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Volumn 19, Issue 4, 2000, Pages 662-671

Regulation of E2F1 activity by acetylation

Author keywords

Acetylation; E2F1; Histone deacetylase; P CAF; p300; Retinoblastoma protein

Indexed keywords

ACYLTRANSFERASE; HISTONE DEACETYLASE; TRANSCRIPTION FACTOR E2F;

EID: 0343484254     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.4.662     Document Type: Article
Times cited : (583)

References (57)
  • 1
    • 0030774301 scopus 로고    scopus 로고
    • Distinct mechanisms of nuclear accumulation regulate the functional consequence of E2F transcription factors
    • Allen, K.E., de la Luna, S., Kerkhoven, R.M., Bernards, R. and La Thangue, N.B. (1997) Distinct mechanisms of nuclear accumulation regulate the functional consequence of E2F transcription factors. J. Cell Sci., 110, 2819-2831.
    • (1997) J. Cell Sci. , vol.110 , pp. 2819-2831
    • Allen, K.E.1    De La Luna, S.2    Kerkhoven, R.M.3    Bernards, R.4    La Thangue, N.B.5
  • 2
    • 0025910802 scopus 로고
    • The retinoblastoma protein copurifies with E2F-1, an E1A-regulated inhibitor of the transcription factor E2E
    • Bagchi, S., Weinmann, R. and Raychaudhuri, P. (1991) The retinoblastoma protein copurifies with E2F-1, an E1A-regulated inhibitor of the transcription factor E2E Cell, 65, 1063-1072.
    • (1991) Cell , vol.65 , pp. 1063-1072
    • Bagchi, S.1    Weinmann, R.2    Raychaudhuri, P.3
  • 3
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister, A.J. and Kouzarides, T. (1996) The CBP co-activator is a histone acetyltransferase. Nature, 384, 641-643.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 4
    • 0032506542 scopus 로고    scopus 로고
    • Regulation of activity of the transcription factor GATA-1 by acetylation
    • Boyes, J., Byfield, P., Nakatani, Y. and Ogryzko, V. (1998) Regulation of activity of the transcription factor GATA-1 by acetylation. Nature, 396, 594-598.
    • (1998) Nature , vol.396 , pp. 594-598
    • Boyes, J.1    Byfield, P.2    Nakatani, Y.3    Ogryzko, V.4
  • 6
    • 0030903750 scopus 로고    scopus 로고
    • Regulation of E2F through ubiquitin-proteasome-dependent degradation: Stabilization by pRB tumor supressor protein
    • Campero, M.R. and Flemmgton, E.K. (1997) Regulation of E2F through ubiquitin-proteasome-dependent degradation: stabilization by pRB tumor supressor protein. Proc. Natl Acad. Sci. USA, 94, 221-2226.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 221-2226
    • Campero, M.R.1    Flemmgton, E.K.2
  • 7
    • 0026609875 scopus 로고
    • Independent binding of the retinoblastoma protein and p107 to the transcription factor E2F
    • Cao, L., Faha, B., Dembski, M., Tsai, L.H., Harlow, E. and Dyson, N. (1992) Independent binding of the retinoblastoma protein and p107 to the transcription factor E2F. Nature, 355, 176-179.
    • (1992) Nature , vol.355 , pp. 176-179
    • Cao, L.1    Faha, B.2    Dembski, M.3    Tsai, L.H.4    Harlow, E.5    Dyson, N.6
  • 9
    • 0029912789 scopus 로고    scopus 로고
    • Nuclear accumulation of the E2F heterodimer regulated by subunit composition and alternative splicing of a nuclear localization signal
    • de la Luna, S., Burden, M.J., Lee, C.-W. and La Thangue, N.B. (1996) Nuclear accumulation of the E2F heterodimer regulated by subunit composition and alternative splicing of a nuclear localization signal. J. Cell Sci., 109, 2443-2452.
    • (1996) J. Cell Sci. , vol.109 , pp. 2443-2452
    • De La Luna, S.1    Burden, M.J.2    Lee, C.-W.3    La Thangue, N.B.4
  • 10
    • 0027936686 scopus 로고
    • Differential regulation of E2F transactivation by cyclin cdk2 complexes
    • Dynlacht, B.D., Flores, O., Lees, J.A. and Harlow, E. (1994) Differential regulation of E2F transactivation by cyclin cdk2 complexes. Genes Dev., 8, 1772-1786.
    • (1994) Genes Dev. , vol.8 , pp. 1772-1786
    • Dynlacht, B.D.1    Flores, O.2    Lees, J.A.3    Harlow, E.4
  • 11
    • 0030990095 scopus 로고    scopus 로고
    • Specific regulation of E2F family members by cyclin-dependent kinases
    • Dynlacht, B.D., Moberg, K., Lees, J.A., Harlow, E. and Zhu, L. (1997) Specific regulation of E2F family members by cyclin-dependent kinases. Mol. Biol. Cell, 17, 3867-3875.
    • (1997) Mol. Biol. Cell , vol.17 , pp. 3867-3875
    • Dynlacht, B.D.1    Moberg, K.2    Lees, J.A.3    Harlow, E.4    Zhu, L.5
  • 12
    • 0032146274 scopus 로고    scopus 로고
    • The regulation of E2F by pRB-family proteins
    • Dyson, N. (1998) The regulation of E2F by pRB-family proteins. Genes Dev., 12, 2245-2262.
    • (1998) Genes Dev. , vol.12 , pp. 2245-2262
    • Dyson, N.1
  • 13
    • 0027250860 scopus 로고
    • E2F1-mediated transactivation is inhibited by complex formation with the retinoblastoma susceptibility gene product
    • Flemington, E.K., Speck, S.H. and Kaelin, W.G. (1993) E2F1-mediated transactivation is inhibited by complex formation with the retinoblastoma susceptibility gene product. Proc. Natl Acad Sci. USA, 90, 6914-6918.
    • (1993) Proc. Natl Acad Sci. USA , vol.90 , pp. 6914-6918
    • Flemington, E.K.1    Speck, S.H.2    Kaelin, W.G.3
  • 15
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. (1997) Histone acetylation in chromatin structure and transcription. Nature, 389, 349-352.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 16
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W. and Roeder, R.G. (1997) Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell, 90, 595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 17
    • 0027520469 scopus 로고
    • The retinoblastoma protein binds E2F residues required for activation in vivo and TBP binding in vitro
    • Hagemeier, C., Cook, A. and Kouzarides, T. (1993) The retinoblastoma protein binds E2F residues required for activation in vivo and TBP binding in vitro. Nucleic Acids Res., 21, 4998-5004.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4998-5004
    • Hagemeier, C.1    Cook, A.2    Kouzarides, T.3
  • 18
    • 0029921317 scopus 로고    scopus 로고
    • Genetic alterations of cyclins, cyclin-dependent kinases and cdk inhibitors in human cancer
    • Hall, M. and Peters, G. (1996) Genetic alterations of cyclins, cyclin-dependent kinases and cdk inhibitors in human cancer. Adv. Cancer Res., 68, 67-108.
    • (1996) Adv. Cancer Res. , vol.68 , pp. 67-108
    • Hall, M.1    Peters, G.2
  • 19
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane, D. (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 20
    • 0029797841 scopus 로고    scopus 로고
    • Degradation of E2F by the ubiquitin -proteasome pathway - Regulation by retinoblastoma family proteins and adenovirus transforming protein
    • Hateboer, G., Kerkhoven, R.M., Shvarts, A., Bernards, R. and Beijersbergen, R.L. (1996) Degradation of E2F by the ubiquitin -proteasome pathway - regulation by retinoblastoma family proteins and adenovirus transforming protein. Genes Dev., 10, 2960-2970.
    • (1996) Genes Dev. , vol.10 , pp. 2960-2970
    • Hateboer, G.1    Kerkhoven, R.M.2    Shvarts, A.3    Bernards, R.4    Beijersbergen, R.L.5
  • 21
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes, T.R., Thorne, A.W. and Crane-Robinson, C.A. (1988) A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J., 7, 1395-1402.
    • (1988) EMBO J. , vol.7 , pp. 1395-1402
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.A.3
  • 22
    • 0031886093 scopus 로고    scopus 로고
    • Regulation of cell proliferation by the E2F transcription factors
    • Helin, K. (1998) Regulation of cell proliferation by the E2F transcription factors. Curr. Opin. Genet. Dev., 8, 28-35.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 28-35
    • Helin, K.1
  • 23
    • 0026652346 scopus 로고
    • A cDNA encoding a pRb-binding protein with properties of the transcription factor E2F
    • Helin, K., Lees, J.A., Vidal, M., Dyson, N., Harlow, E. and Fattaey, A. (1992) A cDNA encoding a pRb-binding protein with properties of the transcription factor E2F. Cell, 70, 337-350.
    • (1992) Cell , vol.70 , pp. 337-350
    • Helin, K.1    Lees, J.A.2    Vidal, M.3    Dyson, N.4    Harlow, E.5    Fattaey, A.6
  • 24
    • 0029820095 scopus 로고    scopus 로고
    • The retinoblastoma gene-product protects E2F-1 from degradation by the ubiquitin - Proteasome pathway
    • Hofmann, F., Martelli, F., Livingston, D.M. and Wang, Z.Y. (1996) The retinoblastoma gene-product protects E2F-1 from degradation by the ubiquitin - proteasome pathway. Genes Dev., 10, 2949-2959.
    • (1996) Genes Dev. , vol.10 , pp. 2949-2959
    • Hofmann, F.1    Martelli, F.2    Livingston, D.M.3    Wang, Z.Y.4
  • 25
    • 0027938209 scopus 로고
    • Cyclins and cancer
    • Hunter, T. and Pines, J. (1994) Cyclins and cancer. Cell, 79, 573-582.
    • (1994) Cell , vol.79 , pp. 573-582
    • Hunter, T.1    Pines, J.2
  • 26
    • 0031239891 scopus 로고    scopus 로고
    • Acetylation of general transcription factors by histone acetyltransferases
    • Imhof, A., Yang, X.-J., Ogryzko, V.V., Nakatani, Y. Wolffe, A.P. and Ge, H. (1997) Acetylation of general transcription factors by histone acetyltransferases. Curr. Biol., 7, 689-692.
    • (1997) Curr. Biol. , vol.7 , pp. 689-692
    • Imhof, A.1    Yang, X.-J.2    Ogryzko, V.V.3    Nakatani, Y.4    Wolffe, A.P.5    Ge, H.6
  • 27
    • 0027491775 scopus 로고
    • Expression of transcription factor E2F1 induces quiescent cells to enter S phase
    • Johnson, D.G., Schwarz, J.K., Cress, W.D. and Nevins, J.R. (1993) Expression of transcription factor E2F1 induces quiescent cells to enter S phase. Nature, 365, 349-352.
    • (1993) Nature , vol.365 , pp. 349-352
    • Johnson, D.G.1    Schwarz, J.K.2    Cress, W.D.3    Nevins, J.R.4
  • 28
    • 0026766083 scopus 로고
    • Expression cloning of a cDNA encoding a retinoblastoma-binding protein with E2F-like properties
    • Kaelin, W.G. et al. (1992) Expression cloning of a cDNA encoding a retinoblastoma-binding protein with E2F-like properties. Cell, 70, 351-364.
    • (1992) Cell , vol.70 , pp. 351-364
    • Kaelin, W.G.1
  • 29
    • 0029559027 scopus 로고
    • Cyclin A-kinase regulation of E2F-1 DNA binding function underlies suppression of an S phase checkpoint
    • Krek, W., Xu, G. and Livingston, D.M. (1995) Cyclin A-kinase regulation of E2F-1 DNA binding function underlies suppression of an S phase checkpoint. Cell, 83, 1149-1158.
    • (1995) Cell , vol.83 , pp. 1149-1158
    • Krek, W.1    Xu, G.2    Livingston, D.M.3
  • 30
    • 0028267869 scopus 로고
    • DRTF1/E2F: An expanding family of heterodimeric transcription factors implicated in cell-cycle control
    • La Thangue, N.B. (1994) DRTF1/E2F: an expanding family of heterodimeric transcription factors implicated in cell-cycle control. Trends Biochem. Sci., 19, 108-114.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 108-114
    • La Thangue, N.B.1
  • 33
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • Luo, R.X., Postigo, A.A. and Dean, D.C. (1998) Rb interacts with histone deacetylase to repress transcription. Cell, 92, 463-473.
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 35
    • 0033020484 scopus 로고    scopus 로고
    • Regulation of endogenous E2F1 stability by the retinoblastoma family proteins
    • Martelli, F. and Livingston, D.M. (1999) Regulation of endogenous E2F1 stability by the retinoblastoma family proteins. Proc. Natl Acad. Sci. USA, 96, 2858-2863.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 2858-2863
    • Martelli, F.1    Livingston, D.M.2
  • 37
    • 0031935648 scopus 로고    scopus 로고
    • Control of pRB phosphorylation
    • Mittnacht, S. (1998) Control of pRB phosphorylation. Curr. Opin. Genet. Dev., 8, 21-27.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 21-27
    • Mittnacht, S.1
  • 38
    • 0032186185 scopus 로고    scopus 로고
    • Acetylation of HMG I(Y) by CBP turns off INFβ expression by disrupting the enhanceosome
    • Munshi, N., Merika, M., Yie, J., Senger, K., Chen, G. and Thanos, D. (1998) Acetylation of HMG I(Y) by CBP turns off INFβ expression by disrupting the enhanceosome. Mol. Cell, 2, 457-467.
    • (1998) Mol. Cell , vol.2 , pp. 457-467
    • Munshi, N.1    Merika, M.2    Yie, J.3    Senger, K.4    Chen, G.5    Thanos, D.6
  • 39
    • 0026526437 scopus 로고
    • E2F: A link between the Rb tumor suppresser protein and viral oncoproteins
    • Nevins, J.R. (1992) E2F: a link between the Rb tumor suppresser protein and viral oncoproteins. Science, 258, 424-129.
    • (1992) Science , vol.258 , pp. 424-1129
    • Nevins, J.R.1
  • 40
    • 0029615315 scopus 로고
    • Physical and functional interactions between p53 and cell cycle co-operating transcription factors, E2F1 and DP1
    • O'Connor, D.J., Lam, E.W.-F., Griffin, S., Zhong, S., Leighton, L.C., Burbidge, S.A. and Lu, X. (1995) Physical and functional interactions between p53 and cell cycle co-operating transcription factors, E2F1 and DP1. EMBO J., 14, 6184-6192.
    • (1995) EMBO J. , vol.14 , pp. 6184-6192
    • O'Connor, D.J.1    Lam, E.W.-F.2    Griffin, S.3    Zhong, S.4    Leighton, L.C.5    Burbidge, S.A.6    Lu, X.7
  • 41
    • 0029583648 scopus 로고
    • Regulation of the cyclin E gene by transcription factor E2F1
    • Ohtani, K., DeGregori, J. and Nevins, J.R. (1995) Regulation of the cyclin E gene by transcription factor E2F1. Proc. Natl Acad. Sci. USA, 92, 12146-12150.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 12146-12150
    • Ohtani, K.1    Degregori, J.2    Nevins, J.R.3
  • 42
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V.V., Schiltz, R.L., Russanova, V., Howard, B.H. and Nakatani, Y. (1996) The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell, 87, 953-959.
    • (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
  • 43
    • 0030690423 scopus 로고    scopus 로고
    • Modular organization of the E2F activation domain and its interaction with general transcription factors TBP and TFIIH
    • Pearson, A. and Greenblatt, J. (1997) Modular organization of the E2F activation domain and its interaction with general transcription factors TBP and TFIIH. Oncogene, 15, 2643-2658.
    • (1997) Oncogene , vol.15 , pp. 2643-2658
    • Pearson, A.1    Greenblatt, J.2
  • 45
    • 0030688065 scopus 로고    scopus 로고
    • Subunit composition determines E2F DNA-binding site specificity
    • Tao, Y., Kassatly, R.F., Cress, C.W. and Horowitz, J.M. (1997) Subunit composition determines E2F DNA-binding site specificity. Mol. Cell. Biol., 17, 6994-7007.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6994-7007
    • Tao, Y.1    Kassatly, R.F.2    Cress, C.W.3    Horowitz, J.M.4
  • 46
    • 0029670046 scopus 로고    scopus 로고
    • E2F1 and E1A 12S have a homologous activation domain regulated by RB and CBP
    • Trouche, D. and Kouzarides, T. (1996) E2F1 and E1A 12S have a homologous activation domain regulated by RB and CBP. Proc. Natl Acad. Sci. USA, 93, 1439-1442.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1439-1442
    • Trouche, D.1    Kouzarides, T.2
  • 47
    • 0029997146 scopus 로고    scopus 로고
    • The CBP co-activator stimulates E2F1/DP1 activity
    • Trouche, D., Cook, A. and Kouzarides, T. (1996) The CBP co-activator stimulates E2F1/DP1 activity. Nucleic Acids Res., 24, 4139-4145.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4139-4145
    • Trouche, D.1    Cook, A.2    Kouzarides, T.3
  • 48
    • 0033517132 scopus 로고    scopus 로고
    • Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase
    • Vandel, L. and Kouzarides, T. (1999) Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase. EMBO J., 18, 4280-4291.
    • (1999) EMBO J. , vol.18 , pp. 4280-4291
    • Vandel, L.1    Kouzarides, T.2
  • 49
    • 0029043782 scopus 로고
    • Mechanism of active transcription repression by the retinoblastoma protein
    • Weintraub, S.J., Chow, K., Luo, R.X., Zhang, S.H., He, S. and Dean, D.C. (1995) Mechanism of active transcription repression by the retinoblastoma protein. Nature, 375, 812-815.
    • (1995) Nature , vol.375 , pp. 812-815
    • Weintraub, S.J.1    Chow, K.2    Luo, R.X.3    Zhang, S.H.4    He, S.5    Dean, D.C.6
  • 51
    • 0028019279 scopus 로고
    • Cyclin A-cdk2 binds directly to E2F-1 and inhibits the DNA-binding activity of E2F-1/DP-1 by phosphorylation
    • Xu, M., Sheppard, K.A., Peng, C.Y. Yee, A.S. and Piwnica-Worms, H. (1994) Cyclin A-cdk2 binds directly to E2F-1 and inhibits the DNA-binding activity of E2F-1/DP-1 by phosphorylation. Mol. Cell. Biol., 14, 8420-8431.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8420-8431
    • Xu, M.1    Sheppard, K.A.2    Peng, C.Y.3    Yee, A.S.4    Piwnica-Worms, H.5
  • 52
  • 53
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associatcd factor that competes with the adenoviral oncoprotein E1a
    • Yang, X.J., Ogryzko, V., Nishikawa, J., Howard, B. and Nakatani, Y. (1996) A p300/CBP-associatcd factor that competes with the adenoviral oncoprotein E1a. Nature, 382, 319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.2    Nishikawa, J.3    Howard, B.4    Nakatani, Y.5
  • 54
    • 0026645529 scopus 로고
    • Adenovirus E1a prevents the retinoblastoma gene product from repressing the activity of a cellular transcription factor
    • Zamanian, M. and La Thangue, N.B. (1992) Adenovirus E1a prevents the retinoblastoma gene product from repressing the activity of a cellular transcription factor. EMBO J., 11, 2603-2610.
    • (1992) EMBO J. , vol.11 , pp. 2603-2610
    • Zamanian, M.1    La Thangue, N.B.2
  • 55
    • 0033515424 scopus 로고    scopus 로고
    • 1 arrest triggered by p16INK4a. TGFβ and contact inhibition
    • 1 arrest triggered by p16INK4a. TGFβ and contact inhibition. Cell, 97, 53-61.
    • (1999) Cell , vol.97 , pp. 53-61
    • Zhang, H.S.1    Postigo, A.A.2    Dean, D.C.3
  • 56
    • 0032544123 scopus 로고    scopus 로고
    • Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases
    • Zhang, W. and Bieker, J.J. (1998) Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases. Proc. Natl Acad. Sci. USA, 95, 9855-9860.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9855-9860
    • Zhang, W.1    Bieker, J.J.2
  • 57
    • 0033559030 scopus 로고    scopus 로고
    • Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP
    • Zheng, N., Fraenkel, E., Pabo, C.O. and Pavletich, N.P. (1999) Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP. Genes Dev., 13, 666-674.
    • (1999) Genes Dev. , vol.13 , pp. 666-674
    • Zheng, N.1    Fraenkel, E.2    Pabo, C.O.3    Pavletich, N.P.4


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