메뉴 건너뛰기




Volumn 107, Issue 50, 2010, Pages 21499-21504

Reversible methylation of promoter-bound STAT3 by histone-modifying enzymes

Author keywords

Gene regulation; Posttranslational modifications; Signal transduction

Indexed keywords

HISTONE METHYLTRANSFERASE; INTERLEUKIN 6; LYSINE; STAT3 PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING 3;

EID: 78650717706     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1016147107     Document Type: Article
Times cited : (267)

References (27)
  • 1
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD (2000) The language of covalent histone modifications. Nature 403 (6765):41-45.
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 2
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T (2007) Chromatin modifications and their function. Cell 128:693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 44349108499 scopus 로고    scopus 로고
    • The emerging field of dynamic lysine methylation of nonhistone proteins
    • Huang J, Berger SL (2008) The emerging field of dynamic lysine methylation of nonhistone proteins. Curr Opin Genet Dev 18:152-158.
    • (2008) Curr Opin Genet Dev , vol.18 , pp. 152-158
    • Huang, J.1    Berger, S.L.2
  • 4
    • 73149099403 scopus 로고    scopus 로고
    • Regulation of NF-kappaB activity through lysine monomethylation of p65
    • Ea CK, Baltimore D (2009) Regulation of NF-kappaB activity through lysine monomethylation of p65. Proc Natl Acad Sci USA 106:18972-18977.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18972-18977
    • Ea, C.K.1    Baltimore, D.2
  • 5
    • 76249100563 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by NSD1/FBXL11-dependent reversible lysine methylation of p65
    • Lu T, et al. (2010) Regulation of NF-kappaB by NSD1/FBXL11-dependent reversible lysine methylation of p65. Proc Natl Acad Sci USA 107(1):46-51.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.1 , pp. 46-51
    • Lu, T.1
  • 6
    • 0028303977 scopus 로고
    • Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway
    • Akira S, et al. (1994) Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway. Cell 77(1):63-71.
    • (1994) Cell , vol.77 , Issue.1 , pp. 63-71
    • Akira, S.1
  • 7
    • 12244251445 scopus 로고    scopus 로고
    • Stat3 dimerization regulated by reversible acetylation of a single lysine residue
    • Yuan ZL, Guan YJ, Chatterjee D, Chin YE (2005) Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science 307:269-273.
    • (2005) Science , vol.307 , pp. 269-273
    • Yuan, Z.L.1    Guan, Y.J.2    Chatterjee, D.3    Chin, Y.E.4
  • 8
    • 13744255376 scopus 로고    scopus 로고
    • Cell signaling. Stat acetylation-A key facet of cytokine signaling?
    • O'Shea JJ, Kanno Y, Chen X, Levy DE (2005) Cell signaling. Stat acetylation-A key facet of cytokine signaling? Science 307:217-218.
    • (2005) Science , vol.307 , pp. 217-218
    • O'shea, J.J.1    Kanno, Y.2    Chen, X.3    Levy, D.E.4
  • 9
    • 27744499936 scopus 로고    scopus 로고
    • STAT3 NH2-terminal acetylation is activated by the hepatic acute-phase response and required for IL-6 induction of angiotensinogen
    • Ray S, Boldogh I, Brasier AR (2005) STAT3 NH2-terminal acetylation is activated by the hepatic acute-phase response and required for IL-6 induction of angiotensinogen. Gastroenterology 129:1616-1632.
    • (2005) Gastroenterology , vol.129 , pp. 1616-1632
    • Ray, S.1    Boldogh, I.2    Brasier, A.R.3
  • 10
    • 0026327416 scopus 로고
    • High-frequency mutagenesis of human cells and characterization of a mutant unresponsive to both alpha and gamma interferons
    • McKendry R, et al. (1991) High-frequency mutagenesis of human cells and characterization of a mutant unresponsive to both alpha and gamma interferons. Proc Natl Acad Sci USA 88:11455-11459.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11455-11459
    • McKendry, R.1
  • 11
    • 0042206459 scopus 로고    scopus 로고
    • A novel sequence in the coiledcoil domain of Stat3 essential for its nuclear translocation
    • Ma J, Zhang T, Novotny-Diermayr V, Tan AL, Cao X (2003) A novel sequence in the coiledcoil domain of Stat3 essential for its nuclear translocation. J Biol Chem 278:29252-29260.
    • (2003) J Biol Chem , vol.278 , pp. 29252-29260
    • Ma, J.1    Zhang, T.2    Novotny-Diermayr, V.3    Tan, A.L.4    Cao, X.5
  • 12
    • 48249138503 scopus 로고    scopus 로고
    • Recruitment of Stat1 to chromatin is required for interferoninduced serine phosphorylation of Stat1 transactivation domain
    • Sadzak I, et al. (2008) Recruitment of Stat1 to chromatin is required for interferoninduced serine phosphorylation of Stat1 transactivation domain. Proc Natl Acad Sci USA 105:8944-8949.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8944-8949
    • Sadzak, I.1
  • 13
    • 9244247669 scopus 로고    scopus 로고
    • Regulation of p53 activity through lysine methylation
    • Chuikov S, et al. (2004) Regulation of p53 activity through lysine methylation. Nature 432:353-360.
    • (2004) Nature , vol.432 , pp. 353-360
    • Chuikov, S.1
  • 14
    • 0032499801 scopus 로고    scopus 로고
    • Three-dimensional structure of the Stat3beta homodimer bound to DNA
    • Becker S, Groner B, Müller CW (1998) Three-dimensional structure of the Stat3beta homodimer bound to DNA. Nature 394(6689):145-151.
    • (1998) Nature , vol.394 , Issue.6689 , pp. 145-151
    • Becker, S.1    Groner, B.2    Müller, C.W.3
  • 16
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi Y, et al. (2004) Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119:941-953.
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1
  • 17
    • 24144462170 scopus 로고    scopus 로고
    • LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
    • Metzger E, et al. (2005) LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription. Nature 437:436-439.
    • (2005) Nature , vol.437 , pp. 436-439
    • Metzger, E.1
  • 18
    • 34548513035 scopus 로고    scopus 로고
    • P53 is regulated by the lysine demethylase LSD1
    • Huang J, et al. (2007) p53 is regulated by the lysine demethylase LSD1. Nature 449 (7158):105-108.
    • (2007) Nature , vol.449 , Issue.7158 , pp. 105-108
    • Huang, J.1
  • 19
    • 58149156264 scopus 로고    scopus 로고
    • The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation
    • Wang J, et al. (2009) The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation. Nat Genet 41:125-129.
    • (2009) Nat Genet , vol.41 , pp. 125-129
    • Wang, J.1
  • 20
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • Li B, Carey M, Workman JL (2007) The role of chromatin during transcription. Cell 128: 707-719.
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 21
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger SL (2007) The complex language of chromatin regulation during transcription. Nature 447:407-412.
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 22
    • 33845204856 scopus 로고    scopus 로고
    • Repression of p53 activity by Smyd2-mediated methylation
    • Huang J, et al. (2006) Repression of p53 activity by Smyd2-mediated methylation. Nature 444:629-632.
    • (2006) Nature , vol.444 , pp. 629-632
    • Huang, J.1
  • 23
    • 34748898280 scopus 로고    scopus 로고
    • Methylation-acetylation interplay activates p53 in response to DNA damage
    • Ivanov GS, et al. (2007) Methylation-acetylation interplay activates p53 in response to DNA damage. Mol Cell Biol 27:6756-6769.
    • (2007) Mol Cell Biol , vol.27 , pp. 6756-6769
    • Ivanov, G.S.1
  • 24
    • 34547809957 scopus 로고    scopus 로고
    • Modulation of p53 function by SET8-mediated methylation at lysine 382
    • Shi X, et al. (2007) Modulation of p53 function by SET8-mediated methylation at lysine 382. Mol Cell 27:636-646.
    • (2007) Mol Cell , vol.27 , pp. 636-646
    • Shi, X.1
  • 25
    • 0037439085 scopus 로고    scopus 로고
    • Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet
    • Kwon T, et al. (2003) Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. EMBO J 22:292-303.
    • (2003) EMBO J , vol.22 , pp. 292-303
    • Kwon, T.1
  • 26
    • 0038607422 scopus 로고    scopus 로고
    • Covalent histone modifications underlie the developmental regulation of insulin gene transcription in pancreatic beta cells
    • Chakrabarti SK, Francis J, Ziesmann SM, Garmey JC, Mirmira RG (2003) Covalent histone modifications underlie the developmental regulation of insulin gene transcription in pancreatic beta cells. J Biol Chem 278:23617-23623.
    • (2003) J Biol Chem , vol.278 , pp. 23617-23623
    • Chakrabarti, S.K.1    Francis, J.2    Ziesmann, S.M.3    Garmey, J.C.4    Mirmira, R.G.5
  • 27
    • 27744606538 scopus 로고    scopus 로고
    • Pdx-1 links histone H3-Lys-4 methylation to RNA polymerase II elongation during activation of insulin transcription
    • Francis J, Chakrabarti SK, Garmey JC, Mirmira RG (2005) Pdx-1 links histone H3-Lys-4 methylation to RNA polymerase II elongation during activation of insulin transcription. J Biol Chem 280:36244-36253.
    • (2005) J Biol Chem , vol.280 , pp. 36244-36253
    • Francis, J.1    Chakrabarti, S.K.2    Garmey, J.C.3    Mirmira, R.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.