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Volumn 20, Issue 8, 2010, Pages 908-918

The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation

Author keywords

coactivator; histone demethylase; neuronal differentiation; PHF8; XLMR

Indexed keywords

HISTONE; HISTONE DEMETHYLASE; PHF8 PROTEIN, HUMAN; PHF8 PROTEIN, MOUSE; RETINOIC ACID RECEPTOR; TRANSCRIPTION FACTOR; PROTEIN BINDING;

EID: 77955280094     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2010.81     Document Type: Article
Times cited : (92)

References (40)
  • 1
    • 15744396813 scopus 로고    scopus 로고
    • The key to development: Interpreting the histone code?
    • Margueron R, Trojer P, Reinberg D. The key to development: interpreting the histone code? Curr Opin Genet Dev 2005; 15:163-176.
    • (2005) Curr Opin Genet Dev , vol.15 , pp. 163-176
    • Margueron, R.1    Trojer, P.2    Reinberg, D.3
  • 2
    • 14544280757 scopus 로고    scopus 로고
    • Transcriptional regulation and the role of diverse coactivators in animal cells
    • Roeder RG. Transcriptional regulation and the role of diverse coactivators in animal cells. FEBS Lett 2005; 579:909-915.
    • (2005) FEBS Lett , vol.579 , pp. 909-915
    • Roeder, R.G.1
  • 3
    • 34548526743 scopus 로고    scopus 로고
    • Chromatin remodeling and cancer, Part I: Covalent histone modifications
    • Wang GG, Allis CD, Chi P. Chromatin remodeling and cancer, Part I: covalent histone modifications. Trends Mol Med 2007; 13:363-372.
    • (2007) Trends Mol Med , vol.13 , pp. 363-372
    • Wang, G.G.1    Allis, C.D.2    Chi, P.3
  • 4
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin C, Zhang Y. The diverse functions of histone lysine methylation. Nat Rev Mol Cell Biol 2005; 6:838-849.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 5
    • 23944509075 scopus 로고    scopus 로고
    • The SET-domain protein superfamily: Protein lysine methyltransferases
    • Dillon SC, Zhang X, Trievel RC, Cheng X. The SET-domain protein superfamily: protein lysine methyltransferases. Genome Biol 2005; 6:227.
    • (2005) Genome Biol , vol.6 , pp. 227
    • Dillon, S.C.1    Zhang, X.2    Trievel, R.C.3    Cheng, X.4
  • 6
    • 34848911602 scopus 로고    scopus 로고
    • Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4
    • Vermeulen M, Mulder KW, Denissov S, et al. Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4. Cell 2007; 131:58-69.
    • (2007) Cell , vol.131 , pp. 58-69
    • Vermeulen, M.1    Mulder, K.W.2    Denissov, S.3
  • 7
    • 33745839365 scopus 로고    scopus 로고
    • A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling
    • Wysocka J, Swigut T, Xiao H, et al. A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling. Nature 2006; 442:86-90.
    • (2006) Nature , vol.442 , pp. 86-90
    • Wysocka, J.1    Swigut, T.2    Xiao, H.3
  • 8
    • 0037083757 scopus 로고    scopus 로고
    • Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation
    • Nishioka K, Chuikov S, Sarma K, et al. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev 2002; 16:479-489.
    • (2002) Genes Dev , vol.16 , pp. 479-489
    • Nishioka, K.1    Chuikov, S.2    Sarma, K.3
  • 9
    • 0037023681 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex
    • Zegerman P, Canas B, Pappin D, Kouzarides T. Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex. J Biol Chem 2002; 277:11621-11624.
    • (2002) J Biol Chem , vol.277 , pp. 11621-11624
    • Zegerman, P.1    Canas, B.2    Pappin, D.3    Kouzarides, T.4
  • 10
    • 0035282458 scopus 로고    scopus 로고
    • Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
    • Bannister AJ, Zegerman P, Partridge JF, et al. Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 2001; 410:120-124.
    • (2001) Nature , vol.410 , pp. 120-124
    • Bannister, A.J.1    Zegerman, P.2    Partridge, J.F.3
  • 11
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 2001; 410:116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 12
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi Y, Lan F, Matson C, et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 2004; 119:941-953.
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3
  • 13
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • Tsukada Y, Fang J, Erdjument-Bromage H, et al. Histone demethylation by a family of JmjC domain-containing proteins. Nature 2006; 439:811-816.
    • (2006) Nature , vol.439 , pp. 811-816
    • Tsukada, Y.1    Fang, J.2    Erdjument-Bromage, H.3
  • 14
    • 35348812522 scopus 로고    scopus 로고
    • LSD1 and the chemistry of histone demethylation
    • Culhane JC, Cole PA. LSD1 and the chemistry of histone demethylation. Curr Opin Chem Biol 2007; 11:561-568.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 561-568
    • Culhane, J.C.1    Cole, P.A.2
  • 15
    • 33749576106 scopus 로고    scopus 로고
    • Histone demethylation by hydroxylation: Chemistry in action
    • Schneider J, Shilatifard A. Histone demethylation by hydroxylation: chemistry in action. ACS Chem Biol 2006; 1:75-81.
    • (2006) ACS Chem Biol , vol.1 , pp. 75-81
    • Schneider, J.1    Shilatifard, A.2
  • 16
    • 26944461197 scopus 로고    scopus 로고
    • Mutations in PHF8 are associated with X linked mental retardation and cleft lip/ cleft palate
    • Laumonnier F, Holbert S, Ronce N, et al. Mutations in PHF8 are associated with X linked mental retardation and cleft lip/ cleft palate. J Med Genet 2005; 42:780-786.
    • (2005) J Med Genet , vol.42 , pp. 780-786
    • Laumonnier, F.1    Holbert, S.2    Ronce, N.3
  • 17
    • 34547862845 scopus 로고    scopus 로고
    • Screening of mutations in the PHF8 gene and identification of a novel mutation in a Finnish family with XLMR and cleft lip/cleft palate
    • Koivisto AM, Ala-Mello S, Lemmela S, et al. Screening of mutations in the PHF8 gene and identification of a novel mutation in a Finnish family with XLMR and cleft lip/cleft palate. Clin Genet 2007; 72:145-149.
    • (2007) Clin Genet , vol.72 , pp. 145-149
    • Koivisto, A.M.1    Ala-Mello, S.2    Lemmela, S.3
  • 18
    • 33745847680 scopus 로고    scopus 로고
    • The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36
    • Klose RJ, Yamane K, Bae Y, et al. The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36. Nature 2006; 442:312-316.
    • (2006) Nature , vol.442 , pp. 312-316
    • Klose, R.J.1    Yamane, K.2    Bae, Y.3
  • 19
    • 0027385167 scopus 로고
    • Replication-coupled chromatin assembly is required for the repression of basal transcription in vivo
    • Almouzni G, Wolffe AP. Replication-coupled chromatin assembly is required for the repression of basal transcription in vivo. Genes Dev 1993; 7:2033-2047.
    • (1993) Genes Dev , vol.7 , pp. 2033-2047
    • Almouzni, G.1    Wolffe, A.P.2
  • 20
    • 15044350409 scopus 로고    scopus 로고
    • Relationship between histone H3 lysine 9 methylation, transcription repression, and heterochromatin protein 1 recruitment
    • Stewart MD, Li J, Wong J. Relationship between histone H3 lysine 9 methylation, transcription repression, and heterochromatin protein 1 recruitment. Mol Cell Biol 2005; 25:2525-2538.
    • (2005) Mol Cell Biol , vol.25 , pp. 2525-2538
    • Stewart, M.D.1    Li, J.2    Wong, J.3
  • 21
    • 55949118684 scopus 로고    scopus 로고
    • PHD fingers in human diseases: Disorders arising from misinterpreting epigenetic marks
    • Baker LA, Allis CD, Wang GG. PHD fingers in human diseases: disorders arising from misinterpreting epigenetic marks. Mutat Res 2008; 647:3-12.
    • (2008) Mutat Res , vol.647 , pp. 3-12
    • Baker, L.A.1    Allis, C.D.2    Wang, G.G.3
  • 22
    • 37849038263 scopus 로고    scopus 로고
    • ICBP90, a novel methyl K9 H3 binding protein linking protein ubiquitination with heterochromatin formation
    • Karagianni P, Amazit L, Qin J, Wong J. ICBP90, a novel methyl K9 H3 binding protein linking protein ubiquitination with heterochromatin formation. Mol Cell Biol 2008; 28:705-717.
    • (2008) Mol Cell Biol , vol.28 , pp. 705-717
    • Karagianni, P.1    Amazit, L.2    Qin, J.3    Wong, J.4
  • 23
    • 33947100875 scopus 로고    scopus 로고
    • Role of retinoic acid in the differentiation of embryonal carcinoma and embryonic stem cells
    • Soprano DR, Teets BW, Soprano KJ. Role of retinoic acid in the differentiation of embryonal carcinoma and embryonic stem cells. Vitam Horm 2007; 75:69-95.
    • (2007) Vitam Horm , vol.75 , pp. 69-95
    • Soprano, D.R.1    Teets, B.W.2    Soprano, K.J.3
  • 24
    • 3343010551 scopus 로고    scopus 로고
    • Neurogenin1 is sufficient to induce neuronal differentiation of embryonal carcinoma P19 cells in the absence of retinoic acid
    • Kim S, Yoon YS, Kim JW, et al. Neurogenin1 is sufficient to induce neuronal differentiation of embryonal carcinoma P19 cells in the absence of retinoic acid. Cell Mol Neurobiol 2004; 24:343-356.
    • (2004) Cell Mol Neurobiol , vol.24 , pp. 343-356
    • Kim, S.1    Yoon, Y.S.2    Kim, J.W.3
  • 25
    • 0012473279 scopus 로고
    • The nuclear receptor superfamily: The second decade
    • Mangelsdorf DJ, Thummel C, Beato M, et al. The nuclear receptor superfamily: the second decade. Cell 1995; 83:835-839.
    • (1995) Cell , vol.83 , pp. 835-839
    • Mangelsdorf, D.J.1    Thummel, C.2    Beato, M.3
  • 26
    • 34948899771 scopus 로고    scopus 로고
    • Aberrant chromatin remodeling by retinoic acid receptor alpha fusion proteins assessed at the single-cell level
    • Qiu J, Huang Y, Chen G, et al. Aberrant chromatin remodeling by retinoic acid receptor alpha fusion proteins assessed at the single-cell level. Mol Biol Cell 2007; 18:3941-3951.
    • (2007) Mol Biol Cell , vol.18 , pp. 3941-3951
    • Qiu, J.1    Huang, Y.2    Chen, G.3
  • 27
    • 34347341762 scopus 로고    scopus 로고
    • A novel mutation in the PHF8 gene is associated with X-linked mental retardation with cleft lip/cleft palate
    • Abidi FE, Miano MG, Murray JC, Schwartz CE. A novel mutation in the PHF8 gene is associated with X-linked mental retardation with cleft lip/cleft palate. Clin Genet 2007; 72:19-22.
    • (2007) Clin Genet , vol.72 , pp. 19-22
    • Abidi, F.E.1    Miano, M.G.2    Murray, J.C.3    Schwartz, C.E.4
  • 28
    • 77949432014 scopus 로고    scopus 로고
    • PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylase
    • Loenarz C, Ge W, Coleman ML, et al. PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylase. Hum Mol Genet 2010; 19:217-222.
    • (2010) Hum Mol Genet , vol.19 , pp. 217-222
    • Loenarz, C.1    Ge, W.2    Coleman, M.L.3
  • 29
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases
    • Horton JR, Upadhyay AK, Qi HH, et al. Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. Nat Struct Mol Biol 2010; 17:38-43.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 38-43
    • Horton, J.R.1    Upadhyay, A.K.2    Qi, H.H.3
  • 30
    • 77950521594 scopus 로고    scopus 로고
    • PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation
    • Feng W, Yonezawa M, Ye J, Jenuwein T, Grummt I. PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation. Nat Struct Mol Biol 2010; 17:445-450.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 445-450
    • Feng, W.1    Yonezawa, M.2    Ye, J.3    Jenuwein, T.4    Grummt, I.5
  • 31
    • 77953449792 scopus 로고    scopus 로고
    • PHF8 targets histone methylation and RNA polymerase II to activate transcription
    • Apr 26; doi:10.1128/ MCB.01520-09
    • Fortschegger K, de Graaf P, Outchkourov NS, et al. PHF8 targets histone methylation and RNA polymerase II to activate transcription. Mol Cell Biol 2010 Apr 26; doi:10.1128/ MCB.01520-09.
    • (2010) Mol Cell Biol
    • Fortschegger, K.1    De Graaf, P.2    Outchkourov, N.S.3
  • 32
    • 77950893589 scopus 로고    scopus 로고
    • A functional link between the histone demethylase PHF8 and the transcription factor ZNF711 in X-linked mental retardation
    • Kleine-Kohlbrecher D, Christensen J, Vandamme J, et al. A functional link between the histone demethylase PHF8 and the transcription factor ZNF711 in X-linked mental retardation. Mol Cell 2010; 38:165-178.
    • (2010) Mol Cell , vol.38 , pp. 165-178
    • Kleine-Kohlbrecher, D.1    Christensen, J.2    Vandamme, J.3
  • 33
    • 76449093977 scopus 로고    scopus 로고
    • Structural insights into a novel histone demethylase PHF8
    • Yu L, Wang Y, Huang S, et al. Structural insights into a novel histone demethylase PHF8. Cell Res 2010; 20:166-173.
    • (2010) Cell Res , vol.20 , pp. 166-173
    • Yu, L.1    Wang, Y.2    Huang, S.3
  • 34
    • 77951240318 scopus 로고    scopus 로고
    • Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation
    • Wen H, Li J, Song T, et al. Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation. J Biol Chem 2010; 285:9322-9326.
    • (2010) J Biol Chem , vol.285 , pp. 9322-9326
    • Wen, H.1    Li, J.2    Song, T.3
  • 35
    • 76449085537 scopus 로고    scopus 로고
    • Dual-specificity histone demethylase KIAA1718 (KDM7A) regulates neural differentiation through FGF4
    • Huang C, Xiang Y, Wang Y, et al. Dual-specificity histone demethylase KIAA1718 (KDM7A) regulates neural differentiation through FGF4. Cell Res 2010; 20:154-165.
    • (2010) Cell Res , vol.20 , pp. 154-165
    • Huang, C.1    Xiang, Y.2    Wang, Y.3
  • 36
    • 67349266612 scopus 로고    scopus 로고
    • Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger
    • Wang GG, Song J, Wang Z, et al. Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger. Nature 2009; 459:847-851.
    • (2009) Nature , vol.459 , pp. 847-851
    • Wang, G.G.1    Song, J.2    Wang, Z.3
  • 37
    • 33947245128 scopus 로고    scopus 로고
    • RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3
    • Christensen J, Agger K, Cloos PA, et al. RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3. Cell 2007; 128:1063-1076.
    • (2007) Cell , vol.128 , pp. 1063-1076
    • Christensen, J.1    Agger, K.2    Cloos, P.A.3
  • 38
    • 33847401344 scopus 로고    scopus 로고
    • The retinoblastoma binding protein RBP2 is an H3K4 demethylase
    • Klose RJ, Yan Q, Tothova Z, et al. The retinoblastoma binding protein RBP2 is an H3K4 demethylase. Cell 2007; 128:889-900.
    • (2007) Cell , vol.128 , pp. 889-900
    • Klose, R.J.1    Yan, Q.2    Tothova, Z.3
  • 39
    • 0037088996 scopus 로고    scopus 로고
    • Interactions of STAT5b-RARalpha, a novel acute promyelocytic leukemia fusion protein, with retinoic acid receptor and STAT3 signaling pathways
    • Dong S, Tweardy DJ. Interactions of STAT5b-RARalpha, a novel acute promyelocytic leukemia fusion protein, with retinoic acid receptor and STAT3 signaling pathways. Blood 2002; 99:2637-2646.
    • (2002) Blood , vol.99 , pp. 2637-2646
    • Dong, S.1    Tweardy, D.J.2
  • 40
    • 33745624285 scopus 로고    scopus 로고
    • Decreased intranuclear mobility of acute myeloid leukemia 1-containing fusion pro teins is accompanied by reduced mobility and compartmentalization of core binding factor beta
    • Qiu J, Wong J, Tweardy DJ, Dong S. Decreased intranuclear mobility of acute myeloid leukemia 1-containing fusion pro teins is accompanied by reduced mobility and compartmentalization of core binding factor beta. Oncogene 2006; 25:3982-3993.
    • (2006) Oncogene , vol.25 , pp. 3982-3993
    • Qiu, J.1    Wong, J.2    Tweardy, D.J.3    Dong, S.4


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