메뉴 건너뛰기




Volumn 141, Issue 5, 2007, Pages 719-727

Co-repressor SMRT and class II histone deacetylases promote Bach2 nuclear retention and formation of nuclear foci that are responsible for local transcriptional repression

Author keywords

Bach2; HDAC4; Nuclear domain; SMRT; Transcription repression

Indexed keywords

BACH2 PROTEIN; HISTONE DEACETYLASE 4; LEUCINE ZIPPER PROTEIN; PROTEIN; SILENCING MEDIATOR OF RETINOID AND THYROID RECEPTOR PROTEIN; UNCLASSIFIED DRUG;

EID: 34347359786     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvm073     Document Type: Article
Times cited : (15)

References (43)
  • 1
    • 0037128933 scopus 로고    scopus 로고
    • Cyclin-dependent kinases govern formation and maintenance of the nucleolus
    • Sirri, V., Hernandez-Verdun, D., and Roussel, P. (2002) Cyclin-dependent kinases govern formation and maintenance of the nucleolus. J. Cell. Biol. 156, 969-981
    • (2002) J. Cell. Biol , vol.156 , pp. 969-981
    • Sirri, V.1    Hernandez-Verdun, D.2    Roussel, P.3
  • 2
    • 0041669439 scopus 로고    scopus 로고
    • Nuclear speckles: A model for nuclear organelles
    • Lamond, A.I. and Spector, D.L. (2003) Nuclear speckles: a model for nuclear organelles. Nat. Rev. Mol. Cell Biol. 4, 605-612
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 605-612
    • Lamond, A.I.1    Spector, D.L.2
  • 3
    • 0345169047 scopus 로고    scopus 로고
    • The centennial of the Cajal body
    • Gall, J.G. (2003) The centennial of the Cajal body. Nat. Rev. Mol. Cell Biol. 4, 975-980
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 975-980
    • Gall, J.G.1
  • 4
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • Dyck, J.A., Maul, G.G., Miller, W.H.Jr, Chen, J.D., Kakizuka, A., and Evans, R.M. (1994) A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76, 333-343
    • (1994) Cell , vol.76 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller Jr, W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 5
    • 0034685764 scopus 로고    scopus 로고
    • Oxidative stress abolishes leptomycin B-sensitive nuclear export of transcription repressor Bach2 that counteracts activation of Maf recognition element
    • Hoshino, H., Kobayashi, A., Yoshida, M., Kudo, N., Oyake, T., Motohashi, H., Hayashi, N., Yamamoto, M., and Igarashi, K. (2000) Oxidative stress abolishes leptomycin B-sensitive nuclear export of transcription repressor Bach2 that counteracts activation of Maf recognition element. J. Biol. Chem. 275, 15370-15376
    • (2000) J. Biol. Chem , vol.275 , pp. 15370-15376
    • Hoshino, H.1    Kobayashi, A.2    Yoshida, M.3    Kudo, N.4    Oyake, T.5    Motohashi, H.6    Hayashi, N.7    Yamamoto, M.8    Igarashi, K.9
  • 6
    • 0029805130 scopus 로고    scopus 로고
    • Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site
    • Oyake, T., Itoh, K., Motohashi, H., Hayashi, N., Hoshino, H., Nishizawa, M., Yamamoto, M., and Igarashi, K. (1996) Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site. Mol. Cell Biol. 16, 6083-6095
    • (1996) Mol. Cell Biol , vol.16 , pp. 6083-6095
    • Oyake, T.1    Itoh, K.2    Motohashi, H.3    Hayashi, N.4    Hoshino, H.5    Nishizawa, M.6    Yamamoto, M.7    Igarashi, K.8
  • 9
    • 0037036377 scopus 로고    scopus 로고
    • Activation of Maf/AP-1 repressor Bach2 by oxidative stress promotes apoptosis and its interaction with promyelocyte leukemia nuclear bodies
    • Muto, A., Tashiro, S., Tsuchiya, H., Kume, A., Kanno, M., Ito, E., Yamamoto, M., and Igarashi, K. (2002) Activation of Maf/AP-1 repressor Bach2 by oxidative stress promotes apoptosis and its interaction with promyelocyte leukemia nuclear bodies. J. Biol. Chem. 277, 20724-20733
    • (2002) J. Biol. Chem , vol.277 , pp. 20724-20733
    • Muto, A.1    Tashiro, S.2    Tsuchiya, H.3    Kume, A.4    Kanno, M.5    Ito, E.6    Yamamoto, M.7    Igarashi, K.8
  • 12
    • 0032189224 scopus 로고    scopus 로고
    • Identification of Bach2 as a B-cell-specific partner for small maf proteins that negatively regulate the immunoglobulin heavy chain gene 3′ enhancer
    • Muto, A., Hoshino, H., Madisen, L., Yanai, N., Obinata, M., Karasuyama, H., Hayashi, N., Nakauchi, H., Yamamoto, M., Groudine, M., and Igarashi, K. (1998) Identification of Bach2 as a B-cell-specific partner for small maf proteins that negatively regulate the immunoglobulin heavy chain gene 3′ enhancer. EMBO J. 17, 5734-5743
    • (1998) EMBO J , vol.17 , pp. 5734-5743
    • Muto, A.1    Hoshino, H.2    Madisen, L.3    Yanai, N.4    Obinata, M.5    Karasuyama, H.6    Hayashi, N.7    Nakauchi, H.8    Yamamoto, M.9    Groudine, M.10    Igarashi, K.11
  • 14
    • 0035968274 scopus 로고    scopus 로고
    • SMRTE inhibits MEF2C transcriptional activation by targeting HDAC4 and 5 to nuclear domains
    • Wu, X., Li, H., Park, E.J., and Chen, J.D. (2001) SMRTE inhibits MEF2C transcriptional activation by targeting HDAC4 and 5 to nuclear domains. J. Biol. Chem. 276, 24177-24185
    • (2001) J. Biol. Chem , vol.276 , pp. 24177-24185
    • Wu, X.1    Li, H.2    Park, E.J.3    Chen, J.D.4
  • 15
  • 16
    • 0028118492 scopus 로고
    • Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins
    • Igarashi, K., Kataoka, K., Itoh, K., Hayashi, N., Nishizawa, M., and Yamamoto, M. (1994) Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins. Nature 367, 568-572
    • (1994) Nature , vol.367 , pp. 568-572
    • Igarashi, K.1    Kataoka, K.2    Itoh, K.3    Hayashi, N.4    Nishizawa, M.5    Yamamoto, M.6
  • 17
    • 0029080316 scopus 로고
    • Conditional expression of the ubiquitous transcription factor MafK induces erythroleukemia cell differentiation
    • Igarashi, K., Itoh, K., Hayashi, N., Nishizawa, M., and Yamamoto, M. (1995) Conditional expression of the ubiquitous transcription factor MafK induces erythroleukemia cell differentiation. Proc. Natl. Acad. Sci. USA 92, 7445-7449
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7445-7449
    • Igarashi, K.1    Itoh, K.2    Hayashi, N.3    Nishizawa, M.4    Yamamoto, M.5
  • 18
    • 0035964317 scopus 로고    scopus 로고
    • Activation of beta-major globin gene transcription is associated with recruitment of NF-E2 to the beta-globin LCR and gene promoter
    • Sawado, T., Igarashi, K., and Groudine, M. (2001) Activation of beta-major globin gene transcription is associated with recruitment of NF-E2 to the beta-globin LCR and gene promoter. Proc. Natl. Acad. Sci. USA 98, 10226-10231
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10226-10231
    • Sawado, T.1    Igarashi, K.2    Groudine, M.3
  • 20
    • 0034649504 scopus 로고    scopus 로고
    • Dhordain, P., Albagli, O., Honore, N., Guidez, F., Lantoine, D., Schmid, M., The, H.D., Zelent, A., and Koken, M.H. (2000) Colocalization and heteromerization between the two human oncogene POZ/zinc finger proteins, LAZ3 (BCL6) and PLZF. Oncogene 19, 6240-6250
    • Dhordain, P., Albagli, O., Honore, N., Guidez, F., Lantoine, D., Schmid, M., The, H.D., Zelent, A., and Koken, M.H. (2000) Colocalization and heteromerization between the two human oncogene POZ/zinc finger proteins, LAZ3 (BCL6) and PLZF. Oncogene 19, 6240-6250
  • 24
    • 9244253152 scopus 로고    scopus 로고
    • Dong, S., Zhu, J., Reid, A., Strutt, P., Guidez, F., Zhong, H.J., Wang, Z.Y., Licht, J., Waxman, S., Chomienne, C., Chen, Z., Zelent, A., and Chen, S.J. (1996) Amino-terminal protein-protein interaction motif (POZ-domain) is responsible for activities of the promyelocytic leukemia zinc finger-retinoic acid receptor-alpha fusion protein. Proc. Natl. Acad. Sci. USA 93, 3624-3629
    • Dong, S., Zhu, J., Reid, A., Strutt, P., Guidez, F., Zhong, H.J., Wang, Z.Y., Licht, J., Waxman, S., Chomienne, C., Chen, Z., Zelent, A., and Chen, S.J. (1996) Amino-terminal protein-protein interaction motif (POZ-domain) is responsible for activities of the promyelocytic leukemia zinc finger-retinoic acid receptor-alpha fusion protein. Proc. Natl. Acad. Sci. USA 93, 3624-3629
  • 26
    • 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
  • 27
    • 0033616676 scopus 로고    scopus 로고
    • SMRTe, a silencing mediator for retinoid and thyroid hormone receptors-extended isoform that is more related to the nuclear receptor corepressor
    • Park, E.J., Schroen, D.J., Yang, M., Li, H., Li, L., and Chen, J.D. (1999) SMRTe, a silencing mediator for retinoid and thyroid hormone receptors-extended isoform that is more related to the nuclear receptor corepressor. Proc. Natl. Acad. Sci. USA 96, 3519-3524
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3519-3524
    • Park, E.J.1    Schroen, D.J.2    Yang, M.3    Li, H.4    Li, L.5    Chen, J.D.6
  • 28
    • 0032531688 scopus 로고    scopus 로고
    • The LAZ3(BCL-6) oncoprotein recruits a SMRT/mSIN3A/histone deacetylase containing complex to mediate transcriptional repression
    • Dhordain, P., Lin, R.J., Quief, S., Lantoine, D., Kerckaert, J.P., Evans, R.M., and Albagli, O. (1998) The LAZ3(BCL-6) oncoprotein recruits a SMRT/mSIN3A/histone deacetylase containing complex to mediate transcriptional repression. Nucleic Acids Res. 26, 4645-4651
    • (1998) Nucleic Acids Res , vol.26 , pp. 4645-4651
    • Dhordain, P.1    Lin, R.J.2    Quief, S.3    Lantoine, D.4    Kerckaert, J.P.5    Evans, R.M.6    Albagli, O.7
  • 29
    • 0034898560 scopus 로고    scopus 로고
    • Histone deacetylase 4 possesses intrinsic nuclear import and export signals
    • Wang, A.H. and Yang, X.J. (2001) Histone deacetylase 4 possesses intrinsic nuclear import and export signals. Mol. Cell. Biol. 21, 5992-6005
    • (2001) Mol. Cell. Biol , vol.21 , pp. 5992-6005
    • Wang, A.H.1    Yang, X.J.2
  • 30
    • 0035861739 scopus 로고    scopus 로고
    • Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7
    • Kao, H.Y., Verdel, A., Tsai, C.C., Simon, C., Juguilon, H., and Khochbin, S. (2001) Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7. J. Biol. Chem. 276, 47496-47507
    • (2001) J. Biol. Chem , vol.276 , pp. 47496-47507
    • Kao, H.Y.1    Verdel, A.2    Tsai, C.C.3    Simon, C.4    Juguilon, H.5    Khochbin, S.6
  • 31
    • 0035724044 scopus 로고    scopus 로고
    • Identification of a signal-responsive nuclear export sequence in class II histone deacetylases
    • McKinsey, T.A., Zhang, C.L., and Olson, E.N. (2001) Identification of a signal-responsive nuclear export sequence in class II histone deacetylases. Mol. Cell Biol. 21, 6312-6321
    • (2001) Mol. Cell Biol , vol.21 , pp. 6312-6321
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 32
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
    • Kao, H.Y., Downes, M., Ordentlich, P., and Evans, R.M. (2000) Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev. 14, 55-66
    • (2000) Genes Dev , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 33
    • 0033957792 scopus 로고    scopus 로고
    • Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway
    • Huang, E.Y., Zhang, J., Miska, E.A., Guenther, M.G., Kouzarides, T., and Lazar, M.A. (2000) Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev. 14, 45-54
    • (2000) Genes Dev , vol.14 , pp. 45-54
    • Huang, E.Y.1    Zhang, J.2    Miska, E.A.3    Guenther, M.G.4    Kouzarides, T.5    Lazar, M.A.6
  • 34
    • 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. USA 97, 7835-7840
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7835-7840
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 35
    • 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
  • 38
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • Boisvert, F.M., Hendzel, M.J., and Bazett-Jones, D.P. (2000) Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J. Cell Biol. 148, 283-292
    • (2000) J. Cell Biol , vol.148 , pp. 283-292
    • Boisvert, F.M.1    Hendzel, M.J.2    Bazett-Jones, D.P.3
  • 39
    • 0035316574 scopus 로고    scopus 로고
    • Chromosome territories, nuclear architecture and gene regulation in mammalian cells
    • Cremer, T. and Cremer, C. (2001) Chromosome territories, nuclear architecture and gene regulation in mammalian cells. Nat. Rev. Genet. 2, 292-301
    • (2001) Nat. Rev. Genet , vol.2 , pp. 292-301
    • Cremer, T.1    Cremer, C.2
  • 40
    • 2142650203 scopus 로고    scopus 로고
    • Nuclear substructure and dynamics
    • Lamond, A.I. and Sleeman, J.E. (2003) Nuclear substructure and dynamics. Curr. Biol. 13, R825-R828
    • (2003) Curr. Biol , vol.13
    • Lamond, A.I.1    Sleeman, J.E.2
  • 41
    • 1242271330 scopus 로고    scopus 로고
    • Integration of Epstein-Barr virus into chromosome 6q15 of Burkitt lymphoma cell line (Raji) induces loss of BACH2 expression
    • Takakuwa, T., Luo, W.J., Ham, M.F., Sakane-Ishikawa, F., Wada, N., and Aozasa, K. (2004) Integration of Epstein-Barr virus into chromosome 6q15 of Burkitt lymphoma cell line (Raji) induces loss of BACH2 expression. Am. J. Pathol. 164, 967-974
    • (2004) Am. J. Pathol , vol.164 , pp. 967-974
    • Takakuwa, T.1    Luo, W.J.2    Ham, M.F.3    Sakane-Ishikawa, F.4    Wada, N.5    Aozasa, K.6
  • 43
    • 0142183455 scopus 로고    scopus 로고
    • B-cell-specific transcription factor BACH2 modifies the cytotoxic effects of anticancer drugs
    • Kamio, T., Toki, T., Kanezaki, R., Sasaki, S., Tandai, S., Terui, K., Ikebe, D., Igarashi, K., and Ito, E. (2003) B-cell-specific transcription factor BACH2 modifies the cytotoxic effects of anticancer drugs. Blood 102, 3317-3322
    • (2003) Blood , vol.102 , pp. 3317-3322
    • Kamio, T.1    Toki, T.2    Kanezaki, R.3    Sasaki, S.4    Tandai, S.5    Terui, K.6    Ikebe, D.7    Igarashi, K.8    Ito, E.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.