메뉴 건너뛰기




Volumn 967, Issue , 2013, Pages 167-178

Acetylation of endogenous STAT proteins

Author keywords

Acetylation; HAT; HDACi; IFN; Immunoprecipitation; STAT; STAT1

Indexed keywords

STAT PROTEIN; STAT1 PROTEIN; CELL EXTRACT; LYSINE;

EID: 84878769838     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-242-1_12     Document Type: Chapter
Times cited : (10)

References (41)
  • 1
    • 34547924046 scopus 로고    scopus 로고
    • HATs and HDACs: From structure, function and regulation to novel strategies for therapy and prevention
    • Yang XJ, Seto E (2007) HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention. Oncogene 26(37):5310–5318.
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5310-5318
    • Yang, X.J.1    Seto, E.2
  • 2
    • 67349202438 scopus 로고    scopus 로고
    • HDACi–targets beyond chromatin
    • Buchwald M, Krämer OH, Heinzel T (2009) HDACi–targets beyond chromatin. Cancer Lett 280(2):160–167.
    • (2009) Cancer Lett , vol.280 , Issue.2 , pp. 160-167
    • Buchwald, M.1    Krämer, O.H.2    Heinzel, T.3
  • 3
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • Spange S et al (2009) Acetylation of non-histone proteins modulates cellular signalling at multiple levels. Int J Biochem Cell Biol 41(1):185–198.
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.1 , pp. 185-198
    • Spange, S.1
  • 4
    • 70449675089 scopus 로고    scopus 로고
    • HDAC2: A critical factor in health and disease
    • Krämer OH (2009) HDAC2: a critical factor in health and disease. Trends Pharmacol Sci 30(12):647–655.
    • (2009) Trends Pharmacol Sci , vol.30 , Issue.12 , pp. 647-655
    • Krämer, O.H.1
  • 5
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden JE, Peart MJ, Johnstone RW (2006) Anticancer activities of histone deacetylase inhibitors. Nat Rev Drug Discov 5(9):769–784.
    • (2006) Nat Rev Drug Discov , vol.5 , Issue.9 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 6
    • 34547882857 scopus 로고    scopus 로고
    • Aberrant expression of histone deacetylase 6 in oral squamous cell carcinoma
    • Sakuma T et al (2006) Aberrant expression of histone deacetylase 6 in oral squamous cell carcinoma. Int J Oncol 29(1):117–124.
    • (2006) Int J Oncol , vol.29 , Issue.1 , pp. 117-124
    • Sakuma, T.1
  • 7
    • 33744956666 scopus 로고    scopus 로고
    • Histone deacetylase 3 (HDAC3) and other class I HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer
    • Wilson AJ et al (2006) Histone deacetylase 3 (HDAC3) and other class I HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer. J Biol Chem 281(19):13548–13558.
    • (2006) J Biol Chem , vol.281 , Issue.19 , pp. 13548-13558
    • Wilson, A.J.1
  • 8
    • 77950640292 scopus 로고    scopus 로고
    • Inhibitors of HDACs–effective drugs against cancer?
    • Müller S, Krämer OH (2010) Inhibitors of HDACs–effective drugs against cancer? Curr Cancer Drug Targets 10(2):210–228.
    • (2010) Curr Cancer Drug Targets , vol.10 , Issue.2 , pp. 210-228
    • Müller, S.1    Krämer, O.H.2
  • 9
    • 77249087051 scopus 로고    scopus 로고
    • Chemical phylogenetics of histone deacetylases
    • Bradner JE et al (2010) Chemical phylogenetics of histone deacetylases. Nat Chem Biol 6(3):238–243.
    • (2010) Nat Chem Biol , vol.6 , Issue.3 , pp. 238-243
    • Bradner, J.E.1
  • 10
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman KJ et al (2002) Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J Biol Chem 277(47):45099–45107.
    • (2002) J Biol Chem , vol.277 , Issue.47 , pp. 45099-45107
    • Bitterman, K.J.1
  • 11
    • 32644449048 scopus 로고    scopus 로고
    • Acetylation of Stat1 modulates NF-kappaB activity
    • Krämer OH et al (2006) Acetylation of Stat1 modulates NF-kappaB activity. Genes Dev 20(4):473–485.
    • (2006) Genes Dev , vol.20 , Issue.4 , pp. 473-485
    • Krämer, O.H.1
  • 13
    • 35548944961 scopus 로고    scopus 로고
    • SnapShot: JAK-STAT signaling
    • Mertens C, Darnell JE Jr (2007) SnapShot: JAK-STAT signaling. Cell 131(3):612.
    • (2007) Cell , vol.131 , Issue.3 , pp. 612
    • Mertens, C.1    Darnell, J.E.2
  • 14
    • 70349736116 scopus 로고    scopus 로고
    • Cross-regulation of signaling pathways by interferon-gamma: Implications for immune responses and autoimmune diseases
    • Hu X, Ivashkiv LB (2009) Cross-regulation of signaling pathways by interferon-gamma: implications for immune responses and autoimmune diseases. Immunity 31(4):539–550.
    • (2009) Immunity , vol.31 , Issue.4 , pp. 539-550
    • Hu, X.1    Ivashkiv, L.B.2
  • 15
    • 33846202008 scopus 로고    scopus 로고
    • STAT1 as a key modulator of cell death
    • Kim HS, Lee MS (2007) STAT1 as a key modulator of cell death. Cell Signal 19(3):454–465.
    • (2007) Cell Signal , vol.19 , Issue.3 , pp. 454-465
    • Kim, H.S.1    Lee, M.S.2
  • 16
    • 12244251445 scopus 로고    scopus 로고
    • Stat3 dimerization regulated by reversible acetylation of a single lysine residue
    • Yuan ZL et al (2005) Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science 307(5707):269–273.
    • (2005) Science , vol.307 , Issue.5707 , pp. 269-273
    • Yuan, Z.L.1
  • 17
    • 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(5):1616–1632.
    • (2005) Gastroenterology , vol.129 , Issue.5 , pp. 1616-1632
    • Ray, S.1    Boldogh, I.2    Brasier, A.R.3
  • 18
    • 80052470393 scopus 로고    scopus 로고
    • P16INK4a-deficiency promotes IL-4-induced polarization and inhibits pro-inflammatory signaling in macrophages
    • Cudejko C et al (2011) p16INK4a-deficiency promotes IL-4-induced polarization and inhibits pro-inflammatory signaling in macrophages. Blood 118(9):2556–2566.
    • (2011) Blood , vol.118 , Issue.9 , pp. 2556-2566
    • Cudejko, C.1
  • 19
    • 79959895071 scopus 로고    scopus 로고
    • HDAC4-regulated STAT1 activation mediates platinum resistance in ovarian cancer
    • Stronach EA et al (2011) HDAC4-regulated STAT1 activation mediates platinum resistance in ovarian cancer. Cancer Res 71(13):4412–4422.
    • (2011) Cancer Res , vol.71 , Issue.13 , pp. 4412-4422
    • Stronach, E.A.1
  • 20
    • 34547609011 scopus 로고    scopus 로고
    • Stat1 acetylation inhibits inducible nitric oxide synthase expression in interferon-gamma-treated RAW264.7 murine macrophages
    • Guo L et al (2007) Stat1 acetylation inhibits inducible nitric oxide synthase expression in interferon-gamma-treated RAW264.7 murine macrophages. Surgery 142(2):156–162.
    • (2007) Surgery , vol.142 , Issue.2 , pp. 156-162
    • Guo, L.1
  • 21
    • 34249794259 scopus 로고    scopus 로고
    • IFN-gamma protects cerulein-induced acute pancreatitis by repressing NF-kappa B activation
    • Hayashi T et al (2007) IFN-gamma protects cerulein-induced acute pancreatitis by repressing NF-kappa B activation. J Immunol 178(11):7385–7394.
    • (2007) J Immunol , vol.178 , Issue.11 , pp. 7385-7394
    • Hayashi, T.1
  • 22
    • 58849139353 scopus 로고    scopus 로고
    • A phosphorylation-acetylation switch regulates STAT1 signaling
    • Krämer OH et al (2009) A phosphorylation-acetylation switch regulates STAT1 signaling. Genes Dev 23(2):223–235.
    • (2009) Genes Dev , vol.23 , Issue.2 , pp. 223-235
    • Krämer, O.H.1
  • 23
    • 34848817968 scopus 로고    scopus 로고
    • Acetylation-dependent signal transduction for type I interferon receptor
    • Tang X et al (2007) Acetylation-dependent signal transduction for type I interferon receptor. Cell 131(1):93–105.
    • (2007) Cell , vol.131 , Issue.1 , pp. 93-105
    • Tang, X.1
  • 24
    • 84859972405 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors block IFNgamma-induced STAT1 phosphorylation
    • Ginter T et al (2012) Histone deacetylase inhibitors block IFNgamma-induced STAT1 phosphorylation. Cell Signal 24(7):1453–1460.
    • (2012) Cell Signal , vol.24 , Issue.7 , pp. 1453-1460
    • Ginter, T.1
  • 25
    • 3042699400 scopus 로고    scopus 로고
    • Impairment of interferon-induced IRF-7 gene expression due to inhibition of ISGF3 formation by trichostatin A
    • Genin P, Morin P, Civas A (2003) Impairment of interferon-induced IRF-7 gene expression due to inhibition of ISGF3 formation by trichostatin A. J Virol 77(12):7113–7119.
    • (2003) J Virol , vol.77 , Issue.12 , pp. 7113-7119
    • Genin, P.1    Morin, P.2    Civas, A.3
  • 26
    • 4644366536 scopus 로고    scopus 로고
    • Histone deacetylase activity is required to recruit RNA polymerase II to the promoters of selected interferon-stimulated early response genes
    • Sakamoto S, Potla R, Larner AC (2004) Histone deacetylase activity is required to recruit RNA polymerase II to the promoters of selected interferon-stimulated early response genes. J Biol Chem 279(39):40362–40367.
    • (2004) J Biol Chem , vol.279 , Issue.39 , pp. 40362-40367
    • Sakamoto, S.1    Potla, R.2    Larner, A.C.3
  • 27
    • 0344304443 scopus 로고    scopus 로고
    • Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1
    • Nusinzon I, Horvath CM (2003) Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1. Proc Natl Acad Sci USA 100(25):14742–14747.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.25 , pp. 14742-14747
    • Nusinzon, I.1    Horvath, C.M.2
  • 28
    • 3042752799 scopus 로고    scopus 로고
    • Induction of interferon-stimulated gene expression and antiviral responses require protein deacetylase activity
    • Chang HM et al (2004) Induction of interferon-stimulated gene expression and antiviral responses require protein deacetylase activity. Proc Natl Acad Sci U S A 101(26):9578–9583.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.26 , pp. 9578-9583
    • Chang, H.M.1
  • 29
    • 3142721913 scopus 로고    scopus 로고
    • Requirement of histone deacetylase activity for signaling by STAT1
    • Klampfer L et al (2004) Requirement of histone deacetylase activity for signaling by STAT1. J Biol Chem 279(29):30358–30368.
    • (2004) J Biol Chem , vol.279 , Issue.29 , pp. 30358-30368
    • Klampfer, L.1
  • 30
    • 0141653817 scopus 로고    scopus 로고
    • Inhibition of interferon gamma signaling by the short chain fatty acid butyrate
    • Klampfer L et al (2003) Inhibition of interferon gamma signaling by the short chain fatty acid butyrate. Mol Cancer Res 1(11):855–862.
    • (2003) Mol Cancer Res , vol.1 , Issue.11 , pp. 855-862
    • Klampfer, L.1
  • 31
    • 71849101259 scopus 로고    scopus 로고
    • Phosphorylation-acetylation switch in the regulation of STAT1 signaling
    • Krämer OH, Heinzel T (2010) Phosphorylation-acetylation switch in the regulation of STAT1 signaling. Mol Cell Endocrinol 315(1–2):40–48.
    • (2010) Mol Cell Endocrinol , vol.315 , Issue.1-2 , pp. 40-48
    • Krämer, O.H.1    Heinzel, T.2
  • 32
    • 26844499947 scopus 로고    scopus 로고
    • Probing lysine acetylation in proteins: Strategies, limitations, and pitfalls of in vitro acetyltransferase assays
    • Dormeyer W, Ott M, Schnolzer M (2005) Probing lysine acetylation in proteins: strategies, limitations, and pitfalls of in vitro acetyltransferase assays. Mol Cell Proteomics 4(9):1226–1239.
    • (2005) Mol Cell Proteomics , vol.4 , Issue.9 , pp. 1226-1239
    • Dormeyer, W.1    Ott, M.2    Schnolzer, M.3
  • 33
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay RT (2005) SUMO: a history of modification. Mol Cell 18(1):1–12.
    • (2005) Mol Cell , vol.18 , Issue.1 , pp. 1-12
    • Hay, R.T.1
  • 34
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C et al (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325(5942):834–840.
    • (2009) Science , vol.325 , Issue.5942 , pp. 834-840
    • Choudhary, C.1
  • 35
    • 77955476430 scopus 로고    scopus 로고
    • Serine proteases in histone deacetylase inhibitor-induced apoptosis
    • Sonnemann J et al (2010) Serine proteases in histone deacetylase inhibitor-induced apoptosis. Mol Cancer Ther 9(8):2440–2441, author reply 2441–2.
    • (2010) Mol Cancer Ther , vol.9 , Issue.8 , pp. 2440-2441
    • Sonnemann, J.1
  • 36
    • 0037184969 scopus 로고    scopus 로고
    • Acetylation of p53 inhibits its ubiquitination by Mdm2
    • Li M et al (2002) Acetylation of p53 inhibits its ubiquitination by Mdm2. J Biol Chem 277(52):50607–50611.
    • (2002) J Biol Chem , vol.277 , Issue.52 , pp. 50607-50611
    • Li, M.1
  • 37
    • 15744385061 scopus 로고    scopus 로고
    • Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation
    • Wang R, Cherukuri P, Luo J (2005) Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation. J Biol Chem 280(12):11528–11534.
    • (2005) J Biol Chem , vol.280 , Issue.12 , pp. 11528-11534
    • Wang, R.1    Cherukuri, P.2    Luo, J.3
  • 38
    • 64049109876 scopus 로고    scopus 로고
    • STAT3 inhibition of gluconeogenesis is downregulated by SirT1
    • Nie Y et al (2009) STAT3 inhibition of gluconeogenesis is downregulated by SirT1. Nat Cell Biol 11(4):492–500.
    • (2009) Nat Cell Biol , vol.11 , Issue.4 , pp. 492-500
    • Nie, Y.1
  • 39
    • 33646591224 scopus 로고    scopus 로고
    • Stat3 activation of NF-kappa B p100 processing involves CBP/p300-mediated acetylation
    • Nadiminty N et al (2006) Stat3 activation of NF-kappa B p100 processing involves CBP/p300-mediated acetylation. Proc Natl Acad Sci U S A 103(19):7264–7269.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.19 , pp. 7264-7269
    • Nadiminty, N.1
  • 40
    • 78650599487 scopus 로고    scopus 로고
    • Acetylation modulates prolactin receptor dimerization
    • Ma L et al (2010) Acetylation modulates prolactin receptor dimerization. Proc Natl Acad Sci U S A 107(45):19314–19319.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.45 , pp. 19314-19319
    • Ma, L.1
  • 41
    • 0035900679 scopus 로고    scopus 로고
    • Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene
    • Shankaranarayanan P et al (2001) Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene. J Biol Chem 276(46):42753–42760.
    • (2001) J Biol Chem , vol.276 , Issue.46 , pp. 42753-42760
    • Shankaranarayanan, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.