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Volumn 422, Issue 6933, 2003, Pages 730-734

Sequence-specific recruitment of transcriptional co-repressor Cabin1 by myocyte enhancer factor-2

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; DNA; HYDROPHOBICITY; MOLECULES; NEUROLOGY;

EID: 0242417468     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01555     Document Type: Article
Times cited : (97)

References (30)
  • 1
    • 0033595816 scopus 로고    scopus 로고
    • 2+-induced release of the transcription factor MEF 2
    • 2+-induced release of the transcription factor MEF2. Science 286, 790-793 (1999).
    • (1999) Science , vol.286 , pp. 790-793
    • Youn, H.D.1    Sun, L.2    Prywes, R.3    Liu, J.O.4
  • 2
    • 0033595764 scopus 로고    scopus 로고
    • Neuronal activity-dependent cell survival mediated by transcription factor MEF 2
    • Mao, Z., Bonni, A., Xia, F., Nadal-Vicens, M. & Greenberg, M. E. Neuronal activity-dependent cell survival mediated by transcription factor MEF2. Science 286, 785-790 (1999).
    • (1999) Science , vol.286 , pp. 785-790
    • Mao, Z.1    Bonni, A.2    Xia, F.3    Nadal-Vicens, M.4    Greenberg, M.E.5
  • 3
    • 0032437107 scopus 로고    scopus 로고
    • Transcriptional control of muscle development by myocyte enhancer factor-2 (MEF2) proteins
    • Black, B. L. & Olson, E. N. Transcriptional control of muscle development by myocyte enhancer factor-2 (MEF2) proteins. Annu. Rev. Cell Dev. Biol. 14, 167-196 (1998).
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 167-196
    • Black, B.L.1    Olson, E.N.2
  • 4
    • 0036165434 scopus 로고    scopus 로고
    • MEF2: A calcium-dependent regulator of cell division, differentiation and death
    • McKinsey, T. A., Zhang, C. L. & Olson, E. N. MEF2: a calcium-dependent regulator of cell division, differentiation and death. Trends Biochem. Sci. 27, 40-47 (2002).
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 40-47
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 5
    • 0034698113 scopus 로고    scopus 로고
    • Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4
    • Youn, H. D., Grozinger, C. M. & Liu, J. O. Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4. J. Biol. Chem. 275, 22563-22567 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 22563-22567
    • Youn, H.D.1    Grozinger, C.M.2    Liu, J.O.3
  • 6
    • 0037162697 scopus 로고    scopus 로고
    • Class II histone deacetylases act as signal-reponsive repressors of cardiac hypertrophy
    • Zhang, C. L. et al. Class II histone deacetylases act as signal-reponsive repressors of cardiac hypertrophy. Cell 110, 479-488 (2002).
    • (2002) Cell , vol.110 , pp. 479-488
    • Zhang, C.L.1
  • 7
    • 0033681541 scopus 로고    scopus 로고
    • Cabin I represses MEF2-dependent Nur 77 expression and T cell apoptosis by controlling association of histone deacetylases and acetylases with MEF2
    • Youn, H. D. & Liu, J. O. Cabin I represses MEF2-dependent Nur77 expression and T cell apoptosis by controlling association of histone deacetylases and acetylases with MEF2. Immunity 13, 85-94 (2000).
    • (2000) Immunity , vol.13 , pp. 85-94
    • Youn, H.D.1    Liu, J.O.2
  • 8
    • 0034597816 scopus 로고    scopus 로고
    • Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation
    • McKinsey, T. A., Zhang, C. L., Lu, J. & Olson, E. N. Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation. Nature 408, 106-111 (2000).
    • (2000) Nature , vol.408 , pp. 106-111
    • McKinsey, T.A.1    Zhang, C.L.2    Lu, J.3    Olson, E.N.4
  • 9
    • 0033568492 scopus 로고    scopus 로고
    • MEF-2 function is modified by a novel co-repressor, MITR
    • Sparrow, D. B. et al. MEF-2 function is modified by a novel co-repressor, MITR. EMBO J. 18, 5085-5098 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5085-5098
    • Sparrow, D.B.1
  • 10
    • 0033568028 scopus 로고    scopus 로고
    • HDAC 4 deacetylase associates with and represses the MEF2 transcription factor
    • Miska, E. A. et al. HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J. 18, 5099-5107 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5099-5107
    • Miska, E.A.1
  • 11
    • 0032101282 scopus 로고    scopus 로고
    • Cabin 1, a negative regulator for calcineurin signaling in T lymphocytes
    • Sun, L. et al. Cabin 1, a negative regulator for calcineurin signaling in T lymphocytes. Immunity 8, 703-711 (1998).
    • (1998) Immunity , vol.8 , pp. 703-711
    • Sun, L.1
  • 13
    • 0028842908 scopus 로고
    • Regulation of the Nur77 orphan steroid receptor in activation-induced apoptosis
    • Woronicz, J. D. et al. Regulation of the Nur77 orphan steroid receptor in activation-induced apoptosis. Mol. Cell. Biol. 15, 6364-6376 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6364-6376
    • Woronicz, J.D.1
  • 14
    • 0034708333 scopus 로고    scopus 로고
    • Crystal structure of MEF2A core bound to DNA at 1.5 Å resolution
    • Santelli, E. & Richmond, T. J. Crystal structure of MEF2A core bound to DNA at 1.5 Å resolution. J. Mol. Biol. 297, 437-449 (2000).
    • (2000) J. Mol. Biol. , vol.297 , pp. 437-449
    • Santelli, E.1    Richmond, T.J.2
  • 15
    • 0034213458 scopus 로고    scopus 로고
    • Solution structure of the MEF2A-DNA complex: Structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors
    • Huang, K. et al. Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors. EMBO J. 19, 2615-2628 (2000).
    • (2000) EMBO J. , vol.19 , pp. 2615-2628
    • Huang, K.1
  • 16
    • 0032509980 scopus 로고    scopus 로고
    • Crystal structure of the yeast MATα2/MCM1/DNA ternary complex
    • Tan, S. & Richmond, T. J. Crystal structure of the yeast MATα2/MCM1/DNA ternary complex. Nature 391, 660-666 (1998).
    • (1998) Nature , vol.391 , pp. 660-666
    • Tan, S.1    Richmond, T.J.2
  • 17
    • 0035875907 scopus 로고    scopus 로고
    • The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex
    • Hassler, M. & Richmond, T. J. The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex. EMBO J. 26, 3018-3028 (2001).
    • (2001) EMBO J. , vol.26 , pp. 3018-3028
    • Hassler, M.1    Richmond, T.J.2
  • 18
    • 0029102041 scopus 로고
    • Structure of serum response factor core bound to DNA
    • Pellegrini, L., Tan, S. & Richmond, T. J. Structure of serum response factor core bound to DNA. Nature 376, 490-498 (1995).
    • (1995) Nature , vol.376 , pp. 490-498
    • Pellegrini, L.1    Tan, S.2    Richmond, T.J.3
  • 19
    • 0029994419 scopus 로고    scopus 로고
    • Mutational analysis of the DNA binding, dimerization, and transcriptional activation domains of MEF 2C
    • Molkentin, J. D., Black, B. L., Martin, J. F. & Olson, E. N. Mutational analysis of the DNA binding, dimerization, and transcriptional activation domains of MEF2C. Mol. Cell. Biol. 16, 2627-2636 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2627-2636
    • Molkentin, J.D.1    Black, B.L.2    Martin, J.F.3    Olson, E.N.4
  • 20
    • 0029590104 scopus 로고
    • Cooperative activation of muscle gene expression by MEF 2 and myogenic bHLH proteins
    • Molkentin, J. D., Black, B. L., Martin, J. F. & Olson, E. N. Cooperative activation of muscle gene expression by MEF2 and myogenic bHLH proteins. Cell 83, 1125-1136 (1995).
    • (1995) Cell , vol.83 , pp. 1125-1136
    • Molkentin, J.D.1    Black, B.L.2    Martin, J.F.3    Olson, E.N.4
  • 21
    • 0023176346 scopus 로고
    • Structure of the human class 1 histocompatibility antigen, HLA-A 2
    • Bjorkman, P. J. et al. Structure of the human class 1 histocompatibility antigen, HLA-A2. Nature 329, 506-512 (1987).
    • (1987) Nature , vol.329 , pp. 506-512
    • Bjorkman, P.J.1
  • 22
    • 0034685893 scopus 로고    scopus 로고
    • mHDA1/HDAC 5 histone deacetylase interacts with and represses MEF2A transcriptional activity
    • Lemercier, C. et al. mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity. J. Biol. Chem. 275, 15594-15599 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 15594-15599
    • Lemercier, C.1
  • 23
    • 0034635987 scopus 로고    scopus 로고
    • Signal-dependent activation of the MEF 2 transcription factor by dissociation from histone deacetylases
    • Lu, J., McKinsey, T. A., Nicol, R. L. & Olson, E. N. Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases. Proc. Natl Acad. Sci. USA 97, 4070-4075 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4070-4075
    • Lu, J.1    McKinsey, T.A.2    Nicol, R.L.3    Olson, E.N.4
  • 24
    • 0033635242 scopus 로고    scopus 로고
    • Regulation of skeletal myogenesis by association of the MEF 2 transcription factor with class II histone deacetylases
    • Lu, J., McKinsey, T. A., Zhang, C. L. & Olson, E. N. Regulation of skeletal myogenesis by association of the MEF2 transcription factor with class II histone deacetylases. Mol. Cell 6, 233-244 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 233-244
    • Lu, J.1    McKinsey, T.A.2    Zhang, C.L.3    Olson, E.N.4
  • 25
    • 0031045835 scopus 로고    scopus 로고
    • Molecular mechanisms of myogenic coactivation by p300: Direct interaction with the activation domain of MyoD and with the MADS box of MEF 2C
    • Sartorelli, V., Huang, J., Hamamori, Y. & Kedes, L. Molecular mechanisms of myogenic coactivation by p300: direct interaction with the activation domain of MyoD and with the MADS box of MEF2C. Mol. Cell. Biol. 17, 1010-1026 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1010-1026
    • Sartorelli, V.1    Huang, J.2    Hamamori, Y.3    Kedes, L.4
  • 26
    • 0002452464 scopus 로고
    • eds Sawyer, L., Isaacs, N. & Burley, S. SERC Daresbury Laboratory, Daresbury, UK
    • Otwinowski, Z. in Proceedings of the CCP4 Study Weekend (eds Sawyer, L., Isaacs, N. & Burley, S.) 56-62 (SERC Daresbury Laboratory, Daresbury, UK, 1993).
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR System: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR System: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 29
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50, 760-776 (1994).
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-776


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