메뉴 건너뛰기




Volumn 108, Issue 7, 2011, Pages 2801-2806

Histone code pathway involving H3 S28 phosphorylation and K27 acetylation activates transcription and antagonizes polycomb silencing

Author keywords

Chromatin; Gene expression; Methylation; Phospho acetylation

Indexed keywords

ALPHA GLOBIN; HISTONE H3; HISTONE H3 K27; HISTONE H3 S28; MSK 1 ENZYME; PHOSPHOTRANSFERASE; POLYCOMB GROUP PROTEIN; RSK2 ENZYME; UNCLASSIFIED DRUG;

EID: 79952612932     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1012798108     Document Type: Article
Times cited : (136)

References (30)
  • 1
    • 84882921199 scopus 로고    scopus 로고
    • eds Bradshaw RA, Dennis EA (Academic, Oxford), 2nd Ed
    • Lau PN, Cheung P (2009) Handbook of Cell Signaling, eds Bradshaw RA, Dennis EA (Academic, Oxford), 2nd Ed, pp 2399-2408.
    • (2009) Handbook of Cell Signaling , pp. 2399-2408
    • Lau, P.N.1    Cheung, P.2
  • 2
    • 70349694389 scopus 로고    scopus 로고
    • H3 phosphorylation: Dual role in mitosis and interphase
    • Pérez-Cadahía B, Drobic B, Davie JR (2009) H3 phosphorylation: Dual role in mitosis and interphase. Biochem Cell Biol 87:695-709.
    • (2009) Biochem Cell Biol , vol.87 , pp. 695-709
    • Pérez-Cadahía, B.1    Drobic, B.2    Davie, J.R.3
  • 3
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung P, Allis CD, Sassone-Corsi P (2000) Signaling to chromatin through histone modifications. Cell 103:263-271.
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 4
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung P, et al. (2000) Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol Cell 5:905-915.
    • (2000) Mol Cell , vol.5 , pp. 905-915
    • Cheung, P.1
  • 5
    • 0034679625 scopus 로고    scopus 로고
    • Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation
    • Clayton AL, Rose S, Barratt MJ, Mahadevan LC (2000) Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation. EMBO J 19: 3714-3726. (Pubitemid 30462129)
    • (2000) EMBO Journal , vol.19 , Issue.14 , pp. 3714-3726
    • Clayton, A.L.1    Rose, S.2    Barratt, M.J.3    Mahadevan, L.C.4
  • 6
    • 0033638105 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14
    • Lo WS, et al. (2000) Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Mol Cell 5:917-926.
    • (2000) Mol Cell , vol.5 , pp. 917-926
    • Lo, W.S.1
  • 7
    • 38049018539 scopus 로고    scopus 로고
    • 14-3-3 proteins recognize a histone code at histone H3 and are required for transcriptional activation
    • Winter S, et al. (2008) 14-3-3 proteins recognize a histone code at histone H3 and are required for transcriptional activation. EMBO J 27:88-99.
    • (2008) EMBO J , vol.27 , pp. 88-99
    • Winter, S.1
  • 8
    • 42149189465 scopus 로고    scopus 로고
    • 14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation
    • WalterW, et al. (2008) 14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation. Mol Cell Biol 28:2840-2849.
    • (2008) Mol Cell Biol , vol.28 , pp. 2840-2849
    • Walter, W.1
  • 9
    • 77953710050 scopus 로고    scopus 로고
    • Promoter chromatin remodeling of immediate-early genes is mediated through H3 phosphorylation at either serine 28 or 10 by the MSK1 multi-protein complex
    • Drobic B, Pérez-Cadahía B, Yu J, Kung SK, Davie JR (2010) Promoter chromatin remodeling of immediate-early genes is mediated through H3 phosphorylation at either serine 28 or 10 by the MSK1 multi-protein complex. Nucleic Acids Res 38: 3196-3208.
    • (2010) Nucleic Acids Res , vol.38 , pp. 3196-3208
    • Drobic, B.1    Pérez-Cadahía, B.2    Yu, J.3    Kung, S.K.4    Davie, J.R.5
  • 10
    • 70149112313 scopus 로고    scopus 로고
    • Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation
    • Zippo A, et al. (2009) Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation. Cell 138:1122-1136.
    • (2009) Cell , vol.138 , pp. 1122-1136
    • Zippo, A.1
  • 11
    • 19444363852 scopus 로고    scopus 로고
    • Stimulation of the Ras-MAPK pathway leads to independent phosphorylation of histone H3 on serine 10 and 28
    • DOI 10.1038/sj.onc.1208521
    • Dunn KL, Davie JR (2005) Stimulation of the Ras-MAPK pathway leads to independent phosphorylation of histone H3 on serine 10 and 28. Oncogene 24:3492-3502. (Pubitemid 40756250)
    • (2005) Oncogene , vol.24 , Issue.21 , pp. 3492-3502
    • Dunn, K.L.1    Davie, J.R.2
  • 15
    • 4344592639 scopus 로고    scopus 로고
    • Distinct stimulus-specific histone modifications at Hsp70 chromatin targeted by the transcription factor heat shock factor-1
    • DOI 10.1016/j.molcel.2004.08.002, PII S1097276504004484
    • Thomson S, Hollis A, Hazzalin CA, Mahadevan LC (2004) Distinct stimulus-specific histone modifications at hsp70 chromatin targeted by the transcription factor heat shock factor-1. Mol Cell 15:585-594. (Pubitemid 39141785)
    • (2004) Molecular Cell , vol.15 , Issue.4 , pp. 585-594
    • Thomson, S.1    Hollis, A.2    Hazzalin, C.A.3    Mahadevan, L.C.4
  • 16
    • 70349469565 scopus 로고    scopus 로고
    • Mechanisms of polycomb gene silencing: Knowns and unknowns
    • Simon JA, Kingston RE (2009) Mechanisms of polycomb gene silencing: Knowns and unknowns. Nat Rev Mol Cell Biol 10:697-708.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 697-708
    • Simon, J.A.1    Kingston, R.E.2
  • 18
    • 28844475262 scopus 로고    scopus 로고
    • Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin
    • DOI 10.1038/nature04254
    • Hirota T, Lipp JJ, Toh BH, Peters JM (2005) Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin. Nature 438:1176-1180. (Pubitemid 41831689)
    • (2005) Nature , vol.438 , Issue.7071 , pp. 1176-1180
    • Hirota, T.1    Lipp, J.J.2    Toh, B.-H.3    Peters, J.-M.4
  • 19
    • 55749106396 scopus 로고    scopus 로고
    • The role of the polycomb complex in silencing α-globin gene expression in nonerythroid cells
    • Garrick D, et al. (2008) The role of the polycomb complex in silencing α-globin gene expression in nonerythroid cells. Blood 112:3889-3899.
    • (2008) Blood , vol.112 , pp. 3889-3899
    • Garrick, D.1
  • 20
    • 0031041648 scopus 로고    scopus 로고
    • Herpes simplex virus immediate-early proteins ICP0 and ICP4 activate the endogenous human α-globin gene in nonerythroid cells
    • Cheung P, Panning B, Smiley JR (1997) Herpes simplex virus immediate-early proteins ICP0 and ICP4 activate the endogenous human α-globin gene in nonerythroid cells. J Virol 71:1784-1793. (Pubitemid 27078554)
    • (1997) Journal of Virology , vol.71 , Issue.3 , pp. 1784-1793
    • Cheung, P.1    Panning, B.2    Smiley, J.R.3
  • 21
    • 0028978849 scopus 로고
    • Organization of the α-globin promoter and possible role of nuclear factor I in an α-globin-inducible and a noninducible cell line
    • Rein T, Förster R, Krause A, Winnacker EL, Zorbas H (1995) Organization of the α-globin promoter and possible role of nuclear factor I in an α-globin-inducible and a noninducible cell line. J Biol Chem 270:19643-19650.
    • (1995) J Biol Chem , vol.270 , pp. 19643-19650
    • Rein, T.1    Förster, R.2    Krause, A.3    Winnacker, E.L.4    Zorbas, H.5
  • 22
    • 77953973940 scopus 로고    scopus 로고
    • Characterization of an antagonistic switch between histone H3 lysine 27 methylation and acetylation in the transcriptional regulation of Polycomb group target genes
    • Pasini D, et al. (2010) Characterization of an antagonistic switch between histone H3 lysine 27 methylation and acetylation in the transcriptional regulation of Polycomb group target genes. Nucleic Acids Res 38:4958-4969.
    • (2010) Nucleic Acids Res , vol.38 , pp. 4958-4969
    • Pasini, D.1
  • 23
    • 50049086910 scopus 로고    scopus 로고
    • The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor signaling
    • Ananieva O, et al. (2008) The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor signaling. Nat Immunol 9:1028-1036.
    • (2008) Nat Immunol , vol.9 , pp. 1028-1036
    • Ananieva, O.1
  • 24
    • 58149354155 scopus 로고    scopus 로고
    • A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs RARα to target promoters
    • Bruck N, et al. (2009) A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs RARα to target promoters. EMBO J 28:34-47.
    • (2009) EMBO J , vol.28 , pp. 34-47
    • Bruck, N.1
  • 25
    • 35948954744 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 at Ser10 facilitates RNA polymerase II release from promoter-proximal pausing in Drosophila
    • DOI 10.1101/gad.1604007
    • Ivaldi MS, Karam CS, Corces VG (2007) Phosphorylation of histone H3 at Ser10 facilitates RNA polymerase II release from promoter-proximal pausing in Drosophila. Genes Dev 21:2818-2831. (Pubitemid 350070726)
    • (2007) Genes and Development , vol.21 , Issue.21 , pp. 2818-2831
    • Soledad, I.M.1    Karam, C.S.2    Corces, V.G.3
  • 26
    • 36148991452 scopus 로고    scopus 로고
    • Phosphorylated serine 28 of histone H3 is associated with destabilized nucleosomes in transcribed chromatin
    • DOI 10.1093/nar/gkm737
    • Sun JM, Chen HY, Espino PS, Davie JR (2007) Phosphorylated serine 28 of histone H3 is associated with destabilized nucleosomes in transcribed chromatin. Nucleic Acids Res 35:6640-6647. (Pubitemid 350111628)
    • (2007) Nucleic Acids Research , vol.35 , Issue.19 , pp. 6640-6647
    • Sun, J.-M.1    Chen, H.-Y.2    Espino, P.S.3    Davie, J.R.4
  • 27
    • 0037421959 scopus 로고    scopus 로고
    • Regulation of the ER81 transcription factor and its coactivators by mitogen- and stress-activated protein kinase 1 (MSK1)
    • Janknecht R (2003) Regulation of the ER81 transcription factor and its coactivators by mitogen- and stress-activated protein kinase 1 (MSK1). Oncogene 22:746-755.
    • (2003) Oncogene , vol.22 , pp. 746-755
    • Janknecht, R.1
  • 28
    • 0242612949 scopus 로고    scopus 로고
    • A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1
    • Frödin M, Jensen CJ, Merienne K, Gammeltoft S (2000) A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1. EMBO J 19: 2924-2934. (Pubitemid 30386764)
    • (2000) EMBO Journal , vol.19 , Issue.12 , pp. 2924-2934
    • Frodin, M.1    Jensen, C.J.2    Merienne, K.3    Gammeltoft, S.4
  • 30
    • 77956919550 scopus 로고    scopus 로고
    • Polycomb group protein displacement and gene activation through MSK-dependent H3K27me3S28 phosphorylation
    • Gehani SS, et al. (2010) Polycomb group protein displacement and gene activation through MSK-dependent H3K27me3S28 phosphorylation. Mol Cell 39:886-900.
    • (2010) Mol Cell , vol.39 , pp. 886-900
    • Gehani, S.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.