinates transcription elongation and termination by RNA polymerase II
    • A. Morillon, N. Karabetsou, J. O'Sullivan, N. Kent, N. Proudfoot, and J. Mellor Isw1 chromatin remodeling ATPase coordinates transcription elongation and termination by RNA polymerase II Cell 115 2003 425 435
    • (2003) Cell , vol.115 , pp. 425-435
    • Morillon, A.1    Karabetsou, N.2    O'Sullivan, J.3    Kent, N.4    Proudfoot, N.5    Mellor, J.6
  • 31
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • M. Muratani, and W.P. Tansey How the ubiquitin-proteasome system controls transcription Nat. Rev. Mol. Cell Biol. 4 2003 192 201
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 32
    • 0034972804 scopus 로고    scopus 로고
    • Phosphorylation of the RNA polymerase II carboxy-terminal domain by the Bur1 cyclin-dependent kinase
    • S. Murray, R. Udupa, S. Yao, G. Hartzog, and G. Prelich Phosphorylation of the RNA polymerase II carboxy-terminal domain by the Bur1 cyclin-dependent kinase Mol. Cell. Biol. 21 2001 4089 4096
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4089-4096
    • Murray, S.1    Udupa, R.2    Yao, S.3    Hartzog, G.4    Prelich, G.5
  • 33
    • 0025124760 scopus 로고
    • Phosphorylated forms of GAL4 are correlated with ability to activate transcription
    • L.M. Mylin, M. Johnston, and J.E. Hopper Phosphorylated forms of GAL4 are correlated with ability to activate transcription Mol. Cell. Biol. 10 1990 4623 4629
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4623-4629
    • Mylin, L.M.1    Johnston, M.2    Hopper, J.E.3
  • 35
    • 0031831274 scopus 로고    scopus 로고
    • Combinatorial control in ubiquitin-dependent proteolysis: Don't Skp the F-box hypothesis
    • E.E. Patton, A.R. Willems, and M. Tyers Combinatorial control in ubiquitin-dependent proteolysis: don't Skp the F-box hypothesis Trends Genet. 14 1998 236 243
    • (1998) Trends Genet. , vol.14 , pp. 236-243
    • Patton, E.E.1    Willems, A.R.2    Tyers, M.3
  • 36
    • 0037470160 scopus 로고    scopus 로고
    • Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality control
    • Y. Pei, B. Schwer, and S. Shuman Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality control J. Biol. Chem. 278 2003 7180 7188
    • (2003) J. Biol. Chem. , vol.278 , pp. 7180-7188
    • Pei, Y.1    Schwer, B.2    Shuman, S.3
  • 37
    • 0032493625 scopus 로고    scopus 로고
    • Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae
    • D. Rapaport, M. Brunner, W. Neupert, and B. Westermann Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae J. Biol. Chem. 273 1998 20150 20155
    • (1998) J. Biol. Chem. , vol.273 , pp. 20150-20155
    • Rapaport, D.1    Brunner, M.2    Neupert, W.3    Westermann, B.4
  • 38
    • 0010586475 scopus 로고    scopus 로고
    • The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair
    • S.J. Russell, S.H. Reed, W. Huang, E.C. Friedberg, and S.A. Johnston The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair Mol. Cell 3 1999 687 695
    • (1999) Mol. Cell , vol.3 , pp. 687-695
    • Russell, S.J.1    Reed, S.H.2    Huang, W.3    Friedberg, E.C.4    Johnston, S.A.5
  • 39
    • 0025790341 scopus 로고
    • GAL4 is phosphorylated as a consequence of transcriptional activation
    • I. Sadowski, D. Niedbala, K. Wood, and M. Ptashne GAL4 is phosphorylated as a consequence of transcriptional activation Proc. Natl. Acad. Sci. USA 88 1991 10510 10514
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10510-10514
    • Sadowski, I.1    Niedbala, D.2    Wood, K.3    Ptashne, M.4
  • 40
    • 0035979738 scopus 로고    scopus 로고
    • Regulation of transcriptional activation domain function by ubiquitin
    • S.E. Salghetti, A.A. Caudy, J.G. Chenoweth, and W.P. Tansey Regulation of transcriptional activation domain function by ubiquitin Science 293 2001 1651 1653
    • (2001) Science , vol.293 , pp. 1651-1653
    • Salghetti, S.E.1    Caudy, A.A.2    Chenoweth, J.G.3    Tansey, W.P.4
  • 41
    • 0034724166 scopus 로고    scopus 로고
    • Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis
    • S.E. Salghetti, M. Muratani, H. Wijnen, B. Futcher, and W.P. Tansey Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis Proc. Natl. Acad. Sci. USA 97 2000 3118 3123
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3118-3123
    • Salghetti, S.E.1    Muratani, M.2    Wijnen, H.3    Futcher, B.4    Tansey, W.P.5
  • 42
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Z.W. Sun, and C.D. Allis Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast Nature 418 2002 104 108
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 43
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • J. Terrell, S. Shih, R. Dunn, and L. Hicke A function for monoubiquitination in the internalization of a G protein-coupled receptor Mol. Cell 1 1998 193 202
    • (1998) Mol. Cell , vol.1 , pp. 193-202
    • Terrell, J.1    Shih, S.2    Dunn, R.3    Hicke, L.4
  • 44
    • 0029739903 scopus 로고    scopus 로고
    • Quantitation of putative activator-target affinities predicts transcriptional activating potentials
    • Y. Wu, R.J. Reece, and M. Ptashne Quantitation of putative activator-target affinities predicts transcriptional activating potentials EMBO J. 15 1996 3951 3963
    • (1996) EMBO J. , vol.15 , pp. 3951-3963
    • Wu, Y.1    Reece, R.J.2    Ptashne, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.