메뉴 건너뛰기




Volumn 391, Issue 6667, 1998, Pages 601-605

Retinoblastoma protein represses transcription by recruiting a histone deacetylase

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE; HISTONE DEACETYLASE; HYBRID PROTEIN; RETINOBLASTOMA PROTEIN; TRANSCRIPTION FACTOR E2F; TRICHOSTATIN A; VIRUS PROTEIN;

EID: 0032484904     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35410     Document Type: Article
Times cited : (819)

References (30)
  • 1
    • 0026716167 scopus 로고
    • The retinoblastoma gene and gene product
    • Weinberg, R. A. The retinoblastoma gene and gene product. Cancer Surv. 12, 43-57 (1992).
    • (1992) Cancer Surv. , vol.12 , pp. 43-57
    • Weinberg, R.A.1
  • 2
    • 0026526437 scopus 로고
    • E2F: A link between the Rb tumor suppressor protein and viral oncoproteins
    • Nevins, J. R. E2F: a link between the Rb tumor suppressor protein and viral oncoproteins. Science 258, 424-429 (1992).
    • (1992) Science , vol.258 , pp. 424-429
    • Nevins, J.R.1
  • 3
    • 0026652346 scopus 로고
    • A cDNA encoding a pRB-binding protein with properties of the transcription factor E2F
    • Helin, K. et al. A cDNA encoding a pRB-binding protein with properties of the transcription factor E2F. Cell 70, 337-350 (1992).
    • (1992) Cell , vol.70 , pp. 337-350
    • Helin, K.1
  • 4
    • 0027250860 scopus 로고
    • E2F-1-mediated transactivation is inhibited by complex formation with the retinoblastoma susceptibiity gene product
    • Flemington, E. K., Speck, S. H. & Kaelin, W. G. Jr E2F-1-mediated transactivation is inhibited by complex formation with the retinoblastoma susceptibiity gene product. Proc. Natl Acad. Sci. USA 90, 6914-6918 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6914-6918
    • Flemington, E.K.1    Speck, S.H.2    Kaelin Jr., W.G.3
  • 5
    • 0026636908 scopus 로고
    • Retinoblastoma protein switches the E2F site from positive to negative element
    • Weintraub, S. J., Prater, C. A. & Dean, D. C. Retinoblastoma protein switches the E2F site from positive to negative element. Nature 358, 259-261 (1992).
    • (1992) Nature , vol.358 , pp. 259-261
    • Weintraub, S.J.1    Prater, C.A.2    Dean, D.C.3
  • 6
    • 0029043839 scopus 로고
    • Direct transcriptional repression by pRB and its reversal by specific cyclins
    • Bremner, R. et al. Direct transcriptional repression by pRB and its reversal by specific cyclins. Mol. Cell. Biol. 1555, 3256-3265 (1995).
    • (1995) Mol. Cell. Biol. , vol.1555 , pp. 3256-3265
    • Bremner, R.1
  • 7
    • 0029856734 scopus 로고    scopus 로고
    • Dual mechanisms of repression of E2F1 activity by the retinoblastoma gene product
    • Zacksenhaus, E., Jiang, Z., Phillips, R. A. & Gallie, B. L. Dual mechanisms of repression of E2F1 activity by the retinoblastoma gene product. EMBO J. 15, 5917-5927 (1996).
    • (1996) EMBO J. , vol.15 , pp. 5917-5927
    • Zacksenhaus, E.1    Jiang, Z.2    Phillips, R.A.3    Gallie, B.L.4
  • 8
    • 0029958258 scopus 로고    scopus 로고
    • The Rb family contains a conserved cyclin-dependent-kinase-regulated transcriptional repressor motif
    • Chow, K. N., Starostik, P. & Dean, D. C. The Rb family contains a conserved cyclin-dependent-kinase-regulated transcriptional repressor motif. Mol. Cell. Biol. 16, 7173-7181 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 7173-7181
    • Chow, K.N.1    Starostik, P.2    Dean, D.C.3
  • 9
    • 0029977751 scopus 로고    scopus 로고
    • E2F and cell proliferation: A world turned upside down
    • Weinberg, R. A. E2F and cell proliferation: a world turned upside down. Cell 85, 457-459 (1996).
    • (1996) Cell , vol.85 , pp. 457-459
    • Weinberg, R.A.1
  • 10
    • 0025779831 scopus 로고
    • Histone acetylation and control of gene expression
    • Turner, B. M. Histone acetylation and control of gene expression. J. Cell Sci. 99, 13-20 (1991).
    • (1991) J. Cell Sci. , vol.99 , pp. 13-20
    • Turner, B.M.1
  • 11
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription?
    • Pazin, M. J. & Kadonaga, J. T. What's up and down with histone deacetylation and transcription? Cell 89, 325-328 (1997).
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 12
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida, M., Kijima, M., Akita, M. & Beppu, T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem. 265, 17174-17179 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 13
    • 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
  • 14
    • 0029762617 scopus 로고    scopus 로고
    • Domains a and B in the Rb pocket interact to form a transcriptional repressor motif
    • Chow, K. N. & Dean, D. C. Domains A and B in the Rb pocket interact to form a transcriptional repressor motif. Mol. Cell. Biol. 16, 4862-4868 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4862-4868
    • Chow, K.N.1    Dean, D.C.2
  • 15
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3
    • 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 RPD3. 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
  • 16
    • 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
  • 17
    • 0031016121 scopus 로고    scopus 로고
    • RB kinases and RB-binding proteins: New points of view
    • Taya, Y. RB kinases and RB-binding proteins: new points of view. Trends Biochem. Sci. 22, 14-17 (1997).
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 14-17
    • Taya, Y.1
  • 18
    • 0027489749 scopus 로고
    • Independent regions of adenovirus E1A are required for binding to and dissociation of E2F-protein complexes
    • Fattaey, A. R., Harlow, E. & Helin, K. Independent regions of adenovirus E1A are required for binding to and dissociation of E2F-protein complexes. Mol. Cell. Biol. 13, 7267-7277 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7267-7277
    • Fattaey, A.R.1    Harlow, E.2    Helin, K.3
  • 19
    • 2642647227 scopus 로고    scopus 로고
    • Hbrm is a downstream target for E2F1 repression by RB
    • Trouche, D. et al. Hbrm is a downstream target for E2F1 repression by RB. Proc. Natl Acad. Sci. USA 94, 11295-11300 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11295-11300
    • Trouche, D.1
  • 20
    • 0029997378 scopus 로고    scopus 로고
    • Targeting chromatin disruption: Transcription regulators that acetylate histones
    • Wolffe, A. P. & Pruss, D. Targeting chromatin disruption: Transcription regulators that acetylate histones. Cell 84, 817-819 (1996).
    • (1996) Cell , vol.84 , pp. 817-819
    • Wolffe, A.P.1    Pruss, D.2
  • 21
    • 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
  • 22
    • 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
  • 23
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylases associated with the mSin3 corepressor mediate made transcriptional repression
    • Laherty, C. D. et al. Histone deacetylases associated with the mSin3 corepressor mediate made transcriptional repression. Cell 89, 349-356 (1997).
    • (1997) Cell , vol.89 , pp. 349-356
    • Laherty, C.D.1
  • 24
    • 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
  • 25
    • 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
  • 26
    • 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
  • 27
    • 0026021882 scopus 로고
    • Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblastoma gene product
    • Kaelin, W. G., Pallas, D. C., DeCaprio, J. A., Kaye, F. & Livingston, D. M. Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblastoma gene product. Cell 64, 521-532 (1991).
    • (1991) Cell , vol.64 , pp. 521-532
    • Kaelin, W.G.1    Pallas, D.C.2    DeCaprio, J.A.3    Kaye, F.4    Livingston, D.M.5
  • 28
    • 0028334543 scopus 로고
    • DP-1: A cell cycle-regulated and phosphorylated component of transcription factor DRTF1/E2F which is functionally important for recognition by pRb and the adenovirus E4 orf 6/7 protein
    • Bandara, L. R. et al. DP-1: a cell cycle-regulated and phosphorylated component of transcription factor DRTF1/E2F which is functionally important for recognition by pRb and the adenovirus E4 orf 6/7 protein. EMBO J. 13, 3104-3114 (1994).
    • (1994) EMBO J. , vol.13 , pp. 3104-3114
    • Bandara, L.R.1
  • 29
    • 0029868335 scopus 로고    scopus 로고
    • Physical interaction between the mitogen-responsive serum response factor and myogenic bHLH proteins
    • Groisman, R. et al. Physical interaction between the mitogen-responsive serum response factor and myogenic bHLH proteins. J. Biol. Chem. 271, 5258-5264 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 5258-5264
    • Groisman, R.1
  • 30
    • 0001092291 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble
    • Dignam, J. D., Lebowitz, R. M. & Roeder, R. G. Accurate transcription initiation by RNA polymerase II in a soluble. Nucleic Acids Res. 11, 1474-1486 (1983).
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1474-1486
    • Dignam, J.D.1    Lebowitz, R.M.2    Roeder, R.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.