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Volumn 10, Issue 2, 1999, Pages 205-214

MAP kinase-mediated signalling to nucleosomes and immediate-early gene induction

Author keywords

Acetylation; IE gene induction; MAP kinases; Nucleosomes; Phosphorylation

Indexed keywords

ACYLTRANSFERASE; CALCIUM CALMODULIN ACTIVATED HISTONE 3 ARGININE KINASE; CALCIUM-CALMODULIN-ACTIVATED HISTONE 3 ARGININE KINASE; HIGH MOBILITY GROUP PROTEIN; HISTONE; HISTONE ACETYLTRANSFERASE; IMMEDIATE EARLY PROTEIN; MAP KINASE ACTIVATED KINASE 2; MAP-KINASE-ACTIVATED KINASE 2; PROTEIN C FOS; PROTEIN C JUN; PROTEIN KINASE (CALCIUM,CALMODULIN); PROTEIN SERINE THREONINE KINASE; SACCHAROMYCES CEREVISIAE PROTEIN; SER 6 PHOSPHORYLATED HIGH MOBILITY GROUP 14; SER 6-PHOSPHORYLATED HIGH MOBILITY GROUP 14;

EID: 0033113010     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1999.0302     Document Type: Article
Times cited : (190)

References (77)
  • 2
    • 0030271387 scopus 로고    scopus 로고
    • NF-κ B: Ten years after
    • Baeuerle PA, Baltimore D (1996) NF-κ B: Ten years after. Cell 87:13-20
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 3
    • 4243911949 scopus 로고    scopus 로고
    • Signalling genes from the cell surface
    • Darnell JE (1997) Signalling genes from the cell surface. FASEB J 11:888
    • (1997) FASEB J , vol.11 , pp. 888
    • Darnell, J.E.1
  • 4
    • 0028926263 scopus 로고
    • Parallel signal processing among mammalian MAPKs
    • Cano E, Mahadevan LC (1995) Parallel signal processing among mammalian MAPKs. Trends Biochem Sci 20:117-122
    • (1995) Trends Biochem Sci , vol.20 , pp. 117-122
    • Cano, E.1    Mahadevan, L.C.2
  • 5
    • 0025872683 scopus 로고
    • Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors
    • Mahadevan LC, Willis AC, Barratt MJ (1991) Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors. Cell 65:775-783
    • (1991) Cell , vol.65 , pp. 775-783
    • Mahadevan, L.C.1    Willis, A.C.2    Barratt, M.J.3
  • 6
    • 0028291992 scopus 로고
    • Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction
    • Barratt MJ, Hazzalin CA, Cano E, Mahadevan LC (1994) Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction. Proc Natl Acad Sci USA 91:4781-4785
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4781-4785
    • Barratt, M.J.1    Hazzalin, C.A.2    Cano, E.3    Mahadevan, L.C.4
  • 7
    • 0027941473 scopus 로고
    • A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 in its basic amino-terminal domain in vivo and on isolated mononucleosomes
    • Barratt MJ, Hazzalin CA, Zhelev N, Mahadevan LC (1994) A mitogen-and anisomycin-stimulated kinase phosphorylates HMG-14 in its basic amino-terminal domain in vivo and on isolated mononucleosomes. EMBO J 13:4524-4535
    • (1994) EMBO J , vol.13 , pp. 4524-4535
    • Barratt, M.J.1    Hazzalin, C.A.2    Zhelev, N.3    Mahadevan, L.C.4
  • 8
    • 0030220456 scopus 로고    scopus 로고
    • p38/RK is essential for stress-induced nuclear responses: JNK/SAPKs and c-Jun/ATF-2 phosphorylation are insufficient
    • Hazzalin CA, Cano E, Cuenda A, Barratt MJ, Cohen P, Mahadevan LC (1996) p38/RK is essential for stress-induced nuclear responses: JNK/SAPKs and c-Jun/ATF-2 phosphorylation are insufficient. Curr Biol 6:1028-1031
    • (1996) Curr Biol , vol.6 , pp. 1028-1031
    • Hazzalin, C.A.1    Cano, E.2    Cuenda, A.3    Barratt, M.J.4    Cohen, P.5    Mahadevan, L.C.6
  • 9
    • 0030783156 scopus 로고    scopus 로고
    • The search for physiological substrates of MAP and SAP kinases in mammalian cells
    • Cohen P (1997) The search for physiological substrates of MAP and SAP kinases in mammalian cells. Trends Cell Biol 7:353-361
    • (1997) Trends Cell Biol , vol.7 , pp. 353-361
    • Cohen, P.1
  • 10
    • 0029761702 scopus 로고    scopus 로고
    • Signal-transducing protein phosphorylation cascades mediated by Ras/Rho proteins in the mammalian cell: The potential for multiplex signalling
    • Denhardt DT (1996) Signal-transducing protein phosphorylation cascades mediated by Ras/Rho proteins in the mammalian cell: The potential for multiplex signalling. Biochem J 318:729-747
    • (1996) Biochem J , vol.318 , pp. 729-747
    • Denhardt, D.T.1
  • 12
    • 0032422785 scopus 로고    scopus 로고
    • Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals
    • Whitmarsh AJ, Davis RJ (1998) Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals. Trends Biochem Sci 23:481-485
    • (1998) Trends Biochem Sci , vol.23 , pp. 481-485
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 16
    • 0030660391 scopus 로고    scopus 로고
    • Effects of the inhibition of p38/RK MAP kinase on induction of five fos and jun genes by diverse stimuli
    • Hazzalin CA, Cuenda A, Cano E, Cohen P, Mahadevan LC (1997) Effects of the inhibition of p38/RK MAP kinase on induction of five fos and jun genes by diverse stimuli. Oncogene 15:2321-2331
    • (1997) Oncogene , vol.15 , pp. 2321-2331
    • Hazzalin, C.A.1    Cuenda, A.2    Cano, E.3    Cohen, P.4    Mahadevan, L.C.5
  • 17
    • 0029328342 scopus 로고
    • Transcriptional control by protein phosphorylation - Signal transmission from the cell-surface to the nucleus
    • Karin M, Hunter T (1995) Transcriptional control by protein phosphorylation - signal transmission from the cell-surface to the nucleus. Curr Biol 5:747-757
    • (1995) Curr Biol , vol.5 , pp. 747-757
    • Karin, M.1    Hunter, T.2
  • 18
    • 0029935418 scopus 로고    scopus 로고
    • Regulation of transcription by MAP kinase cascades
    • Treisman R (1996) Regulation of transcription by MAP kinase cascades. Curr Opin Cell Biol 8:205-215
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 205-215
    • Treisman, R.1
  • 19
    • 0028897113 scopus 로고
    • Transcriptional regulation by extracellular signals - Mechanisms and specificity
    • Hill CS, Treisman R (1995) Transcriptional regulation by extracellular signals - mechanisms and specificity. Cell 80:199-211
    • (1995) Cell , vol.80 , pp. 199-211
    • Hill, C.S.1    Treisman, R.2
  • 20
    • 0039498752 scopus 로고
    • Transcription factor and chromatin protein phosphorylation associated with immediate-early gene induction
    • (Clemens MJ, ed) Harwood Academic Publishers
    • Buckle RS, Barratt MJ, Mahadevan LC (1995) Transcription factor and chromatin protein phosphorylation associated with immediate-early gene induction, in Protein Phosphorylation in Cell Growth Regulation (Clemens MJ, ed) pp 135-161. Harwood Academic Publishers
    • (1995) Protein Phosphorylation in Cell Growth Regulation , pp. 135-161
    • Buckle, R.S.1    Barratt, M.J.2    Mahadevan, L.C.3
  • 21
    • 0024362535 scopus 로고
    • Occupation of the c-fos serum response element in vivo by a multi-protein complex is unaltered by growth-factor induction
    • Herrera RE, Shaw PE, Nordheim A (1989) Occupation of the c-fos serum response element in vivo by a multi-protein complex is unaltered by growth-factor induction. Nature 340:68-70
    • (1989) Nature , vol.340 , pp. 68-70
    • Herrera, R.E.1    Shaw, P.E.2    Nordheim, A.3
  • 22
    • 0031896910 scopus 로고    scopus 로고
    • Anisomycin selectively desensitizes signalling components involved in stress kinase activation and fos and jun induction
    • Hazzalin CA, Le Panse R, Cano E, Mahadevan LC (1998) Anisomycin selectively desensitizes signalling components involved in stress kinase activation and fos and jun induction. Mol Cell Biol 18:1844-1854
    • (1998) Mol Cell Biol , vol.18 , pp. 1844-1854
    • Hazzalin, C.A.1    Le Panse, R.2    Cano, E.3    Mahadevan, L.C.4
  • 23
    • 0031882123 scopus 로고    scopus 로고
    • The Elk-1 ETS-domain transcription factor contains a mitogen-activated protein kinase targeting motif
    • Yang SH, Yates PR, Whitmarsh AJ, Davis RJ, Sharrocks AD (1998) The Elk-1 ETS-domain transcription factor contains a mitogen-activated protein kinase targeting motif. Mol Cell Biol 18:710-720
    • (1998) Mol Cell Biol , vol.18 , pp. 710-720
    • Yang, S.H.1    Yates, P.R.2    Whitmarsh, A.J.3    Davis, R.J.4    Sharrocks, A.D.5
  • 24
    • 0029827366 scopus 로고    scopus 로고
    • The p38 and ERK MAP kinase pathways cooperate to activate ternary complex factors and c-fas transcription in response to UV light
    • Price MA, Cruzalegui FH, Treisman R (1996) The p38 and ERK MAP kinase pathways cooperate to activate ternary complex factors and c-fas transcription in response to UV light. EMBO J 15:6552-6563
    • (1996) EMBO J , vol.15 , pp. 6552-6563
    • Price, Ma.1    Cruzalegui, F.H.2    Treisman, R.3
  • 25
    • 0029015774 scopus 로고
    • The Rho-Family GT-Pases RhoA, Rac1, and Cdc42hs regulate transcriptional activation by SRF
    • Hill CS, Wynne J, Treisman R (1995) The Rho-Family GT-Pases RhoA, Rac1, and Cdc42hs regulate transcriptional activation by SRF. Cell 81:1159-1170
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 26
    • 0032549013 scopus 로고    scopus 로고
    • Activation of SRF-regulated chromosomal templates by Rho-family GT-Pases requires a signal that also induces H4 hyperacetylation
    • Alberts AS, Geneste O, Treisman R (1998) Activation of SRF-regulated chromosomal templates by Rho-family GT-Pases requires a signal that also induces H4 hyperacetylation. Cell 92:475-487
    • (1998) Cell , vol.92 , pp. 475-487
    • Alberts, A.S.1    Geneste, O.2    Treisman, R.3
  • 27
    • 0030972807 scopus 로고    scopus 로고
    • Transcriptional regulation by cyclic AMP
    • Montminy M (1997) Transcriptional regulation by cyclic AMP. Ann Rev Biochem 66:807-822
    • (1997) Ann Rev Biochem , vol.66 , pp. 807-822
    • Montminy, M.1
  • 28
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen-and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may itself mediate activation of CREB
    • Deak M, Clifton AD, Lucocq JM, Alessi DR (1998) Mitogen-and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may itself mediate activation of CREB. EMBO J 17:4426-4441
    • (1998) EMBO J , vol.17 , pp. 4426-4441
    • Deak, M.1    Clifton, A.D.2    Lucocq, J.M.3    Alessi, D.R.4
  • 29
    • 0032514734 scopus 로고    scopus 로고
    • Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene
    • DeCesare D, Jacquot S, Hanauer A, Sassone-Corsi P (1998) Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene. Proc Natl Acad Sci USA 95:12202-12207
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12202-12207
    • DeCesare, D.1    Jacquot, S.2    Hanauer, A.3    Sassone-Corsi, P.4
  • 30
    • 0027282295 scopus 로고
    • In-vivo protein-DNA interactions at the c-jun promoter - Preformed complexes mediate the UV response
    • Rozek D, Pfeifer GP (1993) In-vivo protein-DNA interactions at the c-jun promoter - preformed complexes mediate the UV response. Mol Cell Biol 13:5490-5499
    • (1993) Mol Cell Biol , vol.13 , pp. 5490-5499
    • Rozek, D.1    Pfeifer, G.P.2
  • 31
    • 0028914934 scopus 로고
    • In-vivo protein-DNA interactions at the c-jun promoter in quiescent and serum-stimulated fibroblasts
    • Rozek D, Pfeifer GP (1995) In-vivo protein-DNA interactions at the c-jun promoter in quiescent and serum-stimulated fibroblasts. J Cell Biochem 57:479-487
    • (1995) J Cell Biochem , vol.57 , pp. 479-487
    • Rozek, D.1    Pfeifer, G.P.2
  • 33
    • 0025139461 scopus 로고
    • Serum stimulation of the c-fos enhancer induces reversible changes in c-fos chromatin structure
    • Feng JL, Villeponteau B (1990) Serum stimulation of the c-fos enhancer induces reversible changes in c-fos chromatin structure. Mol Cell Biol 10:1126-1133
    • (1990) Mol Cell Biol , vol.10 , pp. 1126-1133
    • Feng, J.L.1    Villeponteau, B.2
  • 34
    • 0026560488 scopus 로고
    • High-resolution analysis of c-fos chromatin accessibility using a novel DNase I-PCR assay
    • Feng J, Villeponteau B (1992) High-resolution analysis of c-fos chromatin accessibility using a novel DNase I-PCR assay. Biochim Biophys Acta 1130:253-258
    • (1992) Biochim Biophys Acta , vol.1130 , pp. 253-258
    • Feng, J.1    Villeponteau, B.2
  • 35
    • 0023395729 scopus 로고
    • Rapid and reversible changes in nucleosome structure accompany the activation, repression, and superinduction of murine fibroblast protooncogenes c-fos and c-myc
    • Chen TA, Allfrey VG (1987) Rapid and reversible changes in nucleosome structure accompany the activation, repression, and superinduction of murine fibroblast protooncogenes c-fos and c-myc. Proc Natl Acad Sci USA 84:5252-5256
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5252-5256
    • Chen, T.A.1    Allfrey, V.G.2
  • 36
    • 0023660740 scopus 로고
    • Affinity chromatographic purification of nucleosomes containing transcriptionally active DNA-sequences
    • Allegra P, Sterner R, Clayton DF, Allfrey VG (1987) Affinity chromatographic purification of nucleosomes containing transcriptionally active DNA-sequences. J Mol Biol 196:379-388
    • (1987) J Mol Biol , vol.196 , pp. 379-388
    • Allegra, P.1    Sterner, R.2    Clayton, D.F.3    Allfrey, V.G.4
  • 38
    • 0028156740 scopus 로고
    • s6k containing a bifurcation to histone H3-HMG-like protein phosphorylation and c-fos-c-jun induction
    • s6k containing a bifurcation to histone H3-HMG-like protein phosphorylation and c-fos-c-jun induction. Mol Cell Biol 14:1066-1074
    • (1994) Mol Cell Biol , vol.14 , pp. 1066-1074
    • Kardalinou, E.1    Zhelev, N.2    Hazzalin, C.A.3    Mahadevan, L.C.4
  • 39
    • 0017853206 scopus 로고
    • Histone phosphorylation and chromatin structure during mitosis in Chinese hamster cells
    • Gurley LR, D'Anna JA, Barham SS, Deaven LL, Tobey RA (1978) Histone phosphorylation and chromatin structure during mitosis in Chinese hamster cells. Eur J Biochem 84:1-15
    • (1978) Eur J Biochem , vol.84 , pp. 1-15
    • Gurley, L.R.1    D'Anna, J.A.2    Barham, S.S.3    Deaven, L.L.4    Tobey, R.A.5
  • 40
    • 0020479077 scopus 로고
    • Phosphorylation of histones 1 and 3 and nonhistone high mobility group 14 by an endogenous kinase in HeLa metaphase chromosomes
    • Paulson JR, Taylor SS (1982) Phosphorylation of histones 1 and 3 and nonhistone high mobility group 14 by an endogenous kinase in HeLa metaphase chromosomes. J Biol Chem 257:6064-6072
    • (1982) J Biol Chem , vol.257 , pp. 6064-6072
    • Paulson, J.R.1    Taylor, S.S.2
  • 41
    • 0030828073 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation
    • Hendzel MJ, Wei Y, Mancini MA, VanHooser A, Ranalli T, Brinkley BR, Bazett-Jones DP, Allis CD (1997) Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation. Chromosoma 106:348-360
    • (1997) Chromosoma , vol.106 , pp. 348-360
    • Hendzel, M.J.1    Wei, Y.2    Mancini, Ma.3    VanHooser, A.4    Ranalli, T.5    Brinkley, B.R.6    Bazett-Jones, D.P.7    Allis, C.D.8
  • 43
    • 0025803095 scopus 로고
    • Cyclic adenosine 3′,5′-monophosphate-dependent phosphorylation of HMG-14 inhibits its interactions with nucleosomes
    • Spaulding SW, Fucile NW, Bofinger DP, Sheflin LG (1991) Cyclic adenosine 3′,5′-monophosphate-dependent phosphorylation of HMG-14 inhibits its interactions with nucleosomes. Mol Endocrinol 5:42-50
    • (1991) Mol Endocrinol , vol.5 , pp. 42-50
    • Spaulding, S.W.1    Fucile, N.W.2    Bofinger, D.P.3    Sheflin, L.G.4
  • 44
    • 0028274720 scopus 로고
    • The footprint of chromosomal proteins HMG-14 and HMG-17 on chromatin subunits
    • Alfonso PJ, Crippa MP, Hayes JJ, Bustin M (1994) The footprint of chromosomal proteins HMG-14 and HMG-17 on chromatin subunits. J Mol Biol 236:189-198
    • (1994) J Mol Biol , vol.236 , pp. 189-198
    • Alfonso, P.J.1    Crippa, M.P.2    Hayes, J.J.3    Bustin, M.4
  • 45
    • 0029126965 scopus 로고
    • Homodimers of chromosomal proteins HMG-14 and HMG-17 in nucleosome cores
    • Postnikov YV, Triechsmann L, Rickers A, Bustin M (1995) Homodimers of chromosomal proteins HMG-14 and HMG-17 in nucleosome cores. J Mol Biol 252:423-432
    • (1995) J Mol Biol , vol.252 , pp. 423-432
    • Postnikov, Y.V.1    Triechsmann, L.2    Rickers, A.3    Bustin, M.4
  • 46
    • 0031565914 scopus 로고    scopus 로고
    • Clusters of nucleosomes containing chromosomal protein HMG-17 in chromatin
    • Postnikov YV, Herrera JE, Hock R, Scheer U, Bustin M (1997) Clusters of nucleosomes containing chromosomal protein HMG-17 in chromatin. J Mol Biol 274:454-465
    • (1997) J Mol Biol , vol.274 , pp. 454-465
    • Postnikov, Y.V.1    Herrera, J.E.2    Hock, R.3    Scheer, U.4    Bustin, M.5
  • 47
    • 0030358586 scopus 로고    scopus 로고
    • High-mobility-group chromosomal proteins: Architectural components that facilitate chromatin function
    • Bustin M, Reeves R (1996) High-mobility-group chromosomal proteins: Architectural components that facilitate chromatin function. Progr Nucl Acid Res Mol Biol 54:35-100
    • (1996) Progr Nucl Acid Res Mol Biol , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 48
    • 0028000720 scopus 로고
    • Stimulation of RNA polymerase II elongation by chromosomal protein HMG-14
    • Ding HF, Rimsky S, Batson SC, Bustin M, Hansen U (1994) Stimulation of RNA polymerase II elongation by chromosomal protein HMG-14. Science 265:796-799
    • (1994) Science , vol.265 , pp. 796-799
    • Ding, H.F.1    Rimsky, S.2    Batson, S.C.3    Bustin, M.4    Hansen, U.5
  • 49
    • 0022649274 scopus 로고
    • Purification and characterization of a protein-kinase from Xenopus eggs highly specific for ribosomal-protein S6
    • Erikson E, Maller JL (1986) Purification and characterization of a protein-kinase from Xenopus eggs highly specific for ribosomal-protein S6. J Biol Chem 261:350-355
    • (1986) J Biol Chem , vol.261 , pp. 350-355
    • Erikson, E.1    Maller, J.L.2
  • 50
    • 0029790656 scopus 로고    scopus 로고
    • FGF and stress regulate CREB and ATF-1 via a pathway involving p38 MAP kinase and MAPKAP kinase-2
    • Tan Y, Rouse J, Zhang AH, Cariati S, Cohen P, Comb MJ (1996) FGF and stress regulate CREB and ATF-1 via a pathway involving p38 MAP kinase and MAPKAP kinase-2. EMBO J 15:4629-4642
    • (1996) EMBO J , vol.15 , pp. 4629-4642
    • Tan, Y.1    Rouse, J.2    Zhang, A.H.3    Cariati, S.4    Cohen, P.5    Comb, M.J.6
  • 52
    • 0029923193 scopus 로고    scopus 로고
    • Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase
    • McLaughlin MM, Kumar S, McDonnell PC, VanHorn S, Lee JC, Livi GP, Young PR (1996) Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase. J Biol Chem 271:8488-8492
    • (1996) J Biol Chem , vol.271 , pp. 8488-8492
    • McLaughlin, M.M.1    Kumar, S.2    McDonnell, P.C.3    VanHorn, S.4    Lee, J.C.5    Livi, G.P.6    Young, P.R.7
  • 54
    • 0032563807 scopus 로고    scopus 로고
    • Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2
    • Ben-Levy R, Hooper S, Wilson R, Paterson HF, Marshall CJ (1998) Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2. Curr Biol 8:1049-1057
    • (1998) Curr Biol , vol.8 , pp. 1049-1057
    • Ben-Levy, R.1    Hooper, S.2    Wilson, R.3    Paterson, H.F.4    Marshall, C.J.5
  • 55
    • 0032526988 scopus 로고    scopus 로고
    • Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation
    • Engel K, Kotlyarov A, Gaestel M (1998) Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation. EMBO J 17:3363-3371
    • (1998) EMBO J , vol.17 , pp. 3363-3371
    • Engel, K.1    Kotlyarov, A.2    Gaestel, M.3
  • 56
    • 0026608787 scopus 로고
    • Nuclear-localization and regulation of ERK-encoded and RSK-encoded protein kinases
    • Chen RH, Sarnecki C, Blenis J (1992) Nuclear-localization and regulation of ERK-encoded and RSK-encoded protein kinases. Mol Cell Biol 12:915-927
    • (1992) Mol Cell Biol , vol.12 , pp. 915-927
    • Chen, R.H.1    Sarnecki, C.2    Blenis, J.3
  • 58
    • 0032567039 scopus 로고    scopus 로고
    • PIF3, a phytochrome-interacting factor necessary for normal photoinduced signal transduction, is a novel basic helixloop-helix protein
    • Ni M, Tepperman JM, Quail PH (1998) PIF3, a phytochrome-interacting factor necessary for normal photoinduced signal transduction, is a novel basic helixloop-helix protein. Cell 95:657-667
    • (1998) Cell , vol.95 , pp. 657-667
    • Ni, M.1    Tepperman, J.M.2    Quail, P.H.3
  • 59
    • 0030977270 scopus 로고    scopus 로고
    • MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates
    • Fukunaga R, Hunter T (1997) MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. EMBO J 16:1921-1933
    • (1997) EMBO J , vol.16 , pp. 1921-1933
    • Fukunaga, R.1    Hunter, T.2
  • 60
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases MNK1 and MNK2
    • Waskiewicz AJ, Flynn A, Proud CG, Cooper JA (1997) Mitogen-activated protein kinases activate the serine/threonine kinases MNK1 and MNK2. EMBO J 16:1909-1920
    • (1997) EMBO J , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Cooper, J.A.4
  • 62
    • 85029461568 scopus 로고
    • Divergent functional roles for pp90(Rsk) kinase domains
    • Bjorbaek C, Zhao Y, Moller DE (1995) Divergent functional roles for pp90(Rsk) kinase domains. Diabetes 44:A102
    • (1995) Diabetes , vol.44
    • Bjorbaek, C.1    Zhao, Y.2    Moller, D.E.3
  • 63
    • 0031577164 scopus 로고    scopus 로고
    • Identification of serine 380 as the major site of autophosphorylation of Xenopus pp90rsk
    • Vik TA, Ryder JW (1997) Identification of serine 380 as the major site of autophosphorylation of Xenopus pp90rsk. Biochem Biophys Res Comm 235:398-402
    • (1997) Biochem Biophys Res Comm , vol.235 , pp. 398-402
    • Vik, T.A.1    Ryder, J.W.2
  • 64
    • 0031952597 scopus 로고    scopus 로고
    • Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90(rsk) that are inducible by MAPK
    • Dalby KN, Morrice N, Caudwell FB, Avruch J, Cohen P (1998) Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90(rsk) that are inducible by MAPK. J Biol Chem 273:1496-1505
    • (1998) J Biol Chem , vol.273 , pp. 1496-1505
    • Dalby, K.N.1    Morrice, N.2    Caudwell, F.B.3    Avruch, J.4    Cohen, P.5
  • 65
    • 0030207894 scopus 로고    scopus 로고
    • Transcriptional control: Versatile molecular glue
    • Janknecht R, Hunter T (1996) Transcriptional control: versatile molecular glue. Curr Biol 6:951-954
    • (1996) Curr Biol , vol.6 , pp. 951-954
    • Janknecht, R.1    Hunter, T.2
  • 66
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional co-activators p300 and CBP are histone acetyltransferases
    • Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y (1996) The transcriptional co-activators p300 and CBP are histone acetyltransferases. Cell 87:953-959
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 67
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister AJ, Kouzarides T (1996) The CBP co-activator is a histone acetyltransferase. Nature 384:641-643
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 68
    • 0343417089 scopus 로고    scopus 로고
    • The p300/CBP family: Integrating signals with transcription factors and chromatin
    • Shikama N, Lyon J, LaThangue NB (1997) The p300/CBP family: Integrating signals with transcription factors and chromatin. Trends Cell Biol 7:230-236
    • (1997) Trends Cell Biol , vol.7 , pp. 230-236
    • Shikama, N.1    Lyon, J.2    LaThangue, N.B.3
  • 69
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes TR, Thorne AW, Crane-Robinson C (1988) A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J 7:1395-1402
    • (1988) EMBO J , vol.7 , pp. 1395-1402
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 71
    • 0028326787 scopus 로고
    • Core histone hyperacetylation co-maps with generalized DNase-I sensitivity in the chicken β-globin chromosomal domain
    • Hebbes TR, Clayton AL, Thorne AW, Crane-Robinson C (1994) Core histone hyperacetylation co-maps with generalized DNase-I sensitivity in the chicken β-globin chromosomal domain. EMBO J 13:1823-1830
    • (1994) EMBO J , vol.13 , pp. 1823-1830
    • Hebbes, T.R.1    Clayton, A.L.2    Thorne, A.W.3    Crane-Robinson, C.4
  • 72
    • 0026566417 scopus 로고
    • Histone-H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turner BM, Birley AJ, Lavender J (1992) Histone-H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell 69:375-384
    • (1992) Cell , vol.69 , pp. 375-384
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 73
    • 0027183088 scopus 로고
    • The inactive X-chromosome in female mammals is distinguished by a lack of histone-H4 acetylation, a cytogenetic marker for gene-expression
    • Jeppesen P, Turner BM (1993) The inactive X-chromosome in female mammals is distinguished by a lack of histone-H4 acetylation, a cytogenetic marker for gene-expression. Cell 74:281-289
    • (1993) Cell , vol.74 , pp. 281-289
    • Jeppesen, P.1    Turner, B.M.2
  • 74
    • 0025606725 scopus 로고
    • Factors affecting nucleosome structure in transcriptionally active chromatin-histone acetylation, nascent RNA and inhibitors of RNA-synthesis
    • Boffa LC, Walker J, Chen TA, Sterner R, Mariani MR, Allfrey VG (1990) Factors affecting nucleosome structure in transcriptionally active chromatin-histone acetylation, nascent RNA and inhibitors of RNA-synthesis. Eur J Biochem 194:811-823
    • (1990) Eur J Biochem , vol.194 , pp. 811-823
    • Boffa, L.C.1    Walker, J.2    Chen, T.A.3    Sterner, R.4    Mariani, M.R.5    Allfrey, V.G.6
  • 75
    • 0029119093 scopus 로고
    • Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner
    • O'Neill LP, Turner BM (1995) Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner. EMBO J 14:3946-3957
    • (1995) EMBO J , vol.14 , pp. 3946-3957
    • O'Neill, L.P.1    Turner, B.M.2
  • 76
    • 0026546938 scopus 로고
    • HMG protein-14 and protein-17 become cross-linked to the globular domain of histone H3 near the nucleosome core particle dyad
    • Brawley JV, Martinson HG (1992) HMG protein-14 and protein-17 become cross-linked to the globular domain of histone H3 near the nucleosome core particle dyad. Biochemistry 31:364-370
    • (1992) Biochemistry , vol.31 , pp. 364-370
    • Brawley, J.V.1    Martinson, H.G.2
  • 77
    • 0031594573 scopus 로고    scopus 로고
    • Nerve growth factor activates extracelluar signal-regulated kinase and p38 mitogen-activated protein kinase pathways to stimulate CREB serine 133 phosphorylation
    • Xing J, Kornhauser JM, Xia ZG, Thiele EA, Greenberg ME (1998) Nerve growth factor activates extracelluar signal-regulated kinase and p38 mitogen-activated protein kinase pathways to stimulate CREB serine 133 phosphorylation. Mol Cell Biol 18: 1946-1955
    • (1998) Mol Cell Biol , vol.18 , pp. 1946-1955
    • Xing, J.1    Kornhauser, J.M.2    Xia, Z.G.3    Thiele, E.A.4    Greenberg, M.E.5


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