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Volumn 19, Issue 7, 2005, Pages 827-839

Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4

Author keywords

HDAC3; Histone deacetylation; PP4; Protein phosphatase

Indexed keywords

HISTONE; HISTONE DEACETYLASE; HISTONE DEACETYLASE 3; NUCLEAR RECEPTOR COREPRESSOR; PHOSPHATASE; PROTEIN SERINE THREONINE PHOSPHATASE 4; SILENCING MEDIATOR FOR RETINOID AND THYROID RECEPTOR PROTEIN; UNCLASSIFIED DRUG;

EID: 17044370869     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1286005     Document Type: Article
Times cited : (188)

References (89)
  • 1
    • 0034817075 scopus 로고    scopus 로고
    • ETO, a target of t(8; 21) in acute leukemia, makes distinct contacts with multiple historic deacetylases and binds mSin3A through its oligomerization domain
    • Amann, J.M., Nip, J., Strom, D.K., Lutterbach, B., Harada, H., Lenny, N., Downing, J.R., Meyers, S., and Hiebert, S.W. 2001. ETO, a target of t(8; 21) in acute leukemia, makes distinct contacts with multiple historic deacetylases and binds mSin3A through its oligomerization domain. Mol. Cell. Biol. 21: 6470-6483.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6470-6483
    • Amann, J.M.1    Nip, J.2    Strom, D.K.3    Lutterbach, B.4    Harada, H.5    Lenny, N.6    Downing, J.R.7    Meyers, S.8    Hiebert, S.W.9
  • 2
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom, N., Gammeltoft, S., and Brunak, S. 1999. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J. Mol. Biol. 294: 1351-1362.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 3
    • 0035233898 scopus 로고    scopus 로고
    • Two-dimensional phosphoamino acid analysis
    • Blume-Jensen, P. and Hunter, T. 2001. Two-dimensional phosphoamino acid analysis. Methods Mol. Biol. 124: 49-65.
    • (2001) Methods Mol. Biol. , vol.124 , pp. 49-65
    • Blume-Jensen, P.1    Hunter, T.2
  • 4
    • 0034800738 scopus 로고    scopus 로고
    • Total synthesis of fostriecin (CI-920)
    • Boger, D.L., Ichikawa, S., and Zhong, W. 2001. Total synthesis of fostriecin (CI-920). J. Am. Chem. Soc. 123: 4161-4167.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 4161-4167
    • Boger, D.L.1    Ichikawa, S.2    Zhong, W.3
  • 5
    • 0032484989 scopus 로고    scopus 로고
    • Retinoblastoma protein recruits histone deacetylase to repress transcription
    • Brehm, A., Miska, E.A., McCance, D.J., Reid, J.L., Bannister, A.J., and Kouzarides, T. 1998. Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature 391: 597-601.
    • (1998) Nature , vol.391 , pp. 597-601
    • Brehm, A.1    Miska, E.A.2    McCance, D.J.3    Reid, J.L.4    Bannister, A.J.5    Kouzarides, T.6
  • 6
    • 0027522757 scopus 로고
    • PPX, a novel protein serine/threonine phosphatase localized to centrosomes
    • Brewis, N.D., Street, A.J., Prescott, A.R., and Cohen, P.T. 1993. PPX, a novel protein serine/threonine phosphatase localized to centrosomes. EMBO J. 12: 987-996.
    • (1993) EMBO J. , vol.12 , pp. 987-996
    • Brewis, N.D.1    Street, A.J.2    Prescott, A.R.3    Cohen, P.T.4
  • 8
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-κB action regulated by reversible acetylation
    • Chen, L., Fischle, W., Verdin, E., and Greene, W.C. 2001. Duration of nuclear NF-κB action regulated by reversible acetylation. Science 293: 1653-1657.
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 9
    • 0032528624 scopus 로고    scopus 로고
    • Fostriecin-mediated G2-M-phase growth arrest correlates with abnormal centrosome replication, the formation of aberrant mitotic spindles, and the inhibition of serine/threonine protein phosphatase activity
    • Cheng, A., Balczon, R., Zuo, Z., Koons, J.S., Walsh, A.H., and Honkanen, R.E. 1998. Fostriecin-mediated G2-M-phase growth arrest correlates with abnormal centrosome replication, the formation of aberrant mitotic spindles, and the inhibition of serine/threonine protein phosphatase activity. Cancer Res. 58: 3611-3619.
    • (1998) Cancer Res. , vol.58 , pp. 3611-3619
    • Cheng, A.1    Balczon, R.2    Zuo, Z.3    Koons, J.S.4    Walsh, A.H.5    Honkanen, R.E.6
  • 11
    • 0033170853 scopus 로고    scopus 로고
    • Cloning and expression of a murine histone deacetylase 3 (mHdac3) cDNA and mapping to a region of conserved synteny between murine chromosome 18 and human chromosome 5
    • Dangond, F., Foerznler, D., Weremowicz, S., Morton, C.C., Beier, D.R., and Gullans, S.R. 1999. Cloning and expression of a murine histone deacetylase 3 (mHdac3) cDNA and mapping to a region of conserved synteny between murine chromosome 18 and human chromosome 5. Mol. Cell. Biol. Res. Commun. 2: 91-96.
    • (1999) Mol. Cell. Biol. Res. Commun. , vol.2 , pp. 91-96
    • Dangond, F.1    Foerznler, D.2    Weremowicz, S.3    Morton, C.C.4    Beier, D.R.5    Gullans, S.R.6
  • 12
    • 0037220731 scopus 로고    scopus 로고
    • The inv(16) fusion protein associates with corepressors via a smooth muscle myosin heavy-chain domain
    • Durst, K.L., Lutterbach, B., Kummalue, T., Friedman, A.D., and Hiebert, S.W. 2003. The inv(16) fusion protein associates with corepressors via a smooth muscle myosin heavy-chain domain. Mol. Cell. Biol. 23: 607-619.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 607-619
    • Durst, K.L.1    Lutterbach, B.2    Kummalue, T.3    Friedman, A.D.4    Hiebert, S.W.5
  • 14
    • 0033988813 scopus 로고    scopus 로고
    • DNA methyltransferase Dnmt1 associates with histone deacetylase activity
    • Fuks, F., Burgers, W.A., Brehm, A., Hughes-Davies, L., and Kouzarides, T. 2000. DNA methyltransferase Dnmt1 associates with histone deacetylase activity. Nat. Genet. 24: 88-91.
    • (2000) Nat. Genet. , vol.24 , pp. 88-91
    • Fuks, F.1    Burgers, W.A.2    Brehm, A.3    Hughes-Davies, L.4    Kouzarides, T.5
  • 15
    • 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
  • 16
    • 0031723957 scopus 로고    scopus 로고
    • Aberrant recruitment of the nuclear receptor corepressor-histone deacetylase complex by the acute myeloid leukemia fusion partner ETO
    • Gelmetti, V., Zhang, J., Fanelli, M., Minucci, S., Pelicci, P.G., and Lazar, M.A. 1998. Aberrant recruitment of the nuclear receptor corepressor-histone deacetylase complex by the acute myeloid leukemia fusion partner ETO. Mol. Cell. Biol. 18: 7185-7191.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7185-7191
    • Gelmetti, V.1    Zhang, J.2    Fanelli, M.3    Minucci, S.4    Pelicci, P.G.5    Lazar, M.A.6
  • 19
    • 0034192756 scopus 로고    scopus 로고
    • A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness
    • Guenther, M.G., Lane, W.S., Fischle, W., Verdin, E., Lazar, M.A., and Shiekhallar, R. 2000. A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness. Genes & Dev. 14: 1048-1057.
    • (2000) Genes & Dev. , vol.14 , pp. 1048-1057
    • Guenther, M.G.1    Lane, W.S.2    Fischle, W.3    Verdin, E.4    Lazar, M.A.5    Shiekhallar, R.6
  • 20
    • 0035724413 scopus 로고    scopus 로고
    • The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3
    • Guenther, M.G., Barak, O., and Lazar, M.A. 2001. The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3. Mol. Cell. Biol. 21: 6091-6101.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6091-6101
    • Guenther, M.G.1    Barak, O.2    Lazar, M.A.3
  • 21
    • 0037115711 scopus 로고    scopus 로고
    • Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex
    • Guenther, M.G., Yu, J., Kao, G.D., Yen, T.J., and Lazar, M.A. 2002. Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex. Genes & Dev. 16: 3130-3135.
    • (2002) Genes & Dev. , vol.16 , pp. 3130-3135
    • Guenther, M.G.1    Yu, J.2    Kao, G.D.3    Yen, T.J.4    Lazar, M.A.5
  • 22
    • 0034307660 scopus 로고    scopus 로고
    • Recruitment of the nuclear receptor corepressor N-CoR by the TEL moiety of the childhood leukemia-associated TEL-AML1 oncoprotein
    • Guidez, F., Petrie, K., Ford, A.M., Lu, H., Bennett, C.A., MacGregor, A., Hannemann, J., Ito, Y., Ghysdael, J., Greaves, M., et al. 2000. Recruitment of the nuclear receptor corepressor N-CoR by the TEL moiety of the childhood leukemia-associated TEL-AML1 oncoprotein. Blood 96: 2557-2561.
    • (2000) Blood , vol.96 , pp. 2557-2561
    • Guidez, F.1    Petrie, K.2    Ford, A.M.3    Lu, H.4    Bennett, C.A.5    MacGregor, A.6    Hannemann, J.7    Ito, Y.8    Ghysdael, J.9    Greaves, M.10
  • 23
    • 0032563347 scopus 로고    scopus 로고
    • Purification of protein phosphatase 4 catalytic subunit: Inhibition by the antitumour drug fostriecin and other tumour suppressors and promoters
    • Hastie, C.J. and Cohen, P.T. 1998. Purification of protein phosphatase 4 catalytic subunit: Inhibition by the antitumour drug fostriecin and other tumour suppressors and promoters. FEBS Lett. 431: 357-361.
    • (1998) FEBS Lett. , vol.431 , pp. 357-361
    • Hastie, C.J.1    Cohen, P.T.2
  • 24
    • 0034192404 scopus 로고    scopus 로고
    • A novel 50 kDa protein forms complexes with protein phosphatase 4 and is located at centrosomal microtubule organizing centres
    • Hastie, C.J., Carnegie, G.K., Morrice, N., and Cohen, P.T. 2000. A novel 50 kDa protein forms complexes with protein phosphatase 4 and is located at centrosomal microtubule organizing centres. Biochem. J. 347: 845-855.
    • (2000) Biochem. J. , vol.347 , pp. 845-855
    • Hastie, C.J.1    Carnegie, G.K.2    Morrice, N.3    Cohen, P.T.4
  • 25
    • 0031799965 scopus 로고    scopus 로고
    • Protein phosphatase 4 is an essential enzyme required for organisation of microtubules at centrosomes in Drosophila embryos
    • Helps, N.R., Brewis, N.D., Lineruth, K., Davis, T., Kaiser, K., and Cohen, P.T. 1998. Protein phosphatase 4 is an essential enzyme required for organisation of microtubules at centrosomes in Drosophila embryos. J. Cell Sci. 111: 1331-1340.
    • (1998) J. Cell Sci. , vol.111 , pp. 1331-1340
    • Helps, N.R.1    Brewis, N.D.2    Lineruth, K.3    Davis, T.4    Kaiser, K.5    Cohen, P.T.6
  • 27
    • 0031572314 scopus 로고    scopus 로고
    • Genomic organization of the human PP4 gene encoding a serine/threonine protein phosphatase (PP4) suggests a common ancestry with PP2A
    • Huang, X., Cheng, A., and Honkanen, R.E. 1997. Genomic organization of the human PP4 gene encoding a serine/threonine protein phosphatase (PP4) suggests a common ancestry with PP2A. Genomics 44: 336-343.
    • (1997) Genomics , vol.44 , pp. 336-343
    • Huang, X.1    Cheng, A.2    Honkanen, R.E.3
  • 28
    • 0042592941 scopus 로고    scopus 로고
    • The N-CoR/histonc deacetylase 3 complex is required for repression by thyroid hormone receptor
    • Ishizuka, T. and Lazar, M.A. 2003. The N-CoR/histonc deacetylase 3 complex is required for repression by thyroid hormone receptor. Mol. Cell. Biol. 23: 5122-5131.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5122-5131
    • Ishizuka, T.1    Lazar, M.A.2
  • 29
    • 0037084392 scopus 로고    scopus 로고
    • Biological roles and mechanistic actions of co-repressor complexes
    • Jepsen, K. and Rosenfeld, M.G. 2002. Biological roles and mechanistic actions of co-repressor complexes. J. Cell Sci. 115:689-698.
    • (2002) J. Cell Sci. , vol.115 , pp. 689-698
    • Jepsen, K.1    Rosenfeld, M.G.2
  • 30
    • 0032500851 scopus 로고    scopus 로고
    • Molecular cloning of Drosophila melanogaster cDNAs that encode a novel histone deacetylase dHDAC3
    • Johnson, C.A., Barlow, A.L., and Turner, B.M. 1998. Molecular cloning of Drosophila melanogaster cDNAs that encode a novel histone deacetylase dHDAC3. Gene 221: 127-134.
    • (1998) Gene , vol.221 , pp. 127-134
    • Johnson, C.A.1    Barlow, A.L.2    Turner, B.M.3
  • 31
    • 0035895909 scopus 로고    scopus 로고
    • Deacetylase activity associates with topoisomerase II and is necessary for etoposide-induced apoptosis
    • Johnson, C.A., Padget, K., Austin, C.A., and Turner, B.M. 2001. Deacetylase activity associates with topoisomerase II and is necessary for etoposide-induced apoptosis. J. Biol. Chem. 276: 4539-4542.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4539-4542
    • Johnson, C.A.1    Padget, K.2    Austin, C.A.3    Turner, B.M.4
  • 32
    • 0034617261 scopus 로고    scopus 로고
    • Histone deacetylases specifically down-regulate p53-dependent gene activation
    • Juan, L.J., Shia, W.J., Chen, M.H., Yang, W.M., Seto, E., Lin, Y.S., and Wu, C.W. 2000. Histone deacetylases specifically down-regulate p53-dependent gene activation. J. Biol. Chem. 275: 20436-20443.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20436-20443
    • Juan, L.J.1    Shia, W.J.2    Chen, M.H.3    Yang, W.M.4    Seto, E.5    Lin, Y.S.6    Wu, C.W.7
  • 33
    • 0036906832 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: From target to clinical trials
    • Kelly, W.K., O'Connor, O.A., and Marks, P.A. 2002. Histone deacetylase inhibitors: From target to clinical trials. Expert Opin. Investig. Drugs 11: 1695-1713.
    • (2002) Expert Opin. Investig. Drugs , vol.11 , pp. 1695-1713
    • Kelly, W.K.1    O'Connor, O.A.2    Marks, P.A.3
  • 34
    • 0033605130 scopus 로고    scopus 로고
    • Purification and identification of a novel subunit of protein serine/threonine phosphatase 4
    • Kloeker, S. and Wadzinski, B.E. 1999. Purification and identification of a novel subunit of protein serine/threonine phosphatase 4. J. Biol Chem. 274: 5339-5347.
    • (1999) J. Biol Chem. , vol.274 , pp. 5339-5347
    • Kloeker, S.1    Wadzinski, B.E.2
  • 35
    • 0030714161 scopus 로고    scopus 로고
    • Carboxymethylation of nuclear protein serine/threonine phosphatase X
    • Kloeker, S., Bryant, J.C., Strack, S., Colbran, R.J., and Wadzinski, B.E. 1997. Carboxymethylation of nuclear protein serine/threonine phosphatase X. Biochem. J. 327: 481-486.
    • (1997) Biochem. J. , vol.327 , pp. 481-486
    • Kloeker, S.1    Bryant, J.C.2    Strack, S.3    Colbran, R.J.4    Wadzinski, B.E.5
  • 36
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression
    • Laherty, C.D., Yang, W.M., Sun, J.M., Davie, J.R., Seto, E., and Eisenman, R.N. 1997. Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell 89: 349-356.
    • (1997) Cell , vol.89 , pp. 349-356
    • Laherty, C.D.1    Yang, W.M.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5    Eisenman, R.N.6
  • 38
    • 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
  • 39
    • 0242439348 scopus 로고    scopus 로고
    • Regulating histone acetyltransferases and deacetylases
    • Legube, G. and Trouche, D. 2003. Regulating histone acetyltransferases and deacetylases. EMBO Rep. 4: 944-947.
    • (2003) EMBO Rep. , vol.4 , pp. 944-947
    • Legube, G.1    Trouche, D.2
  • 41
    • 0034663815 scopus 로고    scopus 로고
    • Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3
    • Li, J., Wang, J., Nawaz, Z., Liu, J.M., Qin, J., and Wong, J. 2000. Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3. EMBO J. 19: 4342-4350.
    • (2000) EMBO J. , vol.19 , pp. 4342-4350
    • Li, J.1    Wang, J.2    Nawaz, Z.3    Liu, J.M.4    Qin, J.5    Wong, J.6
  • 42
    • 0141793860 scopus 로고    scopus 로고
    • Identification of histone deacetylase-3 domains that interact with the orphan nuclear receptor TR2
    • Li, G., Franco, P.J., and Wei, L.N. 2003. Identification of histone deacetylase-3 domains that interact with the orphan nuclear receptor TR2. Biochem. Biophys. Res. Commun. 310: 384-390.
    • (2003) Biochem. Biophys. Res. Commun. , vol.310 , pp. 384-390
    • Li, G.1    Franco, P.J.2    Wei, L.N.3
  • 43
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • Lin, R.J., Nagy, L., Inoue, S., Shao, W., Miller Jr., W.H., and Evans, R.M. 1998. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 391: 811-814.
    • (1998) Nature , vol.391 , pp. 811-814
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3    Shao, W.4    Miller Jr., W.H.5    Evans, R.M.6
  • 44
    • 0032433854 scopus 로고    scopus 로고
    • lin-35 and lin-53, two genes that antagonize a C. elegans Ras pathway, encode proteins similar to Rb and its binding protein RbAp48
    • Lu, X. and Horvitz, H.R. 1998. lin-35 and lin-53, two genes that antagonize a C. elegans Ras pathway, encode proteins similar to Rb and its binding protein RbAp48. Cell 95: 981-991.
    • (1998) Cell , vol.95 , pp. 981-991
    • Lu, X.1    Horvitz, H.R.2
  • 45
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo, J., Su, F., Chen, D., Shiloh, A., and Gu, W. 2000. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature 408: 377-381.
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 46
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • Luo, J., Nikolaev, A.Y., Imai, S., Chen, D., Su, F., Shiloh, A., Guarente, L., and Gu, W. 2001. Negative control of p53 by Sir2α promotes cell survival under stress. Cell 107: 137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 53
    • 8744219552 scopus 로고    scopus 로고
    • Protein Phosphatase 4 interacts with and down-regulates insulin receptor substrate 4 following tumor necrosis factor-α stimulation
    • Mihindukulasuriya, K.A., Zhou, G., Qin, J., and Tan, T.H. 2004. Protein Phosphatase 4 interacts with and down-regulates insulin receptor substrate 4 following tumor necrosis factor-α stimulation. J. Biol. Chem. 279: 46588-46594.
    • (2004) J. Biol. Chem. , vol.279 , pp. 46588-46594
    • Mihindukulasuriya, K.A.1    Zhou, G.2    Qin, J.3    Tan, T.H.4
  • 55
    • 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
  • 56
    • 0033919595 scopus 로고    scopus 로고
    • DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsivc promoters
    • Robertson, K.D., Ait-Si-Ali, S., Yokochi, T., Wade, P.A., Jones, P.L., and Wolffe, A.P. 2000. DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsivc promoters. Nat. Genet. 25: 338-342.
    • (2000) Nat. Genet. , vol.25 , pp. 338-342
    • Robertson, K.D.1    Ait-Si-Ali, S.2    Yokochi, T.3    Wade, P.A.4    Jones, P.L.5    Wolffe, A.P.6
  • 57
    • 0033945861 scopus 로고    scopus 로고
    • DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci
    • Rountree, M.R., Bachman, K.E., and Baylin, S.B. 2000. DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. Nat. Genet. 25: 269-277.
    • (2000) Nat. Genet. , vol.25 , pp. 269-277
    • Rountree, M.R.1    Bachman, K.E.2    Baylin, S.B.3
  • 58
    • 13844252820 scopus 로고    scopus 로고
    • Regulation of histone deacetylase activities
    • Sengupta, N. and Seto, E. 2004. Regulation of histone deacetylase activities. J. Cell Biochem. 93: 57-67.
    • (2004) J. Cell Biochem. , vol.93 , pp. 57-67
    • Sengupta, N.1    Seto, E.2
  • 59
    • 0032053770 scopus 로고    scopus 로고
    • A CBP/p300 homolog specifies multiple differentiation pathways in Caenorhabditis elegans
    • Shi, Y. and Mello, C. 1998. A CBP/p300 homolog specifies multiple differentiation pathways in Caenorhabditis elegans. Genes & Dev. 12: 943-955.
    • (1998) Genes & Dev. , vol.12 , pp. 943-955
    • Shi, Y.1    Mello, C.2
  • 62
    • 0036538022 scopus 로고    scopus 로고
    • Protein phosphatase 4 is required for centrosome maturation in mitosis and sperm meiosis in C. elegans
    • Sumiyoshi, E., Sugimoto, A., and Yamamoto, M. 2002. Protein phosphatase 4 is required for centrosome maturation in mitosis and sperm meiosis in C. elegans. J. Cell Sci. 115: 1403-1410.
    • (2002) J. Cell Sci. , vol.115 , pp. 1403-1410
    • Sumiyoshi, E.1    Sugimoto, A.2    Yamamoto, M.3
  • 63
    • 0034717022 scopus 로고    scopus 로고
    • N-terminal region, C-terminal region, nuclear export signal, and deacetylation activity of histone deacetylase-3 are essential for the viability of the DT40 chicken B cell line
    • Takami, Y. and Nakayama, T. 2000. N-terminal region, C-terminal region, nuclear export signal, and deacetylation activity of histone deacetylase-3 are essential for the viability of the DT40 chicken B cell line. J. Biol. Chem. 275: 16191-16201.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16191-16201
    • Takami, Y.1    Nakayama, T.2
  • 64
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C.A., and Schreiber, S.L. 1996. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272: 408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 66
    • 0032578762 scopus 로고    scopus 로고
    • Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex
    • Tong, J.K., Hassig, C.A., Schnitzler, G.R., Kingston, R.E., and Schreiber, S.L. 1998. Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. Nature 395: 917-921.
    • (1998) Nature , vol.395 , pp. 917-921
    • Tong, J.K.1    Hassig, C.A.2    Schnitzler, G.R.3    Kingston, R.E.4    Schreiber, S.L.5
  • 67
    • 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
  • 68
    • 0033757588 scopus 로고    scopus 로고
    • Histone deacetylase interacts directly with DNA topoisomerase II
    • Tsai, S.C., Valkov, N., Yang, W.M., Gump, J., Sullivan, D., and Seto, E. 2000. Histone deacetylase interacts directly with DNA topoisomerase II. Nat. Genet. 26: 349-353.
    • (2000) Nat. Genet. , vol.26 , pp. 349-353
    • Tsai, S.C.1    Valkov, N.2    Yang, W.M.3    Gump, J.4    Sullivan, D.5    Seto, E.6
  • 69
    • 0036789944 scopus 로고    scopus 로고
    • Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PlASxbeta
    • Tussic-Luna, M.L, Bayarsaihan, D., Seto, E., Ruddle, F.H., and Roy, A.L. 2002. Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PlASxbeta. Proc. Natl. Acad. Sci. 99: 12807-12812.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 12807-12812
    • Tussic-Luna, M.L.1    Bayarsaihan, D.2    Seto, E.3    Ruddle, F.H.4    Roy, A.L.5
  • 70
    • 0034704078 scopus 로고    scopus 로고
    • A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1
    • Underbill, C., Qutob, M.S., Yee, S.P., and Torchia, J. 2000. A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1. J. Biol. Chem. 275: 40463-40470.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40463-40470
    • Underbill, C.1    Qutob, M.S.2    Yee, S.P.3    Torchia, J.4
  • 71
    • 0034254668 scopus 로고    scopus 로고
    • Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-erbA yields a chromatin infrastructure-dependent transcriptional repression pathway
    • Urnov, F.D., Yee, J., Sachs, L., Collingwood, T.N., Bauer, A., Beug, H., Shi, Y.B., and Wolffe, A.P. 2000. Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-erbA yields a chromatin infrastructure-dependent transcriptional repression pathway. EMBO J. 19: 4074-4090.
    • (2000) EMBO J. , vol.19 , pp. 4074-4090
    • Urnov, F.D.1    Yee, J.2    Sachs, L.3    Collingwood, T.N.4    Bauer, A.5    Beug, H.6    Shi, Y.B.7    Wolffe, A.P.8
  • 74
    • 0032474826 scopus 로고    scopus 로고
    • A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase
    • Wade, P.A., Jones, P.L., Vermaak, D., and Wolffe, A.P. 1998. A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase. Curr. Biol. 8: 843-846.
    • (1998) Curr. Biol. , vol.8 , pp. 843-846
    • Wade, P.A.1    Jones, P.L.2    Vermaak, D.3    Wolffe, A.P.4
  • 75
    • 0030720062 scopus 로고    scopus 로고
    • Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A
    • Walsh, A.H., Cheng, A., and Honkanen, R.E. 1997. Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A. FEBS Lett. 416: 230-234.
    • (1997) FEBS Lett. , vol.416 , pp. 230-234
    • Walsh, A.H.1    Cheng, A.2    Honkanen, R.E.3
  • 76
    • 0041813250 scopus 로고    scopus 로고
    • JNK phosphorylation relieves HDAC3-dependent suppression of the transcriptional activity of c-Jun
    • Weiss, C., Schneider, S., Wagner, E.F., Zhang, X., Seto, E., and Bohmann, D. 2003. JNK phosphorylation relieves HDAC3-dependent suppression of the transcriptional activity of c-Jun. EMBO J. 22: 3686-3695.
    • (2003) EMBO J. , vol.22 , pp. 3686-3695
    • Weiss, C.1    Schneider, S.2    Wagner, E.F.3    Zhang, X.4    Seto, E.5    Bohmann, D.6
  • 78
    • 0037449784 scopus 로고    scopus 로고
    • Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I
    • Wen, Y.D., Cress, W.D., Roy, A.L., and Seto, E. 2003. Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I. J. Biol. Chem. 278: 1841-1847.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1841-1847
    • Wen, Y.D.1    Cress, W.D.2    Roy, A.L.3    Seto, E.4
  • 79
    • 0037382681 scopus 로고    scopus 로고
    • Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression
    • Yang, X.J. and Seto, E. 2003. Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression. Curr. Opin. Genet. Dev. 13: 143-153.
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 143-153
    • Yang, X.J.1    Seto, E.2
  • 80
    • 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., and Seto, E. 1996. Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. Proc. Natl. Acad. Sci. 93: 12845-12850.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 12845-12850
    • Yang, W.M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 81
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family
    • Yang, W.M., Yao, Y.L., Sun, J.M., Davie, J.R., and Seto, E. 1997. Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J. Biol. Chem. 272: 28001-28007.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28001-28007
    • Yang, W.M.1    Yao, Y.L.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5
  • 83
    • 2942702021 scopus 로고    scopus 로고
    • Suppression of MEK/ERK signaling pathway enhances cisplatin-induced NF-κB activation by protein phosphatase 4-mediated NF-κB p65 Thr dephosphorylation
    • Yeh, P.Y., Yeh, K.H., Chuang, S.E., Song, Y.C., and Cheng, A.L. 2004. Suppression of MEK/ERK signaling pathway enhances cisplatin-induced NF-κB activation by protein phosphatase 4-mediated NF-κB p65 Thr dephosphorylation. J. Kiol. Chem. 279: 26143-26148.
    • (2004) J. Kiol. Chem. , vol.279 , pp. 26143-26148
    • Yeh, P.Y.1    Yeh, K.H.2    Chuang, S.E.3    Song, Y.C.4    Cheng, A.L.5
  • 84
    • 0344405718 scopus 로고    scopus 로고
    • Purification and functional characterization of the human N-CoR complex: The roles of HDAC3, TBL1 and TBLR1
    • Yoon, H.G., Chan, D.W., Huang, Z.Q., Li, J., Fondell, J.D., Qui, J., and Wong, J. 2003. Purification and functional characterization of the human N-CoR complex: The roles of HDAC3, TBL1 and TBLR1. EMBO J. 22: 1336-1346.
    • (2003) EMBO J. , vol.22 , pp. 1336-1346
    • Yoon, H.G.1    Chan, D.W.2    Huang, Z.Q.3    Li, J.4    Fondell, J.D.5    Qui, J.6    Wong, J.7
  • 85
    • 0032538293 scopus 로고    scopus 로고
    • The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities
    • Zhang, Y., LeRoy, G., Seelig, H.P., Lane, W.S., and Reinberg, D. 1998. The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell 95: 279-289.
    • (1998) Cell , vol.95 , pp. 279-289
    • Zhang, Y.1    LeRoy, G.2    Seelig, H.P.3    Lane, W.S.4    Reinberg, D.5
  • 86
    • 0036211850 scopus 로고    scopus 로고
    • The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2
    • Zhang, J., Kalkum, M., Chait, B.T., and Roeder, R.G. 2002. The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2. Mol. Cell 9: 611-623.
    • (2002) Mol. Cell , vol.9 , pp. 611-623
    • Zhang, J.1    Kalkum, M.2    Chait, B.T.3    Roeder, R.G.4
  • 87
    • 2942594784 scopus 로고    scopus 로고
    • Activation of the growth-differentiation factor 11 gene by the histone deacetylase (HDAC) inhibitor trichostatin A and repression by HDAC3
    • Zhang, X., Wharton, W., Yuan, Z., Tsai, S.C., Olashaw, N., and Seto, E. 2004. Activation of the growth-differentiation factor 11 gene by the histone deacetylase (HDAC) inhibitor trichostatin A and repression by HDAC3. Mol. Cell. Biol. 24: 5106-5118.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5106-5118
    • Zhang, X.1    Wharton, W.2    Yuan, Z.3    Tsai, S.C.4    Olashaw, N.5    Seto, E.6
  • 89
    • 10344227738 scopus 로고    scopus 로고
    • Protein phosphatase 4 is a positive regulator of hematopoietic progenitor kinase 1
    • Zhou, G., Boomer, J.S., and Tan, T.H. 2004. Protein phosphatase 4 is a positive regulator of hematopoietic progenitor kinase 1. J. Biol. Chem. 279: 49551-49561.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49551-49561
    • Zhou, G.1    Boomer, J.S.2    Tan, T.H.3


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