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Volumn 101, Issue 4, 2009, Pages 193-205

Histone deacetylases: Salesmen and customers in the post-translational modification market

Author keywords

Cancer; Histone deacetylase; Post translational modification; Signalling

Indexed keywords

AURORA A KINASE; CYCLIN DEPENDENT KINASE 1; HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 4; JANUS KINASE 2; MITOGEN ACTIVATED PROTEIN KINASE; PARKIN; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN KINASE C; PROTEIN MDM2; VALPROIC ACID; HISTONE; ISOENZYME;

EID: 61549116543     PISSN: 02484900     EISSN: 1768322X     Source Type: Journal    
DOI: 10.1042/BC20080158     Document Type: Review
Times cited : (104)

References (92)
  • 2
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali, P., Pranpat, M., Bradner, J., Balasis, M., Fiskus, W., Guo, F., Rocha, K., Kumaraswamy, S., Boyapalle, S., Atadja, P., Seto, E. and Bhalla, K. (2005) Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J. Biol. Chem. 280, 26729-26734
    • (2005) J. Biol. Chem , vol.280 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3    Balasis, M.4    Fiskus, W.5    Guo, F.6    Rocha, K.7    Kumaraswamy, S.8    Boyapalle, S.9    Atadja, P.10    Seto, E.11    Bhalla, K.12
  • 3
    • 0036898253 scopus 로고    scopus 로고
    • Acetylation inactivates the transcriptional repressor BCL6
    • Bereshchenko, O.R., Gu, W. and Dalla-Favera, R. (2002) Acetylation inactivates the transcriptional repressor BCL6. Nat. Genet. 32, 606-613
    • (2002) Nat. Genet , vol.32 , pp. 606-613
    • Bereshchenko, O.R.1    Gu, W.2    Dalla-Favera, R.3
  • 4
    • 0141987892 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation
    • Bloom, J., Amador, V., Bartolini, F., DeMartino, G. and Pagano, M. (2003) Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation. Cell 115, 71-82
    • (2003) Cell , vol.115 , pp. 71-82
    • Bloom, J.1    Amador, V.2    Bartolini, F.3    DeMartino, G.4    Pagano, M.5
  • 5
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden, J.E., Peart, M.J. and Johnstone, R.W. (2006) Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Discov. 5, 769-784
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 7
    • 1542289920 scopus 로고    scopus 로고
    • Deactylase inhibitors disrupt cellular complexes containing protein phosphatases and deacetylases
    • Brush, M.H., Guardiola, A., Connor, J.H., Yao, T.P. and Shenolikar, S. (2004) Deactylase inhibitors disrupt cellular complexes containing protein phosphatases and deacetylases. J. Biol. Chem. 279, 7685-7691
    • (2004) J. Biol. Chem , vol.279 , pp. 7685-7691
    • Brush, M.H.1    Guardiola, A.2    Connor, J.H.3    Yao, T.P.4    Shenolikar, S.5
  • 10
    • 2942735131 scopus 로고    scopus 로고
    • SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1
    • Cheng, J., Wang, D., Wang, Z. and Yeh, E.T. (2004) SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1. Mol. Cell. Biol. 24, 6021-6028
    • (2004) Mol. Cell. Biol , vol.24 , pp. 6021-6028
    • Cheng, J.1    Wang, D.2    Wang, Z.3    Yeh, E.T.4
  • 11
    • 0038050244 scopus 로고    scopus 로고
    • The adenovirus protein Gam1 interferes with sumoylation of histone deacetylase 1
    • Colombo, R., Boggio, R., Seiser, C., Draetta, G.F. and Chiocca, S. (2002) The adenovirus protein Gam1 interferes with sumoylation of histone deacetylase 1. EMBO Rep. 3, 1062-1068
    • (2002) EMBO Rep , vol.3 , pp. 1062-1068
    • Colombo, R.1    Boggio, R.2    Seiser, C.3    Draetta, G.F.4    Chiocca, S.5
  • 12
    • 0037189568 scopus 로고    scopus 로고
    • SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
    • David, G., Neptune, M.A. and DePinho, R.A. (2002) SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities. J. Biol. Chem. 277, 23658-23663
    • (2002) J. Biol. Chem , vol.277 , pp. 23658-23663
    • David, G.1    Neptune, M.A.2    DePinho, R.A.3
  • 14
  • 17
    • 3242671372 scopus 로고    scopus 로고
    • A field guide to ubiquitylation
    • Fang, S. and Weissman, A.M. (2004) A field guide to ubiquitylation. Cell. Mol. Life Sci. 61, 1546-1561
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 1546-1561
    • Fang, S.1    Weissman, A.M.2
  • 18
    • 53649100104 scopus 로고    scopus 로고
    • JNK2-dependent regulation of SIRT1 protein stability
    • Ford, J., Ahmed, S., Allison, S., Jiang, M. and Milner, J. (2008) JNK2-dependent regulation of SIRT1 protein stability. Cell Cycle 7, 3091-3097
    • (2008) Cell Cycle , vol.7 , pp. 3091-3097
    • Ford, J.1    Ahmed, S.2    Allison, S.3    Jiang, M.4    Milner, J.5
  • 19
    • 0037205476 scopus 로고    scopus 로고
    • Phosphatase inhibition leads to histone deacetylases 1 and 2 phosphorylation and disruption of corepressor interactions
    • Galasinski, S.C., Resing, K.A., Goodrich, J.A. and Ahn, N.G. (2002) Phosphatase inhibition leads to histone deacetylases 1 and 2 phosphorylation and disruption of corepressor interactions. J. Biol. Chem. 277, 19618-19626
    • (2002) J. Biol. Chem , vol.277 , pp. 19618-19626
    • Galasinski, S.C.1    Resing, K.A.2    Goodrich, J.A.3    Ahn, N.G.4
  • 20
    • 13744257306 scopus 로고    scopus 로고
    • Regulation of androgen receptor and histone deacetylase 1 by Mdm2-mediated ubiquitylation
    • Gaughan, L., Logan, I.R., Neal, D.E. and Robson, C.N. (2005) Regulation of androgen receptor and histone deacetylase 1 by Mdm2-mediated ubiquitylation. Nucleic Acids Res. 33, 13-26
    • (2005) Nucleic Acids Res , vol.33 , pp. 13-26
    • Gaughan, L.1    Logan, I.R.2    Neal, D.E.3    Robson, C.N.4
  • 21
    • 36548998840 scopus 로고    scopus 로고
    • Concepts in sumoylation: A decade on
    • Geiss-Friedlander, R. and Melchior, F. (2007) Concepts in sumoylation: a decade on. Nat. Rev. 8, 947-956
    • (2007) Nat. Rev , vol.8 , pp. 947-956
    • Geiss-Friedlander, R.1    Melchior, F.2
  • 22
    • 33845970925 scopus 로고    scopus 로고
    • Parallel SUMOylation-dependent pathways mediate gene- and signal-specific transrepression by LXRs and PPAR?
    • Ghisletti, S., Huang, W., Ogawa, S., Pascual, G., Lin, M.E., Willson, T.M., Rosenfeld, M.G. and Glass, C.K. (2007) Parallel SUMOylation-dependent pathways mediate gene- and signal-specific transrepression by LXRs and PPAR?. Mol. Cell 25, 57-70
    • (2007) Mol. Cell , vol.25 , pp. 57-70
    • Ghisletti, S.1    Huang, W.2    Ogawa, S.3    Pascual, G.4    Lin, M.E.5    Willson, T.M.6    Rosenfeld, M.G.7    Glass, C.K.8
  • 23
    • 34547897023 scopus 로고    scopus 로고
    • Histone deacetylases and cancer
    • Glozak, M.A. and Seto, E. (2007) Histone deacetylases and cancer. Oncogene 26, 5420-5432
    • (2007) Oncogene , vol.26 , pp. 5420-5432
    • Glozak, M.A.1    Seto, E.2
  • 25
    • 14844344773 scopus 로고    scopus 로고
    • Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors
    • Gregoire, S. and Yang, X.J. (2005) Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors. Mol. Cell. Biol. 25, 2273-2287
    • (2005) Mol. Cell. Biol , vol.25 , pp. 2273-2287
    • Gregoire, S.1    Yang, X.J.2
  • 26
    • 0034608955 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization
    • Grozinger, C.M. and Schreiber, S.L. (2000) Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. Proc. Natl. Acad. Sci. U.S.A. 97, 7835-7840
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 7835-7840
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 27
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • Grozinger, C.M. and Schreiber, S.L. (2002) Deacetylase enzymes: biological functions and the use of small-molecule inhibitors. Chem. Biol. 9, 3-16
    • (2002) Chem. Biol , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 28
    • 20744456118 scopus 로고    scopus 로고
    • Guidez, F., Howell, L., Isalan, M., Cebrat, M., Alani, R.M., Ivins, S., Hormaeche, I., McConnell, M.J., Pierce, S., Cole, P.A. et al. (2005) Histone acetyltransferase activity of p300 is required for transcriptional repression by the promyelocytic leukemia zinc finger protein. Mol. Cell. Biol. 25, 5552-5566
    • Guidez, F., Howell, L., Isalan, M., Cebrat, M., Alani, R.M., Ivins, S., Hormaeche, I., McConnell, M.J., Pierce, S., Cole, P.A. et al. (2005) Histone acetyltransferase activity of p300 is required for transcriptional repression by the promyelocytic leukemia zinc finger protein. Mol. Cell. Biol. 25, 5552-5566
  • 29
    • 33846203708 scopus 로고    scopus 로고
    • ATM regulates ionizing radiation-induced disruption of HDAC1:PP1:Rb complexes
    • Guo, C., Mi, J., Brautigan, D.L. and Larner, J.M. (2007) ATM regulates ionizing radiation-induced disruption of HDAC1:PP1:Rb complexes. Cell. Signal. 19, 504-510
    • (2007) Cell. Signal , vol.19 , pp. 504-510
    • Guo, C.1    Mi, J.2    Brautigan, D.L.3    Larner, J.M.4
  • 30
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay, R.T. (2005) SUMO: a history of modification. Mol. Cell 18, 1-12
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 31
    • 47049127380 scopus 로고    scopus 로고
    • Pharmacodynamic markers for histone deacetylase inhibitor development
    • Heinzel, T. and Krämer, O.H. (2008) Pharmacodynamic markers for histone deacetylase inhibitor development. Drug Discov. Today 4, 277-283
    • (2008) Drug Discov. Today , vol.4 , pp. 277-283
    • Heinzel, T.1    Krämer, O.H.2
  • 32
    • 34248656480 scopus 로고    scopus 로고
    • Histone deacetylases-an important class of cellular regulators with a variety of functions
    • Hildmann, C., Riester, D. and Schwienhorst, A. (2007) Histone deacetylases-an important class of cellular regulators with a variety of functions. Appl. Microbiol. Biotechnol. 75, 487-497
    • (2007) Appl. Microbiol. Biotechnol , vol.75 , pp. 487-497
    • Hildmann, C.1    Riester, D.2    Schwienhorst, A.3
  • 33
    • 0037108963 scopus 로고    scopus 로고
    • Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes
    • Hook, S.S., Orian, A., Cowley, S.M. and Eisenman, R.N. (2002) Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes. Proc. Natl. Acad. Sci. U.S.A. 99, 13425-13430
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 13425-13430
    • Hook, S.S.1    Orian, A.2    Cowley, S.M.3    Eisenman, R.N.4
  • 34
    • 33749572938 scopus 로고    scopus 로고
    • Valproate inhibition of histone deacetylase 2 affects differentiation and decreases proliferation of endometrial stromal sarcoma cells
    • Hrzenjak, A., Moinfar, F., Kremser, M.L., Strohmeier, B., Staber, P.B., Zatloukal, K. and Denk, H. (2006) Valproate inhibition of histone deacetylase 2 affects differentiation and decreases proliferation of endometrial stromal sarcoma cells. Mol. Cancer Ther. 5, 2203-2210
    • (2006) Mol. Cancer Ther , vol.5 , pp. 2203-2210
    • Hrzenjak, A.1    Moinfar, F.2    Kremser, M.L.3    Strohmeier, B.4    Staber, P.B.5    Zatloukal, K.6    Denk, H.7
  • 35
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T. and Allis, C.D. (2001) Translating the histone code. Science 293, 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 36
    • 0037088610 scopus 로고    scopus 로고
    • Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70
    • Johnson, C.A., White, D.A., Lavender, J.S., O'Neill, L.P. and Turner, B.M. (2002) Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70. J. Biol. Chem. 277, 9590-9597
    • (2002) J. Biol. Chem , vol.277 , pp. 9590-9597
    • Johnson, C.A.1    White, D.A.2    Lavender, J.S.3    O'Neill, L.P.4    Turner, B.M.5
  • 37
    • 4344685827 scopus 로고    scopus 로고
    • Expression profiling of sodium butyrate (NaB)-treated cells: Identification of regulation of genes related to cytokine signaling and cancer metastasis by NaB
    • Joseph, J., Mudduluru, G., Antony, S., Vashistha, S., Ajitkumar, P. and Somasundaram, K. (2004) Expression profiling of sodium butyrate (NaB)-treated cells: identification of regulation of genes related to cytokine signaling and cancer metastasis by NaB. Oncogene 23, 6304-6315
    • (2004) Oncogene , vol.23 , pp. 6304-6315
    • Joseph, J.1    Mudduluru, G.2    Antony, S.3    Vashistha, S.4    Ajitkumar, P.5    Somasundaram, K.6
  • 38
    • 34547515687 scopus 로고    scopus 로고
    • Histone deacetylase 1 phosphorylation at S421 and S423 is constitutive invivo, but dispensable invitro
    • Karwowska-Desaulniers, P., Ketko, A., Kamath, N. and Pflum, M.K. (2007) Histone deacetylase 1 phosphorylation at S421 and S423 is constitutive invivo, but dispensable invitro. Biochem. Biophys. Res. Commun. 361, 349-355
    • (2007) Biochem. Biophys. Res. Commun , vol.361 , pp. 349-355
    • Karwowska-Desaulniers, P.1    Ketko, A.2    Kamath, N.3    Pflum, M.K.4
  • 39
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi, Y., Kovacs, J.J., McLaurin, A., Vance, J.M., Ito, A. and Yao, T.P. (2003) The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115, 727-738
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.P.6
  • 42
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. (2007) Chromatin modifications and their function. Cell 128, 693-705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 46
    • 43249104204 scopus 로고    scopus 로고
    • Mechanism for ubiquitylation of the leukemia fusion proteins AML1-ETO and PML-RARα
    • Krämer, O.H., Müller, S., Buchwald, M., Reichardt, S. and Heinzel, T. (2008a) Mechanism for ubiquitylation of the leukemia fusion proteins AML1-ETO and PML-RARα. FASEB J. 22, 1369-1379
    • (2008) FASEB J , vol.22 , pp. 1369-1379
    • Krämer, O.H.1    Müller, S.2    Buchwald, M.3    Reichardt, S.4    Heinzel, T.5
  • 47
    • 38749121729 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and hydroxyurea modulate the cell cycle and cooperatively induce apoptosis
    • Krämer, O.H., Knauer, S.K., Zimmermann, D., Stauber, R.H. and Heinzel, T. (2008b) Histone deacetylase inhibitors and hydroxyurea modulate the cell cycle and cooperatively induce apoptosis. Oncogene 27, 732-740
    • (2008) Oncogene , vol.27 , pp. 732-740
    • Krämer, O.H.1    Knauer, S.K.2    Zimmermann, D.3    Stauber, R.H.4    Heinzel, T.5
  • 49
    • 0346725952 scopus 로고    scopus 로고
    • Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A
    • Lee, H., Rezai-Zadeh, N. and Seto, E. (2004) Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A. Mol. Cell. Biol. 24, 765-773
    • (2004) Mol. Cell. Biol , vol.24 , pp. 765-773
    • Lee, H.1    Rezai-Zadeh, N.2    Seto, E.3
  • 50
    • 4544229876 scopus 로고    scopus 로고
    • Phosphorylation of the histone deacetylase 7 modulates its stability and association with 14-3-3 proteins
    • Li, X., Song, S., Liu, Y., Ko, S.H. and Kao, H.Y. (2004) Phosphorylation of the histone deacetylase 7 modulates its stability and association with 14-3-3 proteins. J. Biol. Chem. 279, 34201-34208
    • (2004) J. Biol. Chem , vol.279 , pp. 34201-34208
    • Li, X.1    Song, S.2    Liu, Y.3    Ko, S.H.4    Kao, H.Y.5
  • 51
    • 34547919621 scopus 로고    scopus 로고
    • Class IIa histone deacetylases: Regulating the regulators
    • Martin, M., Kettmann, R. and Dequiedt, F. (2007) Class IIa histone deacetylases: regulating the regulators. Oncogene 26, 5450-5467
    • (2007) Oncogene , vol.26 , pp. 5450-5467
    • Martin, M.1    Kettmann, R.2    Dequiedt, F.3
  • 53
    • 0034597816 scopus 로고    scopus 로고
    • Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation
    • McKinsey, T.A., Zhang, C.L., Lu, J. and Olson, E.N. (2000) Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation. Nature 408, 106-111
    • (2000) Nature , vol.408 , pp. 106-111
    • McKinsey, T.A.1    Zhang, C.L.2    Lu, J.3    Olson, E.N.4
  • 54
  • 55
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier, R., Penot, G., Hubner, M.R., Reid, G., Brand, H., Kos, M. and Gannon, F. (2003) Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115, 751-763
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 56
    • 42049108221 scopus 로고    scopus 로고
    • Cell biology: SUMO
    • Meulmeester, E. and Melchior, F. (2008) Cell biology: SUMO. Nature 452, 709-711
    • (2008) Nature , vol.452 , pp. 709-711
    • Meulmeester, E.1    Melchior, F.2
  • 57
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: Insights into their biological function
    • Michan, S. and Sinclair, D. (2007) Sirtuins in mammals: insights into their biological function. Biochem. J. 404, 1-13
    • (2007) Biochem. J , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 58
    • 3042566927 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor trichostatin A modulates CD4+ T cell responses
    • Moreira, J.M., Scheipers, P. and Sorensen, P. (2003) The histone deacetylase inhibitor trichostatin A modulates CD4+ T cell responses. BMC Cancer 3, 30
    • (2003) BMC Cancer , vol.3 , pp. 30
    • Moreira, J.M.1    Scheipers, P.2    Sorensen, P.3
  • 59
    • 0344304443 scopus 로고    scopus 로고
    • Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1
    • Nusinzon, I. and Horvath, C.M. (2003) Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1. Proc. Natl. Acad. Sci. U.S.A. 100, 14742-14747
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 14742-14747
    • Nusinzon, I.1    Horvath, C.M.2
  • 61
    • 33947311828 scopus 로고    scopus 로고
    • Myosin phosphatase dephosphorylates HDAC7, controls its nucleocytoplasmic shuttling, and inhibits apoptosis in thymocytes
    • Parra, M., Mahmoudi, T. and Verdin, E. (2007) Myosin phosphatase dephosphorylates HDAC7, controls its nucleocytoplasmic shuttling, and inhibits apoptosis in thymocytes. Genes Dev. 21, 638-643
    • (2007) Genes Dev , vol.21 , pp. 638-643
    • Parra, M.1    Mahmoudi, T.2    Verdin, E.3
  • 62
    • 2542579359 scopus 로고    scopus 로고
    • Getting into position: The catalytic mechanisms of protein ubiquitylation
    • Passmore, L.A. and Barford, D. (2004) Getting into position: the catalytic mechanisms of protein ubiquitylation. Biochem. J. 379, 513-525
    • (2004) Biochem. J , vol.379 , pp. 513-525
    • Passmore, L.A.1    Barford, D.2
  • 63
    • 0038521295 scopus 로고    scopus 로고
    • Petrie, K., Guidez, F., Howell, L., Healy, L., Waxman, S., Greaves, M. and Zelent, A. (2003) The histone deacetylase 9 gene encodes multiple protein isoforms. J. Biol. Chem. 278, 16059-16072
    • Petrie, K., Guidez, F., Howell, L., Healy, L., Waxman, S., Greaves, M. and Zelent, A. (2003) The histone deacetylase 9 gene encodes multiple protein isoforms. J. Biol. Chem. 278, 16059-16072
  • 64
    • 0035861594 scopus 로고    scopus 로고
    • Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation
    • Pflum, M.K., Tong, J.K., Lane, W.S. and Schreiber, S.L. (2001) Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation. J. Biol. Chem. 276, 47733-47741
    • (2001) J. Biol. Chem , vol.276 , pp. 47733-47741
    • Pflum, M.K.1    Tong, J.K.2    Lane, W.S.3    Schreiber, S.L.4
  • 65
    • 36849093080 scopus 로고    scopus 로고
    • Protein kinase CK2 is a key activator of histone deacetylase in hypoxia-associated tumors
    • Pluemsampant, S., Safronova, O.S., Nakahama, K. and Morita, I. (2008) Protein kinase CK2 is a key activator of histone deacetylase in hypoxia-associated tumors. Int. J. Cancer 122, 333-341
    • (2008) Int. J. Cancer , vol.122 , pp. 333-341
    • Pluemsampant, S.1    Safronova, O.S.2    Nakahama, K.3    Morita, I.4
  • 66
    • 34250758641 scopus 로고    scopus 로고
    • HEF1-dependent Aurora A activation induces disassembly of the primary cilium
    • Pugacheva, E.N., Jablonski, S.A., Hartman, T.R., Henske, E.P. and Golemis, E.A. (2007) HEF1-dependent Aurora A activation induces disassembly of the primary cilium. Cell 129, 1351-1363
    • (2007) Cell , vol.129 , pp. 1351-1363
    • Pugacheva, E.N.1    Jablonski, S.A.2    Hartman, T.R.3    Henske, E.P.4    Golemis, E.A.5
  • 68
    • 33744792310 scopus 로고    scopus 로고
    • Sensors and signals: A coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response
    • Rosenfeld, M.G., Lunyak, V.V. and Glass, C.K. (2006) Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response. Genes Dev. 20, 1405-1428
    • (2006) Genes Dev , vol.20 , pp. 1405-1428
    • Rosenfeld, M.G.1    Lunyak, V.V.2    Glass, C.K.3
  • 69
    • 0037074010 scopus 로고    scopus 로고
    • Signaling network model of chromatin
    • Schreiber, S.L. and Bernstein, B.E. (2002) Signaling network model of chromatin. Cell 111, 771-778
    • (2002) Cell , vol.111 , pp. 771-778
    • Schreiber, S.L.1    Bernstein, B.E.2
  • 70
    • 0035163063 scopus 로고    scopus 로고
    • Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways
    • Seigneurin-Berny, D., Verdel, A., Curtet, S., Lemercier, C., Garin, J., Rousseaux, S. and Khochbin, S. (2001) Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways. Mol. Cell. Biol. 21, 8035-8044
    • (2001) Mol. Cell. Biol , vol.21 , pp. 8035-8044
    • Seigneurin-Berny, D.1    Verdel, A.2    Curtet, S.3    Lemercier, C.4    Garin, J.5    Rousseaux, S.6    Khochbin, S.7
  • 71
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • Spange, S., Wagner, T., Heinzel, T. and Kramer, O.H. (2009) Acetylation of non-histone proteins modulates cellular signalling at multiple levels. Int. J. Biochem. Cell Biol. 41, 185-198
    • (2009) Int. J. Biochem. Cell Biol , vol.41 , pp. 185-198
    • Spange, S.1    Wagner, T.2    Heinzel, T.3    Kramer, O.H.4
  • 72
    • 34147208064 scopus 로고    scopus 로고
    • An acetylation/ deacetylation-SUMOylation switch through a phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1 regulates transcriptional repression activity
    • Stankovic-Valentin, N., Deltour, S., Seeler, J., Pinte, S., Vergoten, G., Guerardel, C., Dejean, A. and Leprince, D. (2007) An acetylation/ deacetylation-SUMOylation switch through a phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1 regulates transcriptional repression activity. Mol. Cell. Biol. 27, 2661-2675
    • (2007) Mol. Cell. Biol , vol.27 , pp. 2661-2675
    • Stankovic-Valentin, N.1    Deltour, S.2    Seeler, J.3    Pinte, S.4    Vergoten, G.5    Guerardel, C.6    Dejean, A.7    Leprince, D.8
  • 73
    • 0037184021 scopus 로고    scopus 로고
    • The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2
    • Sun, J.M., Chen, H.Y., Moniwa, M., Litchfield, D.W., Seto, E. and Davie, J.R. (2002) The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2. J. Biol. Chem. 277, 35783-35786
    • (2002) J. Biol. Chem , vol.277 , pp. 35783-35786
    • Sun, J.M.1    Chen, H.Y.2    Moniwa, M.3    Litchfield, D.W.4    Seto, E.5    Davie, J.R.6
  • 74
    • 36448954666 scopus 로고    scopus 로고
    • Differential distribution of unmodified and phosphorylated histone deacetylase 2 in chromatin
    • Sun, J.M., Chen, H.Y. and Davie, J.R. (2007) Differential distribution of unmodified and phosphorylated histone deacetylase 2 in chromatin. J. Biol. Chem. 282, 33227-33236
    • (2007) J. Biol. Chem , vol.282 , pp. 33227-33236
    • Sun, J.M.1    Chen, H.Y.2    Davie, J.R.3
  • 76
    • 1842557733 scopus 로고    scopus 로고
    • Regulation of mammalian epithelial differentiation and intestine development by class I histone deacetylases
    • Tou, L., Liu, Q. and Shivdasani, R.A. (2004) Regulation of mammalian epithelial differentiation and intestine development by class I histone deacetylases. Mol. Cell. Biol. 24, 3132-3139
    • (2004) Mol. Cell. Biol , vol.24 , pp. 3132-3139
    • Tou, L.1    Liu, Q.2    Shivdasani, R.A.3
  • 77
    • 0037199944 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 2 by protein kinase CK2
    • Tsai, S.C. and Seto, E. (2002) Regulation of histone deacetylase 2 by protein kinase CK2. J. Biol. Chem. 277, 31826-31833
    • (2002) J. Biol. Chem , vol.277 , pp. 31826-31833
    • Tsai, S.C.1    Seto, E.2
  • 78
    • 33645640622 scopus 로고    scopus 로고
    • Parkin ubiquitinates and promotes the degradation of RanBP2
    • Um, J.W., Min, D.S., Rhim, H., Kim, J., Paik, S.R. and Chung, K.C. (2006) Parkin ubiquitinates and promotes the degradation of RanBP2. J. Biol. Chem. 281, 3595-3603
    • (2006) J. Biol. Chem , vol.281 , pp. 3595-3603
    • Um, J.W.1    Min, D.S.2    Rhim, H.3    Kim, J.4    Paik, S.R.5    Chung, K.C.6
  • 79
    • 33645772214 scopus 로고    scopus 로고
    • Tumour necrosis factor-a depletes histone deacetylase 1 protein through IKK2
    • Vashisht Gopal, Y.N., Arora, T.S. and Van Dyke, M.W. (2006) Tumour necrosis factor-a depletes histone deacetylase 1 protein through IKK2. EMBO Rep. 7, 291-296
    • (2006) EMBO Rep , vol.7 , pp. 291-296
    • Vashisht Gopal, Y.N.1    Arora, T.S.2    Van Dyke, M.W.3
  • 80
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: Versatile regulators
    • Verdin, E., Dequiedt, F. and Kasler, H.G. (2003) Class II histone deacetylases: versatile regulators. Trends Genet. 19, 286-293
    • (2003) Trends Genet , vol.19 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 81
    • 33744813908 scopus 로고    scopus 로고
    • CK2 signaling in androgen-dependent and -independent prostate cancer
    • Wang, G., Ahmad, K.A., Unger, G., Slaton, J.W. and Ahmed, K. (2006) CK2 signaling in androgen-dependent and -independent prostate cancer. J. Cell. Biochem. 99, 382-391
    • (2006) J. Cell. Biochem , vol.99 , pp. 382-391
    • Wang, G.1    Ahmad, K.A.2    Unger, G.3    Slaton, J.W.4    Ahmed, K.5
  • 82
    • 45549101405 scopus 로고    scopus 로고
    • Control of endothelial cell proliferation and migration by VEGF signaling to histone deacetylase 7
    • Wang, S., Li, X., Parra, M., Verdin, E., Bassel-Duby, R. and Olson, E.N. (2008) Control of endothelial cell proliferation and migration by VEGF signaling to histone deacetylase 7. Proc. Natl. Acad. Sci. U.S.A. 105, 7738-7743
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 7738-7743
    • Wang, S.1    Li, X.2    Parra, M.3    Verdin, E.4    Bassel-Duby, R.5    Olson, E.N.6
  • 83
    • 0038333357 scopus 로고    scopus 로고
    • Stimulation of preadipocyte differentiation by steroid through targeting of an HDAC1 complex
    • Wiper-Bergeron, N., Wu, D., Pope, L., Schild-Poulter, C. and Hache, R.J. (2003) Stimulation of preadipocyte differentiation by steroid through targeting of an HDAC1 complex. EMBO J. 22, 2135-2145
    • (2003) EMBO J , vol.22 , pp. 2135-2145
    • Wiper-Bergeron, N.1    Wu, D.2    Pope, L.3    Schild-Poulter, C.4    Hache, R.J.5
  • 84
    • 7044250740 scopus 로고    scopus 로고
    • Lysine acetylation and the bromodomain: A new partnership for signaling
    • Yang, X.J. (2004) Lysine acetylation and the bromodomain: a new partnership for signaling. Bioessays 26, 1076-1087
    • (2004) Bioessays , vol.26 , pp. 1076-1087
    • Yang, X.J.1
  • 85
    • 34547924046 scopus 로고    scopus 로고
    • HATs and HDACs: From structure, function and regulation to novel strategies for therapy and prevention
    • Yang, X.J. and Seto, E. (2007) HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention. Oncogene 26, 5310-5318
    • (2007) Oncogene , vol.26 , pp. 5310-5318
    • Yang, X.J.1    Seto, E.2
  • 86
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3/Hda1 family of lysine deacetylases: From bacteria and yeast to mice and men
    • Yang, X.J. and Seto, E. (2008) The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. Nat. Rev. 9, 206-218
    • (2008) Nat. Rev , vol.9 , pp. 206-218
    • Yang, X.J.1    Seto, E.2
  • 87
    • 35748962613 scopus 로고    scopus 로고
    • SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress
    • Yang, Y., Fu, W., Chen, J., Olashaw, N., Zhang, X., Nicosia, S.V., Bhalla, K. and Bai, W. (2007) SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress. Nat. Cell Biol. 9, 1253-1262
    • (2007) Nat. Cell Biol , vol.9 , pp. 1253-1262
    • Yang, Y.1    Fu, W.2    Chen, J.3    Olashaw, N.4    Zhang, X.5    Nicosia, S.V.6    Bhalla, K.7    Bai, W.8
  • 88
    • 0037162697 scopus 로고    scopus 로고
    • Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy
    • Zhang, C.L., McKinsey, T.A., Chang, S., Antos, C.L., Hill, J.A. and Olson, E.N. (2002) Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy. Cell 110, 479-488
    • (2002) Cell , vol.110 , pp. 479-488
    • Zhang, C.L.1    McKinsey, T.A.2    Chang, S.3    Antos, C.L.4    Hill, J.A.5    Olson, E.N.6
  • 89
    • 17044370869 scopus 로고    scopus 로고
    • Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4
    • Zhang, X., Ozawa, Y., Lee, H., Wen, Y.D., Tan, T.H., Wadzinski, B.E. and Seto, E. (2005) Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4. Genes Dev. 19, 827-839
    • (2005) Genes Dev , vol.19 , pp. 827-839
    • Zhang, X.1    Ozawa, Y.2    Lee, H.3    Wen, Y.D.4    Tan, T.H.5    Wadzinski, B.E.6    Seto, E.7
  • 91
    • 25444462980 scopus 로고    scopus 로고
    • Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications
    • Zhao, X., Sternsdorf, T., Bolger, T.A., Evans, R.M. and Yao, T.P. (2005) Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications. Mol. Cell. Biol. 25, 8456-8464
    • (2005) Mol. Cell. Biol , vol.25 , pp. 8456-8464
    • Zhao, X.1    Sternsdorf, T.2    Bolger, T.A.3    Evans, R.M.4    Yao, T.P.5


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