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Volumn 8, Issue 6, 2013, Pages 1311-1323

Probing p300/CBP associated factor (PCAF)-dependent pathways with a small molecule inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; CASPASE RECRUITMENT DOMAIN PROTEIN 4; EMBELIN; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; PROBING P300 CBP ASSOCIATED FACTOR; UNCLASSIFIED DRUG;

EID: 84879756597     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb4000597     Document Type: Article
Times cited : (61)

References (61)
  • 5
    • 78149480527 scopus 로고    scopus 로고
    • Regulating a master regulator: Establishing tissue-specific gene expression in skeletal muscle
    • Aziz, A., Liu, Q. C., and Dilworth, F. J. (2010) Regulating a master regulator: establishing tissue-specific gene expression in skeletal muscle Epigenetics 5, 691-695
    • (2010) Epigenetics , vol.5 , pp. 691-695
    • Aziz, A.1    Liu, Q.C.2    Dilworth, F.J.3
  • 6
    • 33744534726 scopus 로고    scopus 로고
    • GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1alpha
    • Lerin, C., Rodgers, J. T., Kalume, D. E., Kim, S. H., Pandey, A., and Puigserver, P. (2006) GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1alpha Cell Metab. 3, 429-438
    • (2006) Cell Metab. , vol.3 , pp. 429-438
    • Lerin, C.1    Rodgers, J.T.2    Kalume, D.E.3    Kim, S.H.4    Pandey, A.5    Puigserver, P.6
  • 7
    • 84863794131 scopus 로고    scopus 로고
    • The histone acetyltransferase PCAF regulates p21 transcription through stress-induced acetylation of histone H3
    • Love, I. M., Sekaric, P., Shi, D., Grossman, S. R., and Androphy, E. J. (2012) The histone acetyltransferase PCAF regulates p21 transcription through stress-induced acetylation of histone H3 Cell Cycle 11, 2458-2466
    • (2012) Cell Cycle , vol.11 , pp. 2458-2466
    • Love, I.M.1    Sekaric, P.2    Shi, D.3    Grossman, S.R.4    Androphy, E.J.5
  • 8
    • 64549139803 scopus 로고    scopus 로고
    • Reversible acetylation of chromatin: Implication in regulation of gene expression, disease and therapeutics
    • Selvi, R. B. and Kundu, T. K. (2009) Reversible acetylation of chromatin: implication in regulation of gene expression, disease and therapeutics Biotechnol. J. 4, 375-390
    • (2009) Biotechnol. J. , vol.4 , pp. 375-390
    • Selvi, R.B.1    Kundu, T.K.2
  • 9
    • 77956047888 scopus 로고    scopus 로고
    • Nitric oxide-mediated histone hyperacetylation in oral cancer: Target for a water-soluble HAT inhibitor, CTK7A
    • Arif, M., Vedamurthy, B. M., Choudhari, R., Ostwal, Y. B., Mantelingu, K., Kodaganur, G. S., and Kundu, T. K. (2010) Nitric oxide-mediated histone hyperacetylation in oral cancer: target for a water-soluble HAT inhibitor, CTK7A Chem. Biol. 17, 903-913
    • (2010) Chem. Biol. , vol.17 , pp. 903-913
    • Arif, M.1    Vedamurthy, B.M.2    Choudhari, R.3    Ostwal, Y.B.4    Mantelingu, K.5    Kodaganur, G.S.6    Kundu, T.K.7
  • 11
    • 51949111451 scopus 로고    scopus 로고
    • Chemical probes for histone-modifying enzymes
    • Cole, P. A. (2008) Chemical probes for histone-modifying enzymes Nat. Chem. Biol. 4, 590-597
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 590-597
    • Cole, P.A.1
  • 15
    • 2342448582 scopus 로고    scopus 로고
    • Discovery of embelin as a cell-permeable, small-molecular weight inhibitor of XIAP through structure-based computational screening of a traditional herbal medicine three-dimensional structure database
    • Nikolovska-Coleska, Z., Xu, L., Hu, Z., Tomita, Y., Li, P., Roller, P. P., Wang, R., Fang, X., Guo, R., Zhang, M., Lippman, M. E., Yang, D., and Wang, S. (2004) Discovery of embelin as a cell-permeable, small-molecular weight inhibitor of XIAP through structure-based computational screening of a traditional herbal medicine three-dimensional structure database J. Med. Chem. 47, 2430-2440
    • (2004) J. Med. Chem. , vol.47 , pp. 2430-2440
    • Nikolovska-Coleska, Z.1    Xu, L.2    Hu, Z.3    Tomita, Y.4    Li, P.5    Roller, P.P.6    Wang, R.7    Fang, X.8    Guo, R.9    Zhang, M.10    Lippman, M.E.11    Yang, D.12    Wang, S.13
  • 16
    • 78649673612 scopus 로고    scopus 로고
    • Embelin suppresses osteoclastogenesis induced by receptor activator of NF-kappaB ligand and tumor cells in vitro through inhibition of the NF-kappaB cell signaling pathway
    • Reuter, S., Prasad, S., Phromnoi, K., Kannappan, R., Yadav, V. R., and Aggarwal, B. B. (2010) Embelin suppresses osteoclastogenesis induced by receptor activator of NF-kappaB ligand and tumor cells in vitro through inhibition of the NF-kappaB cell signaling pathway Mol. Cancer Res. 8, 1425-1436
    • (2010) Mol. Cancer Res. , vol.8 , pp. 1425-1436
    • Reuter, S.1    Prasad, S.2    Phromnoi, K.3    Kannappan, R.4    Yadav, V.R.5    Aggarwal, B.B.6
  • 17
    • 33845883544 scopus 로고    scopus 로고
    • Embelin, an inhibitor of X chromosome-linked inhibitor-of-apoptosis protein, blocks nuclear factor-kappaB (NF-kappaB) signaling pathway leading to suppression of NF-kappaB-regulated antiapoptotic and metastatic gene products
    • Ahn, K. S., Sethi, G., and Aggarwal, B. B. (2007) Embelin, an inhibitor of X chromosome-linked inhibitor-of-apoptosis protein, blocks nuclear factor-kappaB (NF-kappaB) signaling pathway leading to suppression of NF-kappaB-regulated antiapoptotic and metastatic gene products Mol. Pharmacol. 71, 209-219
    • (2007) Mol. Pharmacol. , vol.71 , pp. 209-219
    • Ahn, K.S.1    Sethi, G.2    Aggarwal, B.B.3
  • 18
    • 0033758416 scopus 로고    scopus 로고
    • Inhibitory effects of sudanese medicinal plant extracts on hepatitis C virus (HCV) protease
    • Hussein, G., Miyashiro, H., Nakamura, N., Hattori, M., Kakiuchi, N., and Shimotohno, K. (2000) Inhibitory effects of sudanese medicinal plant extracts on hepatitis C virus (HCV) protease Phytother. Res. 14, 510-516
    • (2000) Phytother. Res. , vol.14 , pp. 510-516
    • Hussein, G.1    Miyashiro, H.2    Nakamura, N.3    Hattori, M.4    Kakiuchi, N.5    Shimotohno, K.6
  • 19
    • 0038361015 scopus 로고    scopus 로고
    • Antibacterial activity of embelin
    • Chitra, M., Devi, C. S., and Sukumar, E. (2003) Antibacterial activity of embelin Fitoterapia 74, 401-403
    • (2003) Fitoterapia , vol.74 , pp. 401-403
    • Chitra, M.1    Devi, C.S.2    Sukumar, E.3
  • 20
    • 0030071497 scopus 로고    scopus 로고
    • Anthelmintic usage of extracts of Embelia schimperi from Tanzania
    • Bogh, H. O., Andreassen, J., and Lemmich, J. (1996) Anthelmintic usage of extracts of Embelia schimperi from Tanzania J. Ethnopharmacol. 50, 35-42
    • (1996) J. Ethnopharmacol. , vol.50 , pp. 35-42
    • Bogh, H.O.1    Andreassen, J.2    Lemmich, J.3
  • 21
    • 0019292869 scopus 로고
    • Antifertility properties of Embelia ribes: (Embelin)
    • Krishnaswamy, M. and Purushothaman, K. K. (1980) Antifertility properties of Embelia ribes: (embelin) Indian J. Exp. Biol. 18, 1359-1360
    • (1980) Indian J. Exp. Biol. , vol.18 , pp. 1359-1360
    • Krishnaswamy, M.1    Purushothaman, K.K.2
  • 22
    • 0017326573 scopus 로고
    • Some pharmacological investigations of embelin and its semisynthetic derivatives
    • Gupta, O. P., Ali, M. M., Ray Ghatak, B. J., and Atal, C. K. (1977) Some pharmacological investigations of embelin and its semisynthetic derivatives Indian J. Physiol. Pharmacol. 21, 31-39
    • (1977) Indian J. Physiol. Pharmacol. , vol.21 , pp. 31-39
    • Gupta, O.P.1    Ali, M.M.2    Ray Ghatak, B.J.3    Atal, C.K.4
  • 24
    • 84862156464 scopus 로고    scopus 로고
    • HIstome-a relational knowledgebase of human histone proteins and histone modifying enzymes
    • Khare, S. P., Habib, F., Sharma, R., Gadewal, N., Gupta, S., and Galande, S. (2011) HIstome-a relational knowledgebase of human histone proteins and histone modifying enzymes Nucleic Acids Res. 40, D337-342
    • (2011) Nucleic Acids Res. , vol.40 , pp. 337-342
    • Khare, S.P.1    Habib, F.2    Sharma, R.3    Gadewal, N.4    Gupta, S.5    Galande, S.6
  • 25
    • 78751611793 scopus 로고    scopus 로고
    • Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation
    • Jin, Q., Yu, L. R., Wang, L., Zhang, Z., Kasper, L. H., Lee, J. E., Wang, C., Brindle, P. K., Dent, S. Y., and Ge, K. (2011) Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation EMBO J. 30, 249-262
    • (2011) EMBO J. , vol.30 , pp. 249-262
    • Jin, Q.1    Yu, L.R.2    Wang, L.3    Zhang, Z.4    Kasper, L.H.5    Lee, J.E.6    Wang, C.7    Brindle, P.K.8    Dent, S.Y.9    Ge, K.10
  • 26
    • 39149109887 scopus 로고    scopus 로고
    • The structural basis of protein acetylation by the p300/CBP transcriptional coactivator
    • Liu, X., Wang, L., Zhao, K., Thompson, P. R., Hwang, Y., Marmorstein, R., and Cole, P. A. (2008) The structural basis of protein acetylation by the p300/CBP transcriptional coactivator Nature 451, 846-850
    • (2008) Nature , vol.451 , pp. 846-850
    • Liu, X.1    Wang, L.2    Zhao, K.3    Thompson, P.R.4    Hwang, Y.5    Marmorstein, R.6    Cole, P.A.7
  • 27
    • 77950382469 scopus 로고    scopus 로고
    • Hs.137007 is a novel epigenetic marker hypermethylated and up-regulated in breast cancer
    • Kim, T. W., Kim, Y. J., Lee, H. J., Min, S. Y., Kang, H. S., and Kim, S. J. (2010) Hs.137007 is a novel epigenetic marker hypermethylated and up-regulated in breast cancer Int. J. Oncol. 36, 1105-1111
    • (2010) Int. J. Oncol. , vol.36 , pp. 1105-1111
    • Kim, T.W.1    Kim, Y.J.2    Lee, H.J.3    Min, S.Y.4    Kang, H.S.5    Kim, S.J.6
  • 30
    • 4143085011 scopus 로고    scopus 로고
    • In vitro transcription system delineates the distinct roles of the coactivators pCAF and p300 during MyoD/E47-dependent transactivation
    • Dilworth, F. J., Seaver, K. J., Fishburn, A. L., Htet, S. L., and Tapscott, S. J. (2004) In vitro transcription system delineates the distinct roles of the coactivators pCAF and p300 during MyoD/E47-dependent transactivation Proc. Natl. Acad. Sci. U.S.A. 101, 11593-11598
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 11593-11598
    • Dilworth, F.J.1    Seaver, K.J.2    Fishburn, A.L.3    Htet, S.L.4    Tapscott, S.J.5
  • 31
    • 84856663944 scopus 로고    scopus 로고
    • Analysis of early C2C12 myogenesis identifies stably and differentially expressed transcriptional regulators whose knock-down inhibits myoblast differentiation
    • Rajan, S., Chu Pham Dang, H., Djambazian, H., Zuzan, H., Fedyshyn, Y., Ketela, T., Moffat, J., Hudson, T. J., and Sladek, R. (2012) Analysis of early C2C12 myogenesis identifies stably and differentially expressed transcriptional regulators whose knock-down inhibits myoblast differentiation Physiol. Genomics 44, 183-197
    • (2012) Physiol. Genomics , vol.44 , pp. 183-197
    • Rajan, S.1    Chu Pham Dang, H.2    Djambazian, H.3    Zuzan, H.4    Fedyshyn, Y.5    Ketela, T.6    Moffat, J.7    Hudson, T.J.8    Sladek, R.9
  • 32
    • 0034601778 scopus 로고    scopus 로고
    • Kinetic mechanism of human histone acetyltransferase P/CAF
    • Tanner, K. G., Langer, M. R., and Denu, J. M. (2000) Kinetic mechanism of human histone acetyltransferase P/CAF Biochemistry 39, 15652
    • (2000) Biochemistry , vol.39 , pp. 15652
    • Tanner, K.G.1    Langer, M.R.2    Denu, J.M.3
  • 33
    • 0034698085 scopus 로고    scopus 로고
    • Kinetic mechanism of the histone acetyltransferase GCN5 from yeast
    • Tanner, K. G., Langer, M. R., Kim, Y., and Denu, J. M. (2000) Kinetic mechanism of the histone acetyltransferase GCN5 from yeast J. Biol. Chem. 275, 22048-22055
    • (2000) J. Biol. Chem. , vol.275 , pp. 22048-22055
    • Tanner, K.G.1    Langer, M.R.2    Kim, Y.3    Denu, J.M.4
  • 34
    • 66149127693 scopus 로고    scopus 로고
    • The Gcn5 bromodomain of the SAGA complex facilitates cooperative and cross-tail acetylation of nucleosomes
    • Li, S. and Shogren-Knaak, M. (2009) The Gcn5 bromodomain of the SAGA complex facilitates cooperative and cross-tail acetylation of nucleosomes J. Biol. Chem. 284, 9411-9417
    • (2009) J. Biol. Chem. , vol.284 , pp. 9411-9417
    • Li, S.1    Shogren-Knaak, M.2
  • 35
    • 84879774966 scopus 로고    scopus 로고
    • Epigenetic regulation of skeletal muscle development and differentiation
    • Bharathy, N., Ling, B. M., and Taneja, R. (2012) Epigenetic regulation of skeletal muscle development and differentiation Subcell. Biochem. 61, 139-150
    • (2012) Subcell. Biochem. , vol.61 , pp. 139-150
    • Bharathy, N.1    Ling, B.M.2    Taneja, R.3
  • 39
    • 55549108731 scopus 로고    scopus 로고
    • Differential survival response of neurons to exogenous GDNF depends on the presence of skeletal muscle
    • Angka, H. E., Geddes, A. J., and Kablar, B. (2008) Differential survival response of neurons to exogenous GDNF depends on the presence of skeletal muscle Dev. Dyn. 237, 3169-3178
    • (2008) Dev. Dyn. , vol.237 , pp. 3169-3178
    • Angka, H.E.1    Geddes, A.J.2    Kablar, B.3
  • 40
    • 33845697226 scopus 로고    scopus 로고
    • Muscle cachexia is regulated by a p53-PW1/Peg3-dependent pathway
    • Schwarzkopf, M., Coletti, D., Sassoon, D., and Marazzi, G. (2006) Muscle cachexia is regulated by a p53-PW1/Peg3-dependent pathway Genes Dev. 20, 3440-3452
    • (2006) Genes Dev. , vol.20 , pp. 3440-3452
    • Schwarzkopf, M.1    Coletti, D.2    Sassoon, D.3    Marazzi, G.4
  • 41
    • 51349084951 scopus 로고    scopus 로고
    • The role of cell death in sexually dimorphic muscle development: Male-specific muscles are retained in female bax/bak knockout mice
    • Jacob, D. A., Ray, T., Bengston, C. L., Lindsten, T., Wu, J., Thompson, C. B., and Forger, N. G. (2008) The role of cell death in sexually dimorphic muscle development: male-specific muscles are retained in female bax/bak knockout mice Dev. Neurobiol. 68, 1303-1314
    • (2008) Dev. Neurobiol. , vol.68 , pp. 1303-1314
    • Jacob, D.A.1    Ray, T.2    Bengston, C.L.3    Lindsten, T.4    Wu, J.5    Thompson, C.B.6    Forger, N.G.7
  • 42
    • 79958033203 scopus 로고    scopus 로고
    • Acetylation of a conserved lysine residue in the ATP binding pocket of p38 augments its kinase activity during hypertrophy of cardiomyocytes
    • Pillai, V. B., Sundaresan, N. R., Samant, S. A., Wolfgeher, D., Trivedi, C. M., and Gupta, M. P. (2011) Acetylation of a conserved lysine residue in the ATP binding pocket of p38 augments its kinase activity during hypertrophy of cardiomyocytes Mol. Cell. Biol. 31, 2349-2363
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2349-2363
    • Pillai, V.B.1    Sundaresan, N.R.2    Samant, S.A.3    Wolfgeher, D.4    Trivedi, C.M.5    Gupta, M.P.6
  • 43
    • 62749122902 scopus 로고    scopus 로고
    • STAT3 induces muscle stem cell differentiation by interaction with myoD
    • Yang, Y., Xu, Y., Li, W., Wang, G., Song, Y., Yang, G., Han, X., Du, Z., Sun, L., and Ma, K. (2009) STAT3 induces muscle stem cell differentiation by interaction with myoD Cytokine 46, 137-141
    • (2009) Cytokine , vol.46 , pp. 137-141
    • Yang, Y.1    Xu, Y.2    Li, W.3    Wang, G.4    Song, Y.5    Yang, G.6    Han, X.7    Du, Z.8    Sun, L.9    Ma, K.10
  • 45
    • 57749109116 scopus 로고    scopus 로고
    • JAK2/STAT2/STAT3 are required for myogenic differentiation
    • Wang, K., Wang, C., Xiao, F., Wang, H., and Wu, Z. (2008) JAK2/STAT2/STAT3 are required for myogenic differentiation J. Biol. Chem. 283, 34029-34036
    • (2008) J. Biol. Chem. , vol.283 , pp. 34029-34036
    • Wang, K.1    Wang, C.2    Xiao, F.3    Wang, H.4    Wu, Z.5
  • 46
    • 70249146174 scopus 로고    scopus 로고
    • SOCS1, SOCS3, and PIAS1 promote myogenic differentiation by inhibiting the leukemia inhibitory factor-induced JAK1/STAT1/STAT3 pathway
    • Diao, Y., Wang, X., and Wu, Z. (2009) SOCS1, SOCS3, and PIAS1 promote myogenic differentiation by inhibiting the leukemia inhibitory factor-induced JAK1/STAT1/STAT3 pathway Mol. Cell. Biol. 29, 5084-5093
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5084-5093
    • Diao, Y.1    Wang, X.2    Wu, Z.3
  • 49
    • 14244252323 scopus 로고    scopus 로고
    • GATA-6 can act as a positive or negative regulator of smooth muscle-specific gene expression
    • Yin, F. and Herring, B. P. (2005) GATA-6 can act as a positive or negative regulator of smooth muscle-specific gene expression J. Biol. Chem. 280, 4745-4752
    • (2005) J. Biol. Chem. , vol.280 , pp. 4745-4752
    • Yin, F.1    Herring, B.P.2
  • 53
    • 84864021783 scopus 로고    scopus 로고
    • Constitutive notch activation upregulates pax7 and promotes the self-renewal of skeletal muscle satellite cells
    • Wen, Y., Bi, P., Liu, W., Asakura, A., Keller, C., and Kuang, S. (2012) Constitutive notch activation upregulates pax7 and promotes the self-renewal of skeletal muscle satellite cells Mol. Cell. Biol. 32, 2300-2311
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 2300-2311
    • Wen, Y.1    Bi, P.2    Liu, W.3    Asakura, A.4    Keller, C.5    Kuang, S.6
  • 55
    • 78149327922 scopus 로고    scopus 로고
    • CLP-1 associates with MyoD and HDAC to restore skeletal muscle cell regeneration
    • Galatioto, J., Mascareno, E., and Siddiqui, M. A. (2010) CLP-1 associates with MyoD and HDAC to restore skeletal muscle cell regeneration J. Cell Sci. 123, 3789-3795
    • (2010) J. Cell Sci. , vol.123 , pp. 3789-3795
    • Galatioto, J.1    Mascareno, E.2    Siddiqui, M.A.3
  • 56
    • 0033580826 scopus 로고    scopus 로고
    • Insulin-like growth factor-II, phosphatidylinositol 3-kinase, nuclear factor-kappaB and inducible nitric-oxide synthase define a common myogenic signaling pathway
    • Kaliman, P., Canicio, J., Testar, X., Palacin, M., and Zorzano, A. (1999) Insulin-like growth factor-II, phosphatidylinositol 3-kinase, nuclear factor-kappaB and inducible nitric-oxide synthase define a common myogenic signaling pathway J. Biol. Chem. 274, 17437-17444
    • (1999) J. Biol. Chem. , vol.274 , pp. 17437-17444
    • Kaliman, P.1    Canicio, J.2    Testar, X.3    Palacin, M.4    Zorzano, A.5
  • 57
    • 34547095498 scopus 로고    scopus 로고
    • Biomechanical signals upregulate myogenic gene induction in the presence or absence of inflammation
    • Chandran, R., Knobloch, T. J., Anghelina, M., and Agarwal, S. (2007) Biomechanical signals upregulate myogenic gene induction in the presence or absence of inflammation Am. J. Physiol. Cell Physiol. 293, C267-276
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293 , pp. 267-276
    • Chandran, R.1    Knobloch, T.J.2    Anghelina, M.3    Agarwal, S.4
  • 59
    • 0032006563 scopus 로고    scopus 로고
    • P300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation
    • Kraus, W. L. and Kadonaga, J. T. (1998) p300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation Genes Dev. 12, 331-342
    • (1998) Genes Dev. , vol.12 , pp. 331-342
    • Kraus, W.L.1    Kadonaga, J.T.2


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