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Volumn 493, Issue 7433, 2013, Pages 561-564

TET2 promotes histone O-GlcNAcylation during gene transcription

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; HISTONE H2B; N ACETYLGLUCOSAMINE; SERINE; TET2 PROTEIN; TET3 PROTEIN; UNCLASSIFIED DRUG;

EID: 84872953223     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11742     Document Type: Article
Times cited : (425)

References (35)
  • 1
    • 66149146320 scopus 로고    scopus 로고
    • Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1
    • Tahiliani, M. et al. Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1. Science 324, 930-935 (2009).
    • (2009) Science , vol.324 , pp. 930-935
    • Tahiliani, M.1
  • 2
    • 79956323623 scopus 로고    scopus 로고
    • Dynamic regulation of 5-hydroxymethylcytosine in mouse ES cells and during differentiation
    • Ficz, G. et al. Dynamic regulation of 5-hydroxymethylcytosine in mouse ES cells and during differentiation. Nature 473, 398-402 (2011).
    • (2011) Nature , vol.473 , pp. 398-402
    • Ficz, G.1
  • 3
    • 79956308473 scopus 로고    scopus 로고
    • Genome-wide mapping of 5-hydroxymethylcytosine in embryonic stem cells
    • Pastor, W. A. et al. Genome-wide mapping of 5-hydroxymethylcytosine in embryonic stem cells. Nature 473, 394-397 (2011).
    • (2011) Nature , vol.473 , pp. 394-397
    • Pastor, W.A.1
  • 4
    • 79955948324 scopus 로고    scopus 로고
    • Genome-wide regulation of 5hmC, 5mC, and gene expression by Tet1 hydroxylase in mouse embryonic stem cells
    • Xu, Y. et al. Genome-wide regulation of 5hmC, 5mC, and gene expression by Tet1 hydroxylase in mouse embryonic stem cells. Mol. Cell 42, 451-464 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 451-464
    • Xu, Y.1
  • 5
    • 79956292024 scopus 로고    scopus 로고
    • Dual functions of Tet1 in transcriptional regulation in mouse embryonic stem cells
    • Wu, H. et al. Dual functions of Tet1 in transcriptional regulation in mouse embryonic stem cells. Nature 473, 389-393 (2011).
    • (2011) Nature , vol.473 , pp. 389-393
    • Wu, H.1
  • 6
    • 77956189495 scopus 로고    scopus 로고
    • Role of Tet proteins in 5mC to 5hmC conversion ES-cell self-renewal and inner cell mass specification
    • Ito, S. et al. Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal and inner cell mass specification. Nature 466, 1129-1133 (2010).
    • (2010) Nature , vol.466 , pp. 1129-1133
    • Ito, S.1
  • 7
    • 0036898933 scopus 로고    scopus 로고
    • Diverse regulationof protein function by O-GlcNAc: A nuclear and cytoplasmic carbohydrate post-translational modification
    • Vosseller, K., Sakabe, K.,Wells, L.&Hart, G. W. Diverse regulationof protein function by O-GlcNAc: a nuclear and cytoplasmic carbohydrate post-translational modification. Curr. Opin. Chem. Biol. 6, 851-857 (2002).
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 851-857
    • Vosseller, K.1    Sakabe, K.2    Wells, L.3    Hart, G.W.4
  • 8
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
    • Kreppel, L. K., Blomberg, M. A. & Hart, G. W. Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J. Biol. Chem. 272, 9308-9315 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 9
    • 80053348585 scopus 로고    scopus 로고
    • The role of Tet3 DNA dioxygenase in epigenetic reprogramming by oocytes
    • Gu, T. P. et al. The role of Tet3 DNA dioxygenase in epigenetic reprogramming by oocytes. Nature 477, 606-610 (2011).
    • (2011) Nature , vol.477 , pp. 606-610
    • Gu, T.P.1
  • 10
    • 54349112556 scopus 로고    scopus 로고
    • Structural insights into mechanism and specificity of O-GlcNAc transferase
    • Clarke, A. J. et al. Structural insights into mechanism and specificity of O-GlcNAc transferase. EMBO J. 27, 2780-2788 (2008).
    • (2008) EMBO J. , vol.27 , pp. 2780-2788
    • Clarke, A.J.1
  • 11
    • 46449085222 scopus 로고    scopus 로고
    • Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation
    • Martinez-Fleites, C. et al. Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation. Nature Struct.Mol. Biol. 15, 764-765(2008).
    • (2008) Nature Struct.Mol. Biol. , vol.15 , pp. 764-765
    • Martinez-Fleites, C.1
  • 12
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferaseand its complex with a peptide substrate
    • Lazarus,M. B., Nam, Y., Jiang, J., Sliz, P. & Walker, S. Structure of human O-GlcNAc transferaseand its complex with a peptide substrate.Nature469, 564-567(2011).
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 13
    • 53849113697 scopus 로고    scopus 로고
    • Base J: Discovery, biosyn thesis, and possible functions
    • Borst, P. & Sabatini, R. Base J: discovery, biosynthesis, and possible functions. Annu. Rev. Microbiol. 62, 235-251 (2008).
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 235-251
    • Borst, P.1    Sabatini, R.2
  • 14
    • 80054818714 scopus 로고    scopus 로고
    • Modificationof histonesby sugar b-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated
    • Zhang,S.,Roche,K.,Nasheuer, H. P.&Lowndes,N. F.Modificationof histonesby sugar b-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated. J. Biol. Chem. 286, 37483-37495 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 37483-37495
    • Zhang, S.1    Roche, K.2    Nasheuer, H.P.3    Lowndes, N.F.4
  • 15
    • 84355161950 scopus 로고    scopus 로고
    • GlcNAcylation of histone H2B facilitates its monoubiquitination
    • Fujiki, R. et al. GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature 480, 557-560 (2011).
    • (2011) Nature , vol.480 , pp. 557-560
    • Fujiki, R.1
  • 16
    • 78650447665 scopus 로고    scopus 로고
    • B-N-acetylglucosamine (O-GlcNAc) is part of the histone code
    • Sakabe, K., Wang, Z. & Hart, G. W. b-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proc. Natl Acad. Sci. USA 107, 19915-19920 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 19915-19920
    • Sakabe, K.1    Wang, Z.2    Hart, G.W.3
  • 17
    • 84859512121 scopus 로고    scopus 로고
    • B-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosisspecific phosphorylationson histoneH3
    • Fong, J. J. et al. b-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosisspecific phosphorylationson histoneH3. J. Biol.Chem.287,12195- 12203(2012).
    • (2012) J. Biol.Chem. , vol.287 , pp. 12195-12203
    • Fong, J.J.1
  • 18
    • 79551661274 scopus 로고    scopus 로고
    • O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1
    • Capotosti, F. et al. O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1. Cell 144, 376-388 (2011).
    • (2011) Cell , vol.144 , pp. 376-388
    • Capotosti, F.1
  • 19
    • 0037067659 scopus 로고    scopus 로고
    • Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: Coupling protein O-GlcNAcylation to transcriptional repression
    • Yang, X., Zhang, F. & Kudlow, J. E. Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression. Cell 110, 69-80 (2002).
    • (2002) Cell , vol.110 , pp. 69-80
    • Yang, X.1    Zhang, F.2    Kudlow, J.E.3
  • 20
    • 0033527739 scopus 로고    scopus 로고
    • Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
    • Kreppel, L. K. & Hart, G. W. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J. Biol. Chem. 274, 32015-32022 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 32015-32022
    • Kreppel, L.K.1    Hart, G.W.2
  • 21
    • 0037648473 scopus 로고    scopus 로고
    • Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase
    • Iyer, S. P., Akimoto, Y. & Hart, G. W. Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase. J. Biol. Chem. 278, 5399-5409 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 5399-5409
    • Iyer, S.P.1    Akimoto, Y.2    Hart, G.W.3
  • 22
    • 34547624303 scopus 로고    scopus 로고
    • Genome-wide maps of chromatin state in pluripotent and lineage-committed cells
    • Mikkelsen, T. S. et al. Genome-wide maps of chromatin state in pluripotent and lineage-committed cells. Nature 448, 553-560 (2007).
    • (2007) Nature , vol.448 , pp. 553-560
    • Mikkelsen, T.S.1
  • 23
    • 83855163995 scopus 로고    scopus 로고
    • Uncovering the role of 5-hydroxymethylcytosine in the epigenome
    • Branco, M. R., Ficz, G.&Reik, W.Uncovering the role of 5-hydroxymethylcytosine in the epigenome. Nature Rev. Genet. 13, 7-13 (2012).
    • (2012) Nature Rev. Genet. , vol.13 , pp. 7-13
    • Branco, M.R.1    Ficz, G.2    Reik, W.3
  • 24
    • 79952763586 scopus 로고    scopus 로고
    • Reprogramming of the paternal genome upon fertilization involves genome-wide oxidation of 5-methylcytosine
    • Iqbal, K., Jin, S. G., Pfeifer, G. P. & Szabo, P. E. Reprogramming of the paternal genome upon fertilization involves genome-wide oxidation of 5-methylcytosine. Proc. Natl Acad. Sci. USA 108, 3642-3647 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 3642-3647
    • Iqbal, K.1    Jin, S.G.2    Pfeifer, G.P.3    Szabo, P.E.4
  • 25
    • 80054097425 scopus 로고    scopus 로고
    • Replication-dependent loss of 5-hydroxymethylcytosine in mouse preimplantation embryos
    • Inoue, A. & Zhang, Y. Replication-dependent loss of 5-hydroxymethylcytosine in mouse preimplantation embryos. Science 334, 194 (2011).
    • (2011) Science , vol.334 , Issue.194
    • Inoue, A.1    Zhang, Y.2
  • 26
    • 79954457998 scopus 로고    scopus 로고
    • Genome-wide analysis of 5-hydroxymethylcytosine distribution reveals its dual function in transcriptional regulation in mouse embryonic stem cells
    • Wu, H. et al. Genome-wide analysis of 5-hydroxymethylcytosine distribution reveals its dual function in transcriptional regulation in mouse embryonic stem cells. Genes Dev. 25, 679-684 (2011).
    • (2011) Genes Dev. , vol.25 , pp. 679-684
    • Wu, H.1
  • 27
    • 79956302047 scopus 로고    scopus 로고
    • TET1 and hydroxymethylcytosine in transcription and DNA methylation fidelity
    • Williams, K. et al. TET1 and hydroxymethylcytosine in transcription and DNA methylation fidelity. Nature 473, 343-348 (2011).
    • (2011) Nature , vol.473 , pp. 343-348
    • Williams, K.1
  • 28
    • 78049390185 scopus 로고    scopus 로고
    • O-GlcNAc transferase regulates mitotic chromatin dynamics
    • Sakabe, K. & Hart, G. W. O-GlcNAc transferase regulates mitotic chromatin dynamics. J. Biol. Chem. 285, 34460-34468 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 34460-34468
    • Sakabe, K.1    Hart, G.W.2
  • 29
    • 67650076327 scopus 로고    scopus 로고
    • Essential role of the glycosyltransferase sxc/Ogt in polycomb repression
    • Gambetta, M. C., Oktaba, K. & Muller, J. Essential role of the glycosyltransferase sxc/Ogt in polycomb repression. Science 325, 93-96 (2009).
    • (2009) Science , vol.325 , pp. 93-96
    • Gambetta, M.C.1    Oktaba, K.2    Muller, J.3
  • 30
    • 69449092638 scopus 로고    scopus 로고
    • Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc)
    • Sinclair, D. A. et al. Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc). Proc. Natl Acad. Sci. USA 106, 13427-13432 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 13427-13432
    • Sinclair, D.A.1
  • 32
    • 67349189942 scopus 로고    scopus 로고
    • GlcNAcylation of a histone methyltransferase in retinoic-acidinduced granulopoiesis
    • Fujiki, R. et al. GlcNAcylation of a histone methyltransferase in retinoic-acidinduced granulopoiesis. Nature 459, 455-459 (2009).
    • (2009) Nature , vol.459 , pp. 455-459
    • Fujiki, R.1
  • 33
    • 33947109881 scopus 로고    scopus 로고
    • Reduction of O-GlcNAc protein modification does not prevent insulin resistance in 3T3-L1 adipocytes
    • Robinson, K. A., Ball, L. E. & Buse, M. G. Reduction of O-GlcNAc protein modification does not prevent insulin resistance in 3T3-L1 adipocytes. Am. J. Physiol. Endocrinol. Metab. 292, E884-E890 (2007).
    • (2007) Am. J. Physiol. Endocrinol. Metab. , vol.292
    • Robinson, K.A.1    Ball, L.E.2    Buse, M.G.3
  • 34
    • 78650175023 scopus 로고    scopus 로고
    • Impaired hydroxylation of 5-methylcytosine in myeloid cancers with mutant TET2
    • Ko, M. et al. Impaired hydroxylation of 5-methylcytosine in myeloid cancers with mutant TET2. Nature 468, 839-843 (2010).
    • (2010) Nature , vol.468 , pp. 839-843
    • Ko, M.1
  • 35
    • 78951474461 scopus 로고    scopus 로고
    • MicroRNA hsa-miR-138 inhibits adipogenic differentiation of human adipose tissue-derived mesenchymal stem cells through adenovirus EID-1
    • Yang, Z. et al. MicroRNA hsa-miR-138 inhibits adipogenic differentiation of human adipose tissue-derived mesenchymal stem cells through adenovirus EID-1. Stem Cells Dev. 20, 259-267 (2011).
    • (2011) Stem Cells Dev. , vol.20 , pp. 259-267
    • Yang, Z.1


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