메뉴 건너뛰기




Volumn 391, Issue 6667, 1998, Pages 597-601

Retinoblastoma protein recruits histone deacetylase to repress transcription

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN E; GLUTATHIONE TRANSFERASE; HISTONE DEACETYLASE; ONCOPROTEIN; RETINOBLASTOMA PROTEIN; TRANSCRIPTION FACTOR E2F; TRICHOSTATIN A; VIRUS PROTEIN;

EID: 0032484989     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35404     Document Type: Article
Times cited : (1100)

References (25)
  • 1
    • 0029033861 scopus 로고
    • The retinoblastoma protein and cell cycle control
    • Weinberg, R. A. The retinoblastoma protein and cell cycle control. Cell 81, 323-330 (1995).
    • (1995) Cell , vol.81 , pp. 323-330
    • Weinberg, R.A.1
  • 2
    • 0026636908 scopus 로고
    • Retinoblastoma protein switches the E2F site from positive to negative elements
    • Weintraub, S. J., Prater, C. A. & Dean, D. C. Retinoblastoma protein switches the E2F site from positive to negative elements. Nature 358, 259-261 (1992).
    • (1992) Nature , vol.358 , pp. 259-261
    • Weintraub, S.J.1    Prater, C.A.2    Dean, D.C.3
  • 3
    • 0029043782 scopus 로고
    • Mechanism of active transcriptional repression by the retinoblastoma protein
    • Weintraub, S. J. et al. Mechanism of active transcriptional repression by the retinoblastoma protein. Nature 375, 812-815 (1995).
    • (1995) Nature , vol.375 , pp. 812-815
    • Weintraub, S.J.1
  • 4
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C. A. & Schreiber, S. L. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272, 408-411 (1996).
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 5
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD2
    • Yang, W.-M., Inouye, C., Zeng, Y., Bearss, D. & Seto, E. Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD2. Proc. Natl Acad. Sci. USA 93, 12845-12850 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 12845-12850
    • Yang, W.-M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 6
    • 17744413444 scopus 로고    scopus 로고
    • A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression
    • Heinzel, T. et al. A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature 387, 43-48 (1997).
    • (1997) Nature , vol.387 , pp. 43-48
    • Heinzel, T.1
  • 7
    • 0030959244 scopus 로고    scopus 로고
    • Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression
    • Alland, L. et al. Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression. Nature 387, 49-55 (1997).
    • (1997) Nature , vol.387 , pp. 49-55
    • Alland, L.1
  • 8
    • 0031007189 scopus 로고    scopus 로고
    • Histone deacetylase activity is required for full transcriptional repression by mSin3A
    • Hassig, C. A., Fleischer, T. C., Billin, A. N., Schreiber, S. L. & Ayer, D. E. Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell 89, 341-347 (1997).
    • (1997) Cell , vol.89 , pp. 341-347
    • Hassig, C.A.1    Fleischer, T.C.2    Billin, A.N.3    Schreiber, S.L.4    Ayer, D.E.5
  • 9
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacelylases associated with the mSin3 corepressor mediate Mad transcriptional repression
    • Laherty, C. D. et al. Histone deacelylases associated with the mSin3 corepressor mediate Mad transcriptional repression. Cell 89, 349-356 (1997).
    • (1997) Cell , vol.89 , pp. 349-356
    • Laherty, C.D.1
  • 10
    • 0030916729 scopus 로고    scopus 로고
    • Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex
    • Zhang, Y., Iratni, R., Erdjument-Bromage, H., Tempst, P. & Reinberg, D. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell 89, 357-364 (1997).
    • (1997) Cell , vol.89 , pp. 357-364
    • Zhang, Y.1    Iratni, R.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 11
    • 0030953186 scopus 로고    scopus 로고
    • Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
    • Nagy, L. et al. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 89, 373-380 (1997).
    • (1997) Cell , vol.89 , pp. 373-380
    • Nagy, L.1
  • 12
    • 0343924289 scopus 로고    scopus 로고
    • Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters
    • Kadosh, D. & Struhl, K. Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters. Cell 89, 365-371 (1997).
    • (1997) Cell , vol.89 , pp. 365-371
    • Kadosh, D.1    Struhl, K.2
  • 13
    • 0027320814 scopus 로고
    • A retinoblastoma-binding protein related to a negative regulator of Ras in yeast
    • Qian, Y.-W. et al. A retinoblastoma-binding protein related to a negative regulator of Ras in yeast. Nature 364, 648-652 (1993).
    • (1993) Nature , vol.364 , pp. 648-652
    • Qian, Y.-W.1
  • 14
    • 0025735647 scopus 로고
    • A cellular protein that competes with SV40 T antigen for binding to the retinoblastoma gene product
    • Huang, S., Lee, W.-H. & Lee, E. Y.-H. P. A cellular protein that competes with SV40 T antigen for binding to the retinoblastoma gene product. Nature 350, 160-162 (1991).
    • (1991) Nature , vol.350 , pp. 160-162
    • Huang, S.1    Lee, W.-H.2    Lee, E.Y.-H.P.3
  • 15
    • 0027520469 scopus 로고
    • The retinoblastoma protein binds E2F residues required for activation in vivo and TBP binding in vitro
    • Hagemeier, C., Cook, A. & Kouzarides, T. The retinoblastoma protein binds E2F residues required for activation in vivo and TBP binding in vitro. Nucleic Acids Res. 21, 4998-5004 (1993).
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4998-5004
    • Hagemeier, C.1    Cook, A.2    Kouzarides, T.3
  • 16
    • 0029028353 scopus 로고
    • Stimualtion of F2F1/DP1 transcriptional activity by Mdm2 oncoprotein
    • Martin, K. et al. Stimualtion of F2F1/DP1 transcriptional activity by Mdm2 oncoprotein. Nature 375, 691-694 (1995).
    • (1995) Nature , vol.375 , pp. 691-694
    • Martin, K.1
  • 17
    • 0029942908 scopus 로고    scopus 로고
    • Cell cycle regulation of the murine cyclin e gene depends on an E2F binding site in the promoter
    • Botz, J. et al. Cell cycle regulation of the murine cyclin E gene depends on an E2F binding site in the promoter. Mol. Cell Biol. 16, 3401-3409 (1996).
    • (1996) Mol. Cell Biol. , vol.16 , pp. 3401-3409
    • Botz, J.1
  • 18
    • 15444353328 scopus 로고    scopus 로고
    • pRB and p107/p130 are required for the regulated expression of different sets of E2F responsive genes
    • Hurford, R. K. Jr, Cobrinik, D., Lee, M. H. & Dyson, N. pRB and p107/p130 are required for the regulated expression of different sets of E2F responsive genes. Genes Dev. 11, 1447-1463 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 1447-1463
    • Hurford Jr., R.K.1    Cobrinik, D.2    Lee, M.H.3    Dyson, N.4
  • 19
    • 0029417271 scopus 로고
    • A proline-rich TGF-beta-responsive transcriptional activator interacts with histone H3
    • Alevizopoulos, A. et al. A proline-rich TGF-beta-responsive transcriptional activator interacts with histone H3. Genes Dev. 9, 3051-3066 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 3051-3066
    • Alevizopoulos, A.1
  • 20
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone aceryltransferase
    • Bannister, A. J. & Kouzarides, T. The CBP co-activator is a histone aceryltransferase. Nature 384, 641-643 (1996).
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 21
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 CBP are histone acetyltransferases
    • Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H. & Nakatani, Y, The transcriptional coactivators p300 CBP are histone acetyltransferases. Cell 87, 953-959 (1996).
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 22
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W. & Roeder, R. G. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90, 595-606 (1997).
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 23
    • 0028911033 scopus 로고
    • Activity of RNA polymerase 1 transcription factor UBF blocked by Rb gene product
    • Cavanaugh, A. H. et al. Activity of RNA polymerase 1 transcription factor UBF blocked by Rb gene product. Nature 374, 177-180 (1995).
    • (1995) Nature , vol.374 , pp. 177-180
    • Cavanaugh, A.H.1
  • 24
    • 0029901988 scopus 로고    scopus 로고
    • Repression of RNA polymerase III transcription by the retinoblasioma protein
    • White, R. J., Trouche, D., Martin, K., Jackson, S. P, & Kouzarides, T. Repression of RNA polymerase III transcription by the retinoblasioma protein. Nature 382, 88-90 (1996).
    • (1996) Nature , vol.382 , pp. 88-90
    • White, R.J.1    Trouche, D.2    Martin, K.3    Jackson, S.P.4    Kouzarides, T.5
  • 25
    • 0030943759 scopus 로고    scopus 로고
    • Mechanistic analysis of RNA polymerase III regulation by the retinoblastoma protein
    • Larminie, C. G. et al. Mechanistic analysis of RNA polymerase III regulation by the retinoblastoma protein. EMBO J. 16, 2061-2071 (1997).
    • (1997) EMBO J. , vol.16 , pp. 2061-2071
    • Larminie, C.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.