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Volumn 289, Issue 13, 2014, Pages 9304-9319

Affinity map of bromodomain protein 4 (BRD4) interactions with the histone H4 tail and the small molecule inhibitor JQ1

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL PROLIFERATION;

EID: 84897448118     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.523019     Document Type: Article
Times cited : (122)

References (67)
  • 1
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger, S. L. (2007) The complex language of chromatin regulation during transcription. Nature 447, 407-412
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 2
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister, A. J., and Kouzarides, T. (2011) Regulation of chromatin by histone modifications. Cell Res. 21, 381-395
    • (2011) Cell Res. , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 3
    • 0037138363 scopus 로고    scopus 로고
    • Bromodomain. An acetyl-lysine binding domain
    • Zeng, L., and Zhou, M. M. (2002) Bromodomain. An acetyl-lysine binding domain. FEBS Lett. 513, 124-128
    • (2002) FEBS Lett. , vol.513 , pp. 124-128
    • Zeng, L.1    Zhou, M.M.2
  • 5
    • 0035434378 scopus 로고    scopus 로고
    • You bet-cha. A novel family of transcriptional regulators
    • Florence, B., and Faller, D. V. (2001) You bet-cha. A novel family of transcriptional regulators. Front Biosci. 6, D1008-D1018
    • (2001) Front Biosci. , vol.6
    • Florence, B.1    Faller, D.V.2
  • 6
    • 84866338076 scopus 로고    scopus 로고
    • Druggability analysis and structural classification of bromodomain acetyl-lysine binding sites
    • Vidler, L. R., Brown, N., Knapp, S., and Hoelder, S. (2012) Druggability analysis and structural classification of bromodomain acetyl-lysine binding sites. J. Med. Chem. 55, 7346-7359
    • (2012) J. Med. Chem. , vol.55 , pp. 7346-7359
    • Vidler, L.R.1    Brown, N.2    Knapp, S.3    Hoelder, S.4
  • 7
    • 84859479811 scopus 로고    scopus 로고
    • The bromodomain protein Brd4 associated with acetylated chromatin is important for maintenance of higher-order chromatin structure
    • Wang, R., Li, Q., Helfer, C. M., Jiao, J., and You, J. (2012) The bromodomain protein Brd4 associated with acetylated chromatin is important for maintenance of higher-order chromatin structure. J. Biol. Chem. 287, 10738-10752
    • (2012) J. Biol. Chem. , vol.287 , pp. 10738-10752
    • Wang, R.1    Li, Q.2    Helfer, C.M.3    Jiao, J.4    You, J.5
  • 8
    • 23744514308 scopus 로고    scopus 로고
    • The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription
    • DOI 10.1016/j.molcel.2005.06.027, PII S1097276505014322
    • Jang, M. K., Mochizuki, K., Zhou, M., Jeong, H. S., Brady, J. N., and Ozato, K. (2005) The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription. Mol. Cell 19, 523-534 (Pubitemid 41140009)
    • (2005) Molecular Cell , vol.19 , Issue.4 , pp. 523-534
    • Moon, K.J.1    Mochizuki, K.2    Zhou, M.3    Jeong, H.-S.4    Brady, J.N.5    Ozato, K.6
  • 9
    • 84862911038 scopus 로고    scopus 로고
    • Two-pronged binding with bromodomain-containing protein 4 liberates positive transcription elongation factor b from inactive ribonucleoprotein complexes
    • Schröder, S., Cho, S., Zeng, L., Zhang, Q., Kaehlcke, K., Mak, L., Lau, J., Bisgrove, D., Schnölzer, M., Verdin, E., Zhou, M. M., and Ott, M. (2012) Two-pronged binding with bromodomain-containing protein 4 liberates positive transcription elongation factor b from inactive ribonucleoprotein complexes. J. Biol. Chem. 287, 1090-1099
    • (2012) J. Biol. Chem. , vol.287 , pp. 1090-1099
    • Schröder, S.1    Cho, S.2    Zeng, L.3    Zhang, Q.4    Kaehlcke, K.5    Mak, L.6    Lau, J.7    Bisgrove, D.8    Schnölzer, M.9    Verdin, E.10    Zhou, M.M.11    Ott, M.12
  • 10
    • 38549113034 scopus 로고    scopus 로고
    • 1 gene expression and cell cycle progression
    • DOI 10.1128/MCB.01020-07
    • Yang, Z., He, N., and Zhou, Q. (2008) Brd4 recruits P-TEFb to chromosomes at late mitosis to promote G1 gene expression and cell cycle progression. Mol. Cell. Biol. 28, 967-976 (Pubitemid 351160053)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.3 , pp. 967-976
    • Yang, Z.1    He, N.2    Zhou, Q.3
  • 11
    • 77956392623 scopus 로고    scopus 로고
    • Brd4 engagement from chromatin targeting to transcriptional regulation. Selective contact with acetylated histone H3 and H4
    • Chiang, C. M. (2009) Brd4 engagement from chromatin targeting to transcriptional regulation. Selective contact with acetylated histone H3 and H4. F1000 Biol. Rep. 1, 98
    • (2009) F1000 Biol. Rep. , vol.1 , pp. 98
    • Chiang, C.M.1
  • 14
    • 84899927814 scopus 로고    scopus 로고
    • Brd4 maintains constitutively active NF-κB in cancer cells by binding to acetylated RelA
    • 10.1038/onc.2013.179
    • Zou, Z., Huang, B., Wu, X., Zhang, H., Qi, J., Bradner, J., Nair, S., and Chen, L. F. (2013) Brd4 maintains constitutively active NF-κB in cancer cells by binding to acetylated RelA. Oncogene 10.1038/onc.2013.179
    • (2013) Oncogene
    • Zou, Z.1    Huang, B.2    Wu, X.3    Zhang, H.4    Qi, J.5    Bradner, J.6    Nair, S.7    Chen, L.F.8
  • 15
    • 79959483607 scopus 로고    scopus 로고
    • The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3
    • Rahman, S., Sowa, M. E., Ottinger, M., Smith, J. A., Shi, Y., Harper, J. W., and Howley, P. M. (2011) The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3. Mol. Cell. Biol. 31, 2641-2652
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2641-2652
    • Rahman, S.1    Sowa, M.E.2    Ottinger, M.3    Smith, J.A.4    Shi, Y.5    Harper, J.W.6    Howley, P.M.7
  • 16
    • 79959238999 scopus 로고    scopus 로고
    • Disrupting the reader of histone language
    • Oliver, S. S., and Denu, J. M. (2011) Disrupting the reader of histone language. Angew Chem. Int. Ed. Engl. 50, 5801-5803
    • (2011) Angew Chem. Int. Ed. Engl. , vol.50 , pp. 5801-5803
    • Oliver, S.S.1    Denu, J.M.2
  • 23
    • 84876855540 scopus 로고    scopus 로고
    • Phospho switch triggers Brd4 chromatin binding and activator recruitment for gene-specific targeting
    • Wu, S. Y., Lee, A. Y., Lai, H. T., Zhang, H., and Chiang, C. M. (2013) Phospho switch triggers Brd4 chromatin binding and activator recruitment for gene-specific targeting. Mol. Cell 49, 843-857
    • (2013) Mol. Cell , vol.49 , pp. 843-857
    • Wu, S.Y.1    Lee, A.Y.2    Lai, H.T.3    Zhang, H.4    Chiang, C.M.5
  • 26
    • 84874973263 scopus 로고    scopus 로고
    • The importance of diagnosing NUT midline carcinoma
    • French, C. A. (2013) The importance of diagnosing NUT midline carcinoma. Head Neck Pathol. 7, 11-16
    • (2013) Head Neck Pathol. , vol.7 , pp. 11-16
    • French, C.A.1
  • 32
    • 84869753078 scopus 로고    scopus 로고
    • Sensitivity of human lung adenocarcinoma cell lines to targeted inhibition of BET epigenetic signaling proteins
    • Lockwood, W. W., Zejnullahu, K., Bradner, J. E., and Varmus, H. (2012) Sensitivity of human lung adenocarcinoma cell lines to targeted inhibition of BET epigenetic signaling proteins. Proc. Natl. Acad. Sci. U.S.A. 109, 19408-19413
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 19408-19413
    • Lockwood, W.W.1    Zejnullahu, K.2    Bradner, J.E.3    Varmus, H.4
  • 36
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • DOI 10.1038/20974
    • Dhalluin, C., Carlson, J. E., Zeng, L., He, C., Aggarwal, A. K., and Zhou, M. M. (1999) Structure and ligand of a histone acetyltransferase bromodomain. Nature 399, 491-496 (Pubitemid 29258857)
    • (1999) Nature , vol.399 , Issue.6735 , pp. 491-496
    • Dhalluin, C.1    Carlson, J.E.2    Zeng, L.3    He, C.4    Aggarwal, A.K.5    Zhou, M.-M.6
  • 37
    • 0034669210 scopus 로고    scopus 로고
    • The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p
    • Owen, D. J., Ornaghi, P., Yang, J. C., Lowe, N., Evans, P. R., Ballario, P., Neuhaus, D., Filetici, P., and Travers, A. A. (2000) The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p. EMBO J. 19, 6141-6149
    • (2000) EMBO J. , vol.19 , pp. 6141-6149
    • Owen, D.J.1    Ornaghi, P.2    Yang, J.C.3    Lowe, N.4    Evans, P.R.5    Ballario, P.6    Neuhaus, D.7    Filetici, P.8    Travers, A.A.9
  • 39
    • 73649124584 scopus 로고    scopus 로고
    • Structures of the dual bromodomains of the P-TEFb-activating protein Brd4 at atomic resolution
    • Vollmuth, F., Blankenfeldt, W., and Geyer, M. (2009) Structures of the dual bromodomains of the P-TEFb-activating protein Brd4 at atomic resolution. J. Biol. Chem. 284, 36547-36556
    • (2009) J. Biol. Chem. , vol.284 , pp. 36547-36556
    • Vollmuth, F.1    Blankenfeldt, W.2    Geyer, M.3
  • 42
    • 1642564551 scopus 로고    scopus 로고
    • Selective Recognition of Acetylated Histones by Bromodomain Proteins Visualized in Living Cells
    • DOI 10.1016/S1097-2765(03)00482-9
    • Kanno, T., Kanno, Y., Siegel, R. M., Jang, M. K., Lenardo, M. J., and Ozato, K. (2004) Selective recognition of acetylated histones by bromodomain proteins visualized in living cells. Mol. Cell 13, 33-43 (Pubitemid 38117113)
    • (2004) Molecular Cell , vol.13 , Issue.1 , pp. 33-43
    • Kanno, T.1    Kanno, Y.2    Siegel, R.M.3    Jang, M.K.4    Lenardo, M.J.5    Ozato, K.6
  • 44
    • 0042090936 scopus 로고    scopus 로고
    • Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein
    • DOI 10.1128/MCB.23.15.5354-5365.2003
    • Pivot-Pajot, C., Caron, C., Govin, J., Vion, A., Rousseaux, S., and Khochbin, S. (2003) Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein. Mol. Cell. Biol. 23, 5354-5365 (Pubitemid 36950890)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.15 , pp. 5354-5365
    • Pivot-Pajot, C.1    Caron, C.2    Govin, J.3    Vion, A.4    Rousseaux, S.5    Khochbin, S.6
  • 45
    • 79959402979 scopus 로고    scopus 로고
    • Structural basis and specificity of acetylated transcription factor GATA1 recognition by BET family bromodomain protein Brd3
    • Gamsjaeger, R., Webb, S. R., Lamonica, J. M., Billin, A., Blobel, G. A., and Mackay, J. P. (2011) Structural basis and specificity of acetylated transcription factor GATA1 recognition by BET family bromodomain protein Brd3. Mol. Cell. Biol. 31, 2632-2640
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2632-2640
    • Gamsjaeger, R.1    Webb, S.R.2    Lamonica, J.M.3    Billin, A.4    Blobel, G.A.5    Mackay, J.P.6
  • 46
    • 77950678272 scopus 로고    scopus 로고
    • Molecular mechanisms of acquired resistance to tyrosine kinase targeted therapy
    • Sierra, J. R., Cepero, V., and Giordano, S. (2010) Molecular mechanisms of acquired resistance to tyrosine kinase targeted therapy. Mol. Cancer 9, 75
    • (2010) Mol. Cancer , vol.9 , pp. 75
    • Sierra, J.R.1    Cepero, V.2    Giordano, S.3
  • 47
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang, J., Yang, P. L., and Gray, N. S. (2009) Targeting cancer with small molecule kinase inhibitors. Nat. Rev. Cancer 9, 28-39
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 49
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Durocher, Y., Perret, S., and Kamen, A. (2002) High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res. 30, E9
    • (2002) Nucleic Acids Res. , vol.30
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 50
    • 0000715366 scopus 로고
    • Site-directed mutagenesis by double polymerase chain reaction. Megaprimer method
    • Barik, S. (1993) Site-directed mutagenesis by double polymerase chain reaction. Megaprimer method. Methods Mol. Biol. 15, 277-286
    • (1993) Methods Mol. Biol. , vol.15 , pp. 277-286
    • Barik, S.1
  • 51
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • DOI 10.1021/bi00481a024
    • Brandts, J. F., and Lin, L. N. (1990) Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry 29, 6927-6940 (Pubitemid 20225495)
    • (1990) Biochemistry , vol.29 , Issue.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.-N.2
  • 52
    • 0028820703 scopus 로고
    • Denaturantmvalues and heat capacity changes. Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Denaturantmvalues and heat capacity changes. Relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 53
    • 78650485354 scopus 로고    scopus 로고
    • Thermodynamic analysis of ligand-induced changes in protein thermal unfolding applied to high-throughput determination of ligand affinities with extrinsic fluorescent dyes
    • Layton, C. J., and Hellinga, H. W. (2010) Thermodynamic analysis of ligand-induced changes in protein thermal unfolding applied to high-throughput determination of ligand affinities with extrinsic fluorescent dyes. Biochemistry 49, 10831-10841
    • (2010) Biochemistry , vol.49 , pp. 10831-10841
    • Layton, C.J.1    Hellinga, H.W.2
  • 56
    • 1642377367 scopus 로고    scopus 로고
    • Measurement of Dynamic Protein Binding to Chromatin In Vivo, Using Photobleaching Microscopy
    • DOI 10.1016/S0076-6879(03)75025-3
    • Phair, R. D., Gorski, S. A., and Misteli, T. (2004) Measurement of dynamic protein binding to chromatin in vivo, using photobleaching microscopy. Methods Enzymol. 375, 393-414 (Pubitemid 38124881)
    • (2004) Methods in Enzymology , vol.375 , pp. 393-414
    • Phair, R.D.1    Gorski, S.A.2    Misteli, T.3
  • 57
    • 61749088806 scopus 로고    scopus 로고
    • Brd4 coactivates transcriptional activation of NF-κB via specific binding to acetylated RelA
    • Huang, B., Yang, X. D., Zhou, M. M., Ozato, K., and Chen, L. F. (2009) Brd4 coactivates transcriptional activation of NF-κB via specific binding to acetylated RelA. Mol. Cell. Biol. 29, 1375-1387
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1375-1387
    • Huang, B.1    Yang, X.D.2    Zhou, M.M.3    Ozato, K.4    Chen, L.F.5
  • 58
    • 83455202613 scopus 로고    scopus 로고
    • Progress in the discovery of small-molecule inhibitors of bromodomain-histone interactions
    • Chung, C. W., and Witherington, J. (2011) Progress in the discovery of small-molecule inhibitors of bromodomain-histone interactions. J. Biomol. Screen 16, 1170-1185
    • (2011) J. Biomol. Screen , vol.16 , pp. 1170-1185
    • Chung, C.W.1    Witherington, J.2
  • 59
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using thermofluor
    • DOI 10.1021/bi048135v
    • Matulis, D., Kranz, J. K., Salemme, F. R., and Todd, M. J. (2005) Thermodynamic stability of carbonic anhydrase. Measurements of binding affinity and stoichiometry using ThermoFluor. Biochemistry 44, 5258-5266 (Pubitemid 40471238)
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 61
    • 84886099830 scopus 로고    scopus 로고
    • Mutations in regulators of the epigenome and their connections to global chromatin patterns in cancer
    • Plass, C., Pfister, S. M., Lindroth, A. M., Bogatyrova, O., Claus, R., and Lichter, P. (2013) Mutations in regulators of the epigenome and their connections to global chromatin patterns in cancer. Nat. Rev. Genet. 14, 765-780
    • (2013) Nat. Rev. Genet. , vol.14 , pp. 765-780
    • Plass, C.1    Pfister, S.M.2    Lindroth, A.M.3    Bogatyrova, O.4    Claus, R.5    Lichter, P.6
  • 63
    • 84870013141 scopus 로고    scopus 로고
    • Progress in the development and application of small molecule inhibitors of bromodomain-acetyl-lysine interactions
    • Hewings, D. S., Rooney, T. P., Jennings, L. E., Hay, D. A., Schofield, C. J., Brennan, P. E., Knapp, S., and Conway, S. J. (2012) Progress in the development and application of small molecule inhibitors of bromodomain-acetyl- lysine interactions. J. Med. Chem. 55, 9393-9413
    • (2012) J. Med. Chem. , vol.55 , pp. 9393-9413
    • Hewings, D.S.1    Rooney, T.P.2    Jennings, L.E.3    Hay, D.A.4    Schofield, C.J.5    Brennan, P.E.6    Knapp, S.7    Conway, S.J.8
  • 65
    • 84879692312 scopus 로고    scopus 로고
    • Does bromodomain flexibility influence histone recognition?
    • Steiner, S., Magno, A., Huang, D., and Caflisch, A. (2013) Does bromodomain flexibility influence histone recognition? FEBS Lett. 587, 2158-2163
    • (2013) FEBS Lett. , vol.587 , pp. 2158-2163
    • Steiner, S.1    Magno, A.2    Huang, D.3    Caflisch, A.4
  • 66
    • 34248512282 scopus 로고    scopus 로고
    • Solution structure of BRD7 bromodomain and its interaction with acetylated peptides from histone H3 and H4
    • DOI 10.1016/j.bbrc.2007.04.139, PII S0006291X07008625
    • Sun, H., Liu, J., Zhang, J., Shen, W., Huang, H., Xu, C., Dai, H., Wu, J., and Shi, Y. (2007) Solution structure of BRD7 bromodomain and its interaction with acetylated peptides from histone H3 and H4. Biochem. Biophys. Res. Commun. 358, 435-441 (Pubitemid 46755725)
    • (2007) Biochemical and Biophysical Research Communications , vol.358 , Issue.2 , pp. 435-441
    • Sun, H.1    Liu, J.2    Zhang, J.3    Shen, W.4    Huang, H.5    Xu, C.6    Dai, H.7    Wu, J.8    Shi, Y.9
  • 67
    • 84862817809 scopus 로고    scopus 로고
    • Place your BETs. The therapeutic potential of bromodomains
    • Prinjha, R. K., Witherington, J., and Lee, K. (2012) Place your BETs. The therapeutic potential of bromodomains. Trends Pharmacol. Sci. 33, 146-153
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 146-153
    • Prinjha, R.K.1    Witherington, J.2    Lee, K.3


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