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Volumn 29, Issue 2, 2004, Pages 155-165

Myocyte enhancer factor-2 transcription factors in neuronal differentiation and survival

Author keywords

Apoptosis; Brain; Calcium signaling; Development; MADS box; Muscle; Neuron; Protein kinases

Indexed keywords

CALCIUM; MYOCYTE ENHANCER FACTOR 2; PROTEIN KINASE; TRANSCRIPTION FACTOR; DNA BINDING PROTEIN; MYOCYTE SPECIFIC ENHANCER BINDING FACTOR 2; MYOCYTE-SPECIFIC ENHANCER-BINDING FACTOR 2; MYOGENIC FACTOR;

EID: 3142705929     PISSN: 08937648     EISSN: None     Source Type: Journal    
DOI: 10.1385/MN:29:2:155     Document Type: Review
Times cited : (72)

References (64)
  • 1
    • 0026782992 scopus 로고
    • Human myocyte-specific enhancer factor 2 comprises a group of tissue-restricted MADS box transcription factors
    • Yu Y.T., Breitbart R.E., Smoot L.B., Lee Y., Mahdavi V., Nadal-Ginard B. (1992) Human myocyte-specific enhancer factor 2 comprises a group of tissue-restricted MADS box transcription factors. Genes Dev. 6, 1783-1798.
    • (1992) Genes Dev. , vol.6 , pp. 1783-1798
    • Yu, Y.T.1    Breitbart, R.E.2    Smoot, L.B.3    Lee, Y.4    Mahdavi, V.5    Nadal-Ginard, B.6
  • 2
    • 0032705145 scopus 로고    scopus 로고
    • MEF2: A transcriptional target for signaling pathways controlling skeletal muscle growth and differentiation
    • Naya F.S., Olson E. (1999) MEF2: a transcriptional target for signaling pathways controlling skeletal muscle growth and differentiation. Curr. Opin. Cell Biol. 11, 683-688.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 683-688
    • Naya, F.S.1    Olson, E.2
  • 3
    • 0028934434 scopus 로고
    • The MADS-box family of transcription factors
    • Shore P., Sharrocks A.D. (1995) The MADS-box family of transcription factors. Eur. J. Biochem. 229, 1-13.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 1-13
    • Shore, P.1    Sharrocks, A.D.2
  • 4
    • 0027270775 scopus 로고
    • A fourth human MEF2 transcription factor, hMEF2D, is an early marker of the myogenic lineage
    • Breitbart R.E., Liang C.S., Smoot L.B., Laheru D.A., Mahdavi V., Nadal-Ginard B. (1993) A fourth human MEF2 transcription factor, hMEF2D, is an early marker of the myogenic lineage. Development 118, 1095-1106.
    • (1993) Development , vol.118 , pp. 1095-1106
    • Breitbart, R.E.1    Liang, C.S.2    Smoot, L.B.3    Laheru, D.A.4    Mahdavi, V.5    Nadal-Ginard, B.6
  • 5
    • 0027409049 scopus 로고
    • MEF2C, a MADS/MEF2-family transcription factor expressed in a laminar distribution in cerebral cortex
    • Leifer D., Krainc D., Yu Y.T., et al. (1993) MEF2C, a MADS/MEF2-family transcription factor expressed in a laminar distribution in cerebral cortex. Proc. Natl. Acad. Sci. USA 90, 1546-1550.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1546-1550
    • Leifer, D.1    Krainc, D.2    Yu, Y.T.3
  • 6
    • 0027468651 scopus 로고
    • hMEF2C gene encodes skeletal muscle-and brain-specific transcription factors
    • McDermott J.C., Cardoso M.C., Yu Y.T., et al. (1993) hMEF2C gene encodes skeletal muscle-and brain-specific transcription factors. Mol. Cell. Biol. 13, 2564-2577.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2564-2577
    • McDermott, J.C.1    Cardoso, M.C.2    Yu, Y.T.3
  • 8
    • 0036793505 scopus 로고    scopus 로고
    • Use of genomics tools to isolate key ripening genes and analyse fruit maturation in tomato
    • Moore S., Vrebalov J., Payton P., Giovannoni J. (2002) Use of genomics tools to isolate key ripening genes and analyse fruit maturation in tomato. J. Exp. Bot. 53, 2023-2030.
    • (2002) J. Exp. Bot. , vol.53 , pp. 2023-2030
    • Moore, S.1    Vrebalov, J.2    Payton, P.3    Giovannoni, J.4
  • 9
    • 0035289981 scopus 로고    scopus 로고
    • Function and evolution of the plant MADS-box gene family
    • Ng M., Yanofsky M.F. (2001) Function and evolution of the plant MADS-box gene family. Nat. Rev. Genet. 2, 186-195.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 186-195
    • Ng, M.1    Yanofsky, M.F.2
  • 10
    • 0030560884 scopus 로고    scopus 로고
    • Skeletal muscle determination and differentiation: Story of a core regulatory network and its context
    • Yun K., Wold B. (1996) Skeletal muscle determination and differentiation: story of a core regulatory network and its context. Curr. Opin. Cell Biol. 8, 877-889.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 877-889
    • Yun, K.1    Wold, B.2
  • 11
    • 0032437107 scopus 로고    scopus 로고
    • Transcriptional control of muscle development by myocyte enhancer factor-2 (MEF2) proteins
    • Black B.L., Olson E.N. (1998) Transcriptional control of muscle development by myocyte enhancer factor-2 (MEF2) proteins. Annu. Rev. Cell. Dev. Biol. 14, 167-196.
    • (1998) Annu. Rev. Cell. Dev. Biol. , vol.14 , pp. 167-196
    • Black, B.L.1    Olson, E.N.2
  • 12
    • 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. (2002) MEF2: a calcium-dependent regulator of cell division, differentiation and death. Trends Biochem. Sci. 27, 40-47.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 40-47
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 13
    • 0029895310 scopus 로고    scopus 로고
    • MEF2B is a potent transactivator expressed in early myogenic lineages
    • Molkentin J.D., Firulli A.B., Black B.L., et al. (1996) MEF2B is a potent transactivator expressed in early myogenic lineages. Mol. Cell. Biol. 16, 3814-3824.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3814-3824
    • Molkentin, J.D.1    Firulli, A.B.2    Black, B.L.3
  • 14
    • 0029841389 scopus 로고    scopus 로고
    • Combinatorial control of muscle development by basic helix-loop-helix and MADS-box transcription factors
    • Molkentin J.D., Olson E.N. (1996) Combinatorial control of muscle development by basic helix-loop-helix and MADS-box transcription factors. Proc. Natl. Acad. Sci. USA 93, 9366-9373.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9366-9373
    • Molkentin, J.D.1    Olson, E.N.2
  • 15
    • 0029773893 scopus 로고    scopus 로고
    • MEF2 protein expression, DNA binding specificity and complex composition, and transcriptional activity in muscle and non-muscle cells
    • Ornatsky O.I., McDermott J.C. (1996) MEF2 protein expression, DNA binding specificity and complex composition, and transcriptional activity in muscle and non-muscle cells. J. Biol. Chem. 271, 24927-24933.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24927-24933
    • Ornatsky, O.I.1    McDermott, J.C.2
  • 16
    • 0033804899 scopus 로고    scopus 로고
    • Regulation of muscle regulatory factors by DNA-binding, interacting proteins, and post-transcriptional modifications
    • Puri P.L., Sartorelli V. (2000) Regulation of muscle regulatory factors by DNA-binding, interacting proteins, and post-transcriptional modifications. J. Cell. Physiol. 185, 155-173.
    • (2000) J. Cell. Physiol. , vol.185 , pp. 155-173
    • Puri, P.L.1    Sartorelli, V.2
  • 17
    • 0034162714 scopus 로고    scopus 로고
    • Induction of terminal differentiation by constitutive activation of p38 MAP kinase in human rhabdomyosarcoma cells
    • Puri P.L., Wu Z., Zhang P., et al. (2000) Induction of terminal differentiation by constitutive activation of p38 MAP kinase in human rhabdomyosarcoma cells. Genes Dev. 14, 574-584.
    • (2000) Genes Dev. , vol.14 , pp. 574-584
    • Puri, P.L.1    Wu, Z.2    Zhang, P.3
  • 18
    • 0030911475 scopus 로고    scopus 로고
    • Control of mouse cardiac morphogenesis and myogenesis by transcription factor MEF2C
    • Lin Q., Schwarz J., Bucana C., Olson E.N. (1997) Control of mouse cardiac morphogenesis and myogenesis by transcription factor MEF2C. Science 276, 1404-1407.
    • (1997) Science , vol.276 , pp. 1404-1407
    • Lin, Q.1    Schwarz, J.2    Bucana, C.3    Olson, E.N.4
  • 19
    • 0028933143 scopus 로고
    • Drosophila MEF2, a transcription factor that is essential for myogenesis
    • Bour B.A., O'Brien M.A., Lockwood W.L., et al. (1995) Drosophila MEF2, a transcription factor that is essential for myogenesis. Genes Dev. 9, 730-741.
    • (1995) Genes Dev. , vol.9 , pp. 730-741
    • Bour, B.A.1    O'Brien, M.A.2    Lockwood, W.L.3
  • 20
    • 0030273675 scopus 로고    scopus 로고
    • Presynaptic development at the Drosophila neuromuscular junction: Assembly and localization of presynaptic active zones
    • Prokop A., Landgraf M., Rushton E., Broadie K., Bate M. (1996) Presynaptic development at the Drosophila neuromuscular junction: assembly and localization of presynaptic active zones. Neuron 17, 617-626.
    • (1996) Neuron , vol.17 , pp. 617-626
    • Prokop, A.1    Landgraf, M.2    Rushton, E.3    Broadie, K.4    Bate, M.5
  • 21
    • 0033592696 scopus 로고    scopus 로고
    • MEF2 is upregulated during cardiac hypertrophy and is required for normal post-natal growth of the myocardium
    • Kolodziejczyk S.M., Wang L., Balazsi K., DeRepentigny Y., Kothary R., Megeney L.A. (1999) MEF2 is upregulated during cardiac hypertrophy and is required for normal post-natal growth of the myocardium. Curr. Biol. 9, 1203-1206.
    • (1999) Curr. Biol. , vol.9 , pp. 1203-1206
    • Kolodziejczyk, S.M.1    Wang, L.2    Balazsi, K.3    DeRepentigny, Y.4    Kothary, R.5    Megeney, L.A.6
  • 22
    • 19244386873 scopus 로고    scopus 로고
    • CaM kinase signaling induces cardiac hypertrophy and activates the MEF2 transcription factor in vivo
    • Passier R., Zeng H., Frey N., et al. (2000) CaM kinase signaling induces cardiac hypertrophy and activates the MEF2 transcription factor in vivo. J. Clin. Invest. 105, 1395-1406.
    • (2000) J. Clin. Invest. , vol.105 , pp. 1395-1406
    • Passier, R.1    Zeng, H.2    Frey, N.3
  • 23
    • 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., 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
  • 24
    • 0033595816 scopus 로고    scopus 로고
    • Apoptosis of T cells mediated by Ca2+-induced release of the transcription factor MEF2
    • Youn H.D., Sun L., Prywes R., Liu J.O. (1999) Apoptosis of T cells mediated by Ca2+-induced release of the transcription factor MEF2. Science 286, 790-793.
    • (1999) Science , vol.286 , pp. 790-793
    • Youn, H.D.1    Sun, L.2    Prywes, R.3    Liu, J.O.4
  • 25
    • 0034663805 scopus 로고    scopus 로고
    • Integration of calcineurin and MEF2 signals by the coactivator p300 during T-cell apoptosis
    • Youn H.D., Chatila T.A., Liu J.O. (2000) Integration of calcineurin and MEF2 signals by the coactivator p300 during T-cell apoptosis. Embo J. 19, 4323-4331.
    • (2000) Embo J. , vol.19 , pp. 4323-4331
    • Youn, H.D.1    Chatila, T.A.2    Liu, J.O.3
  • 26
    • 0028150878 scopus 로고
    • Myocyte-specific enhancer binding factor 2C expression in human brain development
    • Leifer D., Golden J., Kowall N.W. (1994) Myocyte-specific enhancer binding factor 2C expression in human brain development. Neuroscience 63, 1067-1079.
    • (1994) Neuroscience , vol.63 , pp. 1067-1079
    • Leifer, D.1    Golden, J.2    Kowall, N.W.3
  • 27
    • 0029085629 scopus 로고
    • Expression of mef2 genes in the mouse central nervous system suggests a role in neuronal maturation
    • Lyons G.E., Micales B.K., Schwarz J., Martin J.F., Olson E.N. (1995) Expression of mef2 genes in the mouse central nervous system suggests a role in neuronal maturation. J. Neurosci. 15, 5727-5738.
    • (1995) J. Neurosci. , vol.15 , pp. 5727-5738
    • Lyons, G.E.1    Micales, B.K.2    Schwarz, J.3    Martin, J.F.4    Olson, E.N.5
  • 28
    • 0028821749 scopus 로고
    • Expression of a MADS box gene, MEF2D, in neurons of the mouse central nervous system: Implication of its binary function in myogenic and neurogenic cell lineages
    • Ikeshima H., Imai S., Shimoda K., Hata J., Takano T. (1995) Expression of a MADS box gene, MEF2D, in neurons of the mouse central nervous system: implication of its binary function in myogenic and neurogenic cell lineages. Neurosci. Lett. 200, 117-120.
    • (1995) Neurosci. Lett. , vol.200 , pp. 117-120
    • Ikeshima, H.1    Imai, S.2    Shimoda, K.3    Hata, J.4    Takano, T.5
  • 29
    • 0032697805 scopus 로고    scopus 로고
    • Calcineurin enhances MEF2 DNA binding activity in calcium-dependent survival of cerebellar granule neurons
    • Mao Z., Wiedmann M. (1999) Calcineurin enhances MEF2 DNA binding activity in calcium-dependent survival of cerebellar granule neurons. J. Biol. Chem. 274, 31102-31107.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31102-31107
    • Mao, Z.1    Wiedmann, M.2
  • 30
    • 0030477812 scopus 로고    scopus 로고
    • The expression of MEF2 genes is implicated in CNS neuronal differentiation
    • Lin X., Shah S., Bulleit R.F. (1996) The expression of MEF2 genes is implicated in CNS neuronal differentiation. Brain Res. Mol. Brain Res. 42, 307-316.
    • (1996) Brain Res. Mol. Brain Res. , vol.42 , pp. 307-316
    • Lin, X.1    Shah, S.2    Bulleit, R.F.3
  • 31
    • 0033595764 scopus 로고    scopus 로고
    • Neuronal activity-dependent cell survival mediated by transcription factor MEF2
    • Mao Z., Bonni A., Xia F., Nadal-Vicens M., Greenberg M.E. (1999) Neuronal activity-dependent cell survival mediated by transcription factor MEF2. Science 286, 785-790.
    • (1999) Science , vol.286 , pp. 785-790
    • Mao, Z.1    Bonni, A.2    Xia, F.3    Nadal-Vicens, M.4    Greenberg, M.E.5
  • 32
    • 0035448912 scopus 로고    scopus 로고
    • Myocyte enhancer factor 2A and 2D undergo phosphorylation and caspase-mediated degradation during apoptosis of rat cerebellar granule neurons
    • Li M., Linseman D.A., Allen M.P., et al. (2001) Myocyte enhancer factor 2A and 2D undergo phosphorylation and caspase-mediated degradation during apoptosis of rat cerebellar granule neurons. J. Neurosci. 21, 6544-6552.
    • (2001) J. Neurosci. , vol.21 , pp. 6544-6552
    • Li, M.1    Linseman, D.A.2    Allen, M.P.3
  • 33
    • 0037195903 scopus 로고    scopus 로고
    • RNA interference reveals a requirement for myocyte enhancer factor 2A in activity-dependent neuronal survival
    • Gaudilliere B., Shi Y., Bonni A. (2002) RNA interference reveals a requirement for myocyte enhancer factor 2A in activity-dependent neuronal survival. J. Biol. Chem. 277, 46442-46446.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46442-46446
    • Gaudilliere, B.1    Shi, Y.2    Bonni, A.3
  • 34
    • 0037133620 scopus 로고    scopus 로고
    • Dominant-interfering forms of MEF2 generated by caspase cleavage contribute to NMDA-induced neuronal apoptosis
    • Okamoto S., Li Z., Ju C., Scholzke M.N., Mathews E., et al. (2002) Dominant-interfering forms of MEF2 generated by caspase cleavage contribute to NMDA-induced neuronal apoptosis. Proc. Natl. Acad. Sci. USA 99, 3974-3979.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3974-3979
    • Okamoto, S.1    Li, Z.2    Ju, C.3    Scholzke, M.N.4    Mathews, E.5
  • 35
    • 0034691218 scopus 로고    scopus 로고
    • Antiapoptotic role of the p38 mitogen-activated protein kinase-myocyte enhancer factor 2 transcription factor pathway during neuronal differentiation
    • Okamoto S., Krainc D., Sherman K., Lipton S.A. (2000) Antiapoptotic role of the p38 mitogen-activated protein kinase-myocyte enhancer factor 2 transcription factor pathway during neuronal differentiation. Proc. Natl. Acad. Sci. USA 97, 7561-7566.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7561-7566
    • Okamoto, S.1    Krainc, D.2    Sherman, K.3    Lipton, S.A.4
  • 36
    • 0034697109 scopus 로고    scopus 로고
    • Myocyte enhancer factor 2C upregulates MASH-1 expression and induces neurogenesis in P19 cells
    • Skerjanc I.S., Wilton S. (2000) Myocyte enhancer factor 2C upregulates MASH-1 expression and induces neurogenesis in P19 cells. FEBS Lett. 472, 53-56.
    • (2000) FEBS Lett. , vol.472 , pp. 53-56
    • Skerjanc, I.S.1    Wilton, S.2
  • 37
    • 0032475857 scopus 로고    scopus 로고
    • Synergistic activation of the N-methyl-D-aspartate receptor subunit 1 promoter by myocyte enhancer factor 2C and Sp1
    • Krainc D., Bai G., Okamoto S., et al. (1998) Synergistic activation of the N-methyl-D-aspartate receptor subunit 1 promoter by myocyte enhancer factor 2C and Sp1. J. Biol. Chem. 273, 26218-26224.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26218-26224
    • Krainc, D.1    Bai, G.2    Okamoto, S.3
  • 38
    • 0037064051 scopus 로고    scopus 로고
    • Adhesion-related kinase repression of gonadotropin-releasing hormone gene expression requires Rac activation of the extracellular signal-regulated kinase pathway
    • Allen M.P., Xu M., Linseman D.A., et al. (2002) Adhesion-related kinase repression of gonadotropin-releasing hormone gene expression requires Rac activation of the extracellular signal-regulated kinase pathway. J. Biol. Chem. 277, 38133-38140.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38133-38140
    • Allen, M.P.1    Xu, M.2    Linseman, D.A.3
  • 39
    • 0030015713 scopus 로고    scopus 로고
    • Phosphorylation of the MADS-Box transcription factor MEF2C enhances its DNA binding activity
    • Molkentin J.D., Li L., Olson E.N. (1996) Phosphorylation of the MADS-Box transcription factor MEF2C enhances its DNA binding activity. J. Biol. Chem. 271, 17199-17204.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17199-17204
    • Molkentin, J.D.1    Li, L.2    Olson, E.N.3
  • 40
    • 0033011595 scopus 로고    scopus 로고
    • Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors
    • Yang S.H., Galanis A., Sharrocks A.D. (1999) Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors. Mol. Cell. Biol. 19, 4028-4038.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4028-4038
    • Yang, S.H.1    Galanis, A.2    Sharrocks, A.D.3
  • 41
    • 0032953307 scopus 로고    scopus 로고
    • Regulation of the MEF2 family of transcription factors by p38
    • Zhao M., New L., Kravchenko V.V., et al. (1999) Regulation of the MEF2 family of transcription factors by p38. Mol. Cell. Biol. 19, 21-30.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 21-30
    • Zhao, M.1    New, L.2    Kravchenko, V.V.3
  • 42
    • 0034067079 scopus 로고    scopus 로고
    • p38 and extracellular signal-regulated kinases regulate the myogenic program at multiple steps
    • Wu Z., Woodring P.J., Bhakta K.S., et al. (2000) p38 and extracellular signal-regulated kinases regulate the myogenic program at multiple steps. Mol. Cell. Biol. 20, 3951-3964.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3951-3964
    • Wu, Z.1    Woodring, P.J.2    Bhakta, K.S.3
  • 43
    • 0033168093 scopus 로고    scopus 로고
    • Post-translational control of the MEF2A transcriptional regulatory protein
    • Ornatsky O.I., Cox D.M., Tangirala P, et al. (1999) Post-translational control of the MEF2A transcriptional regulatory protein. Nucleic Acids Res. 27, 2646-2654.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2646-2654
    • Ornatsky, O.I.1    Cox, D.M.2    Tangirala, P.3
  • 44
    • 0030894683 scopus 로고    scopus 로고
    • Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation
    • Han J., Jiang Y., Li Z., Kravchenko V.V., Ulevitch R.J. (1997) Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation. Nature 386, 296-299.
    • (1997) Nature , vol.386 , pp. 296-299
    • Han, J.1    Jiang, Y.2    Li, Z.3    Kravchenko, V.V.4    Ulevitch, R.J.5
  • 45
    • 0034595213 scopus 로고    scopus 로고
    • MEF2 responds to multiple calcium-regulated signals in the control of skeletal muscle fiber type
    • Wu H., Naya F.J., McKinsey T.A., et al. (2000) MEF2 responds to multiple calcium-regulated signals in the control of skeletal muscle fiber type. Embo J. 19, 1963-1973.
    • (2000) Embo J. , vol.19 , pp. 1963-1973
    • Wu, H.1    Naya, F.J.2    McKinsey, T.A.3
  • 46
    • 0030694387 scopus 로고    scopus 로고
    • BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C
    • Kato Y., Kravchenko V.V., Tapping R.I., Han J., Ulevitch R.J., Lee J.D. (1997) BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C. Embo J. 16, 7054-7066.
    • (1997) Embo J. , vol.16 , pp. 7054-7066
    • Kato, Y.1    Kravchenko, V.V.2    Tapping, R.I.3    Han, J.4    Ulevitch, R.J.5    Lee, J.D.6
  • 47
    • 0032531753 scopus 로고    scopus 로고
    • Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1
    • Yang C.C., Ornatsky O.I., McDermott J.C., Cruz T.F., Prody C.A. (1998) Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1. Nucleic Acids Res. 26, 4771-4777.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4771-4777
    • Yang, C.C.1    Ornatsky, O.I.2    McDermott, J.C.3    Cruz, T.F.4    Prody, C.A.5
  • 48
    • 0034674622 scopus 로고    scopus 로고
    • Big mitogen-activated kinase regulates multiple members of the MEF2 protein family
    • Kato Y., Zhao M., Morikawa A., et al. (2000) Big mitogen-activated kinase regulates multiple members of the MEF2 protein family. J. Biol. Chem. 275, 18534-18540.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18534-18540
    • Kato, Y.1    Zhao, M.2    Morikawa, A.3
  • 49
    • 0032977187 scopus 로고    scopus 로고
    • A network of mitogen-activated protein kinases links G protein-coupled receptors to the c-jun promoter: A role for c-Jun NH2-terminal kinase, p38s, and extracellular signal-regulated kinase 5
    • Marinissen M.J., Chiariello M., Pallante M., Gutkind J.S. (1999) A network of mitogen-activated protein kinases links G protein-coupled receptors to the c-jun promoter: a role for c-Jun NH2-terminal kinase, p38s, and extracellular signal-regulated kinase 5. Mol. Cell. Biol. 19, 4289-4301.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4289-4301
    • Marinissen, M.J.1    Chiariello, M.2    Pallante, M.3    Gutkind, J.S.4
  • 50
    • 0033761543 scopus 로고    scopus 로고
    • ERK5 is a novel type of mitogen-activated protein kinase containing a transcriptional activation domain
    • Kasler H.G., Victoria J., Duramad O., Winoto A. (2000) ERK5 is a novel type of mitogen-activated protein kinase containing a transcriptional activation domain. Mol. Cell. Biol. 20, 8382-8389.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8382-8389
    • Kasler, H.G.1    Victoria, J.2    Duramad, O.3    Winoto, A.4
  • 51
    • 0038491472 scopus 로고    scopus 로고
    • ERK5 activation of MEF2-mediated gene expression plays a critical role in BDNF-promoted survival of developing but not mature cortical neurons
    • Liu L., Cavanaugh J.E., Wang Y., Sakagami H., Mao Z., Xia Z. (2003) ERK5 activation of MEF2-mediated gene expression plays a critical role in BDNF-promoted survival of developing but not mature cortical neurons. Proc. Natl. Acad. Sci. USA 100, 8532-8537.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8532-8537
    • Liu, L.1    Cavanaugh, J.E.2    Wang, Y.3    Sakagami, H.4    Mao, Z.5    Xia, Z.6
  • 52
    • 0041737614 scopus 로고    scopus 로고
    • Characterization of a neurotrophin signaling mechanism that mediates neuron survival in a temporally specific pattern
    • Shalizi A., Lehtinen M., Gaudilliere B., et al. (2003) Characterization of a neurotrophin signaling mechanism that mediates neuron survival in a temporally specific pattern. J. Neurosci. 23, 7326-7336.
    • (2003) J. Neurosci. , vol.23 , pp. 7326-7336
    • Shalizi, A.1    Lehtinen, M.2    Gaudilliere, B.3
  • 53
    • 0037795747 scopus 로고    scopus 로고
    • A myocyte enhancer factor 2D (MEF2D) kinase activated during neuronal apoptosis is a novel target inhibited by lithium
    • Linseman D.A., Cornejo B.J., Le S.S., et al. (2003) A myocyte enhancer factor 2D (MEF2D) kinase activated during neuronal apoptosis is a novel target inhibited by lithium. J. Neurochem. 85, 1488-1499.
    • (2003) J. Neurochem. , vol.85 , pp. 1488-1499
    • Linseman, D.A.1    Cornejo, B.J.2    Le, S.S.3
  • 54
    • 0037431130 scopus 로고    scopus 로고
    • Cdk-5 mediated inhibition of the protective effects of transcription factor MEF2 in neurotoxicity-induced apoptosis
    • Gong X., X. T, Wiedmann M, Wang X, et al. (2003) Cdk-5 mediated inhibition of the protective effects of transcription factor MEF2 in neurotoxicity-induced apoptosis. Neuron 38, 33-46.
    • (2003) Neuron , vol.38 , Issue.1 , pp. 33-46
    • Gong, X.1    Tang, X.2    Wiedmann, M.3    Wang, X.4
  • 55
    • 0034832115 scopus 로고    scopus 로고
    • Cyclin-dependent protein kinase 5 (Cdk5) and the regulation of neurofilament metabolism
    • Grant P., Sharma P., Pant H.C. (2001) Cyclin-dependent protein kinase 5 (Cdk5) and the regulation of neurofilament metabolism. Eur. J. Biochem. 268, 1534-1546.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1534-1546
    • Grant, P.1    Sharma, P.2    Pant, H.C.3
  • 56
    • 0034570480 scopus 로고    scopus 로고
    • Cyclin-dependent kinase-5 (CDK5) and amyotrophic lateral sclerosis
    • Bajaj N.P. (2000) Cyclin-dependent kinase-5 (CDK5) and amyotrophic lateral sclerosis. Amyotroph Lateral Scler Other Motor Neuron Disord. 1, 319-327.
    • (2000) Amyotroph Lateral Scler Other Motor Neuron Disord. , vol.1 , pp. 319-327
    • Bajaj, N.P.1
  • 57
    • 0034831233 scopus 로고    scopus 로고
    • The protein kinase Cdk5. Structural aspects, roles in neurogenesis and involvement in Alzheimer's pathology
    • Maccioni R.B., Otth C., Concha I.I., Munoz J.P. (2001) The protein kinase Cdk5. Structural aspects, roles in neurogenesis and involvement in Alzheimer's pathology. Eur. J. Biochem. 268, 1518-1527.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1518-1527
    • Maccioni, R.B.1    Otth, C.2    Concha, I.I.3    Munoz, J.P.4
  • 58
    • 0034678823 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 (Cdk5) associated with Lewy bodies in diffuse Lewy body disease
    • Takahashi M., Iseki E., Kosaka K. (2000) Cyclin-dependent kinase 5 (Cdk5) associated with Lewy bodies in diffuse Lewy body disease. Brain Res. 862, 253-256.
    • (2000) Brain Res. , vol.862 , pp. 253-256
    • Takahashi, M.1    Iseki, E.2    Kosaka, K.3
  • 59
    • 0033635242 scopus 로고    scopus 로고
    • Regulation of skeletal myogenesis by association of the MEF2 transcription factor with class II histone deacetylases
    • Lu J., McKinsey T.A., Zhang C.L., Olson E.N. (2000) Regulation of skeletal myogenesis by association of the MEF2 transcription factor with class II histone deacetylases. Mol. Cell 6, 233-244.
    • (2000) Mol. Cell , vol.6 , pp. 233-244
    • Lu, J.1    McKinsey, T.A.2    Zhang, C.L.3    Olson, E.N.4
  • 60
    • 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. (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
  • 62
    • 0035912794 scopus 로고    scopus 로고
    • The transcriptional corepressor MITR is a signal-responsive inhibitor of myogenesis
    • Zhang C.L., McKinsey I.A., Olson E.N. (2001) The transcriptional corepressor MITR is a signal-responsive inhibitor of myogenesis. Proc. Natl. Acad. Sci. USA 98, 7354-7359.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7354-7359
    • Zhang, C.L.1    McKinsey, I.A.2    Olson, E.N.3
  • 63
    • 0142135022 scopus 로고    scopus 로고
    • Inactivation of the myocyte enhancer factor-2 repressor histone deacetylase-5 by endogenous Ca(2+)/calmodulin-dependent kinase II promotes depolarization-mediated cerebellar granule neuron survival
    • Linseman P.A., Bartley C.M., Le S.S., et al. (2003). Inactivation of the myocyte enhancer factor-2 repressor histone deacetylase-5 by endogenous Ca(2+)/calmodulin-dependent kinase II promotes depolarization-mediated cerebellar granule neuron survival. J. Biol. Chem. 278, 41472-41481.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41472-41481
    • Linseman, P.A.1    Bartley, C.M.2    Le, S.S.3
  • 64
    • 0037379709 scopus 로고    scopus 로고
    • Neuronal activity-dependent nucleocytoplasmic shuttling of HDAC4 and HDAC5
    • Chawla S., Vanhoutte P., Arnold F.J., Huang C.L., Bading H. (2003) Neuronal activity-dependent nucleocytoplasmic shuttling of HDAC4 and HDAC5. J. Neurochem. 85, 151-159.
    • (2003) J. Neurochem. , vol.85 , pp. 151-159
    • Chawla, S.1    Vanhoutte, P.2    Arnold, F.J.3    Huang, C.L.4    Bading, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.