Fbxl10/Kdm2b Recruits Polycomb Repressive Complex 1 to CpG Islands and Regulates H2A Ubiquitylation

Polycomb repressive complex 1 (PRC1) catalyzes lysine 119 monoubiquitylation on H2A (H2AK119ub1) and regulates pluripotency in embryonic stem cells (ESCs). However, the mechanisms controlling the binding of PRC1 to genomic sites and its catalytic activity are poorly understood. Here, we show that Fb...

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Published in	Molecular cell Vol. 49; no. 6; pp. 1134 - 1146
Main Authors	Wu, Xudong, Johansen, Jens Vilstrup, Helin, Kristian
Format	Journal Article
Language	English
Published	United States Elsevier Inc 28.03.2013
Subjects	active sites Animals catalytic activity Cell Differentiation Cell Line CpG Islands DNA embryonic stem cells Embryonic Stem Cells - enzymology Embryonic Stem Cells - physiology Epigenesis, Genetic F-Box Proteins - physiology genes genetic techniques and protocols Genome genomic islands Histones - metabolism Humans Jumonji Domain-Containing Histone Demethylases - physiology lysine Mice Models, Molecular mutants Polycomb Repressive Complex 1 - metabolism Protein Binding Protein Structure, Tertiary Protein Transport Transcription Initiation Site Transcription, Genetic Ubiquitin-Protein Ligases - metabolism Ubiquitination
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Abstract	Polycomb repressive complex 1 (PRC1) catalyzes lysine 119 monoubiquitylation on H2A (H2AK119ub1) and regulates pluripotency in embryonic stem cells (ESCs). However, the mechanisms controlling the binding of PRC1 to genomic sites and its catalytic activity are poorly understood. Here, we show that Fbxl10 interacts with Ring1B and Nspc1, forming a noncanonical PRC1 that is required for H2AK119ub1 in mouse ESCs. Genome-wide analyses reveal that Fbxl10 preferentially binds to CpG islands and colocalizes with Ring1B on Polycomb target genes. Notably, Fbxl10 depletion causes a decrease in Ring1B binding to target genes and a major loss of H2AK119ub1. Furthermore, genetic analyses demonstrate that Fbxl10 DNA binding capability and integration into PRC1 are required for H2AK119 ubiquitylation. ESCs lacking Fbxl10, like previously characterized Polycomb mutants, cannot differentiate properly. These results demonstrate that Fbxl10 has a key role in regulating Ring1B recruitment to its target genes and H2AK119 ubiquitylation in ESCs. [Display omitted] ► Fbxl10 binds to most CpG islands in ESCs ► Fbxl10 recruits Nspc1 and Ring1B to CpG islands ► The Fbxl10, Nspc1, and Ring1B complex is required for H2A monoubiquitylation ► Fbxl10 is required for proper ESC differentiation
AbstractList	Polycomb repressive complex 1 (PRC1) catalyzes lysine 119 monoubiquitylation on H2A (H2AK119ub1) and regulates pluripotency in embryonic stem cells (ESCs). However, the mechanisms controlling the binding of PRC1 to genomic sites and its catalytic activity are poorly understood. Here, we show that Fbxl10 interacts with Ring1B and Nspc1, forming a noncanonical PRC1 that is required for H2AK119ub1 in mouse ESCs. Genome-wide analyses reveal that Fbxl10 preferentially binds to CpG islands and colocalizes with Ring1B on Polycomb target genes. Notably, Fbxl10 depletion causes a decrease in Ring1B binding to target genes and a major loss of H2AK119ub1. Furthermore, genetic analyses demonstrate that Fbxl10 DNA binding capability and integration into PRC1 are required for H2AK119 ubiquitylation. ESCs lacking Fbxl10, like previously characterized Polycomb mutants, cannot differentiate properly. These results demonstrate that Fbxl10 has a key role in regulating Ring1B recruitment to its target genes and H2AK119 ubiquitylation in ESCs. Polycomb repressive complex 1 (PRC1) catalyzes lysine 119 monoubiquitylation on H2A (H2AK119ub1) and regulates pluripotency in embryonic stem cells (ESCs). However, the mechanisms controlling the binding of PRC1 to genomic sites and its catalytic activity are poorly understood. Here, we show that Fbxl10 interacts with Ring1B and Nspc1, forming a noncanonical PRC1 that is required for H2AK119ub1 in mouse ESCs. Genome-wide analyses reveal that Fbxl10 preferentially binds to CpG islands and colocalizes with Ring1B on Polycomb target genes. Notably, Fbxl10 depletion causes a decrease in Ring1B binding to target genes and a major loss of H2AK119ub1. Furthermore, genetic analyses demonstrate that Fbxl10 DNA binding capability and integration into PRC1 are required for H2AK119 ubiquitylation. ESCs lacking Fbxl10, like previously characterized Polycomb mutants, cannot differentiate properly. These results demonstrate that Fbxl10 has a key role in regulating Ring1B recruitment to its target genes and H2AK119 ubiquitylation in ESCs. Polycomb repressive complex 1 (PRC1) catalyzes lysine 119 monoubiquitylation on H2A (H2AK119ub1) and regulates pluripotency in embryonic stem cells (ESCs). However, the mechanisms controlling the binding of PRC1 to genomic sites and its catalytic activity are poorly understood. Here, we show that Fbxl10 interacts with Ring1B and Nspc1, forming a noncanonical PRC1 that is required for H2AK119ub1 in mouse ESCs. Genome-wide analyses reveal that Fbxl10 preferentially binds to CpG islands and colocalizes with Ring1B on Polycomb target genes. Notably, Fbxl10 depletion causes a decrease in Ring1B binding to target genes and a major loss of H2AK119ub1. Furthermore, genetic analyses demonstrate that Fbxl10 DNA binding capability and integration into PRC1 are required for H2AK119 ubiquitylation. ESCs lacking Fbxl10, like previously characterized Polycomb mutants, cannot differentiate properly. These results demonstrate that Fbxl10 has a key role in regulating Ring1B recruitment to its target genes and H2AK119 ubiquitylation in ESCs.Polycomb repressive complex 1 (PRC1) catalyzes lysine 119 monoubiquitylation on H2A (H2AK119ub1) and regulates pluripotency in embryonic stem cells (ESCs). However, the mechanisms controlling the binding of PRC1 to genomic sites and its catalytic activity are poorly understood. Here, we show that Fbxl10 interacts with Ring1B and Nspc1, forming a noncanonical PRC1 that is required for H2AK119ub1 in mouse ESCs. Genome-wide analyses reveal that Fbxl10 preferentially binds to CpG islands and colocalizes with Ring1B on Polycomb target genes. Notably, Fbxl10 depletion causes a decrease in Ring1B binding to target genes and a major loss of H2AK119ub1. Furthermore, genetic analyses demonstrate that Fbxl10 DNA binding capability and integration into PRC1 are required for H2AK119 ubiquitylation. ESCs lacking Fbxl10, like previously characterized Polycomb mutants, cannot differentiate properly. These results demonstrate that Fbxl10 has a key role in regulating Ring1B recruitment to its target genes and H2AK119 ubiquitylation in ESCs. Polycomb repressive complex 1 (PRC1) catalyzes lysine 119 monoubiquitylation on H2A (H2AK119ub1) and regulates pluripotency in embryonic stem cells (ESCs). However, the mechanisms controlling the binding of PRC1 to genomic sites and its catalytic activity are poorly understood. Here, we show that Fbxl10 interacts with Ring1B and Nspc1, forming a noncanonical PRC1 that is required for H2AK119ub1 in mouse ESCs. Genome-wide analyses reveal that Fbxl10 preferentially binds to CpG islands and colocalizes with Ring1B on Polycomb target genes. Notably, Fbxl10 depletion causes a decrease in Ring1B binding to target genes and a major loss of H2AK119ub1. Furthermore, genetic analyses demonstrate that Fbxl10 DNA binding capability and integration into PRC1 are required for H2AK119 ubiquitylation. ESCs lacking Fbxl10, like previously characterized Polycomb mutants, cannot differentiate properly. These results demonstrate that Fbxl10 has a key role in regulating Ring1B recruitment to its target genes and H2AK119 ubiquitylation in ESCs. [Display omitted] ► Fbxl10 binds to most CpG islands in ESCs ► Fbxl10 recruits Nspc1 and Ring1B to CpG islands ► The Fbxl10, Nspc1, and Ring1B complex is required for H2A monoubiquitylation ► Fbxl10 is required for proper ESC differentiation
Author	Helin, Kristian Wu, Xudong Johansen, Jens Vilstrup
Author_xml	– sequence: 1 givenname: Xudong surname: Wu fullname: Wu, Xudong organization: Biotech Research and Innovation Centre, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen, Denmark – sequence: 2 givenname: Jens Vilstrup surname: Johansen fullname: Johansen, Jens Vilstrup organization: Biotech Research and Innovation Centre, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen, Denmark – sequence: 3 givenname: Kristian surname: Helin fullname: Helin, Kristian email: kristian.helin@bric.ku.dk organization: Biotech Research and Innovation Centre, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen, Denmark
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/23395003$$D View this record in MEDLINE/PubMed
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Cites_doi	10.1371/journal.pgen.1001244 10.1016/j.stem.2011.12.017 10.1038/nprot.2007.147 10.1038/nature08924 10.1016/j.molcel.2012.01.002 10.1128/MCB.01432-06 10.1016/j.cell.2008.07.020 10.1038/nature02985 10.1038/ncb1628 10.1016/j.cell.2006.02.043 10.1371/journal.pgen.1002774 10.1038/nature10066 10.1038/emboj.2011.399 10.1016/j.stem.2011.12.006 10.1038/sj.emboj.7601187 10.1371/journal.pgen.1000242 10.1371/journal.pgen.1002090 10.1038/nature09934 10.1083/jcb.200612127 10.1101/gad.381706 10.4161/epi.6.2.13640 10.1038/nature06008 10.1016/j.cell.2010.10.012 10.1038/nrc1991 10.1038/ng1817 10.1371/journal.pbio.1000013 10.1074/jbc.M110.194027 10.1016/j.molcel.2008.05.007 10.1038/nrc2736 10.1371/journal.pbio.0060253 10.1038/ncb1663 10.1016/j.molcel.2010.04.009 10.1016/j.cell.2007.05.042 10.1038/emboj.2011.383 10.1128/MCB.00630-06 10.1038/sj.emboj.7601144 10.1101/gad.544410 10.1038/nrm2763 10.1371/journal.pgen.1002494 10.1093/nar/gkn243 10.1038/ng.946 10.1101/gad.2037511 10.1016/j.molcel.2007.08.009 10.1038/nature04733 10.1371/journal.pone.0002235 10.1016/j.cell.2006.02.041 10.1101/gad.484208 10.1242/dev.033902 10.1038/nsmb.1499 10.1016/j.cell.2011.12.029
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References	Brookes, de Santiago, Hebenstreit, Morris, Carroll, Xie, Stock, Heidemann, Eick, Nozaki (bib8) 2012; 10 Bracken, Helin (bib7) 2009; 9 Ku, Koche, Rheinbay, Mendenhall, Endoh, Mikkelsen, Presser, Nusbaum, Xie, Chi (bib19) 2008; 4 Leeb, Wutz (bib22) 2007; 178 Marson, Levine, Cole, Frampton, Brambrink, Johnstone, Guenther, Johnston, Wernig, Newman (bib27) 2008; 134 Lee, Jenner, Boyer, Guenther, Levine, Kumar, Chevalier, Johnstone, Cole, Isono (bib21) 2006; 125 Blackledge, Klose (bib4) 2011; 6 Wu, Gong, Yue, Qiang, Yuan, Peng (bib47) 2008; 36 Mohn, Weber, Rebhan, Roloff, Richter, Stadler, Bibel, Schübeler (bib30) 2008; 30 Wang, Wang, Erdjument-Bromage, Vidal, Tempst, Jones, Zhang (bib45) 2004; 431 Blackledge, Zhou, Tolstorukov, Farcas, Park, Klose (bib5) 2010; 38 Boyer, Plath, Zeitlinger, Brambrink, Medeiros, Lee, Levine, Wernig, Tajonar, Ray (bib6) 2006; 441 Thomson, Skene, Selfridge, Clouaire, Guy, Webb, Kerr, Deaton, Andrews, James (bib43) 2010; 464 Gao, Zhang, Bonasio, Strino, Sawai, Parisi, Kluger, Reinberg (bib14) 2012; 45 Elderkin, Maertens, Endoh, Mallery, Morrice, Koseki, Peters, Brockdorff, Hiom (bib12) 2007; 28 Leeb, Pasini, Novatchkova, Jaritz, Helin, Wutz (bib23) 2010; 24 Schuettengruber, Ganapathi, Leblanc, Portoso, Jaschek, Tolhuis, van Lohuizen, Tanay, Cavalli (bib36) 2009; 7 Bibel, Richter, Lacroix, Barde (bib3) 2007; 2 Bracken, Dietrich, Pasini, Hansen, Helin (bib50) 2006; 20 Lienert, Wirbelauer, Som, Dean, Mohn, Schübeler (bib25) 2011; 43 Morey, Pascual, Cozzuto, Roma, Wutz, Benitah, Di Croce (bib31) 2012; 10 Schmitz, Albert, Malatesta, Morey, Johansen, Bak, Tommerup, Abarrategui, Helin (bib33) 2011; 30 Simon, Kingston (bib39) 2009; 10 Wu, D’Alessio, Ito, Xia, Wang, Cui, Zhao, Sun, Zhang (bib48) 2011; 473 Silva, Barrandon, Nichols, Kawaguchi, Theunissen, Smith (bib38) 2008; 6 Guenther, Levine, Boyer, Jaenisch, Young (bib16) 2007; 130 Koyama-Nasu, David, Tanese (bib18) 2007; 9 Bernstein, Mikkelsen, Xie, Kamal, Huebert, Cuff, Fry, Meissner, Wernig, Plath (bib2) 2006; 125 Lagarou, Mohd-Sarip, Moshkin, Chalkley, Bezstarosti, Demmers, Verrijzer (bib20) 2008; 22 van der Stoop, Boutsma, Hulsman, Noback, Heimerikx, Kerkhoven, Voncken, Wessels, van Lohuizen (bib44) 2008; 3 Dietrich, Lerdrup, Landt, Agrawal-Singh, Bak, Tommerup, Rappsilber, Södersten, Hansen (bib11) 2012; 8 Yuan, Xu, Huang, Liu, Chen, Zhu (bib49) 2011; 286 Mendenhall, Koche, Truong, Zhou, Issac, Chi, Ku, Bernstein (bib28) 2010; 6 Buchwald, van der Stoop, Weichenrieder, Perrakis, van Lohuizen, Sixma (bib9) 2006; 25 Tavares, Dimitrova, Oxley, Webster, Poot, Demmers, Bezstarosti, Taylor, Ura, Koide (bib42) 2012; 148 Mikkelsen, Ku, Jaffe, Issac, Lieberman, Giannoukos, Alvarez, Brockman, Kim, Koche (bib29) 2007; 448 Stock, Giadrossi, Casanova, Brookes, Vidal, Koseki, Brockdorff, Fisher, Pombo (bib41) 2007; 9 Endoh, Endo, Endoh, Isono, Sharif, Ohara, Toyoda, Ito, Eskeland, Bickmore (bib13) 2012; 8 Deaton, Bird (bib10) 2011; 25 Lienert, Mohn, Tiwari, Baubec, Roloff, Gaidatzis, Stadler, Schübeler (bib24) 2011; 7 Bartke, Vermeulen, Xhemalce, Robson, Mann, Kouzarides (bib1) 2010; 143 Sparmann, van Lohuizen (bib40) 2006; 6 Schoeftner, Sengupta, Kubicek, Mechtler, Spahn, Koseki, Jenuwein, Wutz (bib34) 2006; 25 He, Kallin, Tsukada, Zhang (bib17) 2008; 15 Schuettengruber, Cavalli (bib35) 2009; 136 Lynch, Smith, De Gobbi, Flenley, Hughes, Vernimmen, Ayyub, Sharpe, Sloane-Stanley, Sutherland (bib26) 2012; 31 Schwartz, Kahn, Nix, Li, Bourgon, Biggin, Pirrotta (bib37) 2006; 38 Gearhart, Corcoran, Wamstad, Bardwell (bib15) 2006; 26 Pasini, Bracken, Hansen, Capillo, Helin (bib32) 2007; 27 Williams, Christensen, Pedersen, Johansen, Cloos, Rappsilber, Helin (bib46) 2011; 473 Elderkin (10.1016/j.molcel.2013.01.016_bib12) 2007; 28 Guenther (10.1016/j.molcel.2013.01.016_bib16) 2007; 130 Boyer (10.1016/j.molcel.2013.01.016_bib6) 2006; 441 Gearhart (10.1016/j.molcel.2013.01.016_bib15) 2006; 26 Morey (10.1016/j.molcel.2013.01.016_bib31) 2012; 10 Blackledge (10.1016/j.molcel.2013.01.016_bib5) 2010; 38 Simon (10.1016/j.molcel.2013.01.016_bib39) 2009; 10 He (10.1016/j.molcel.2013.01.016_bib17) 2008; 15 Lee (10.1016/j.molcel.2013.01.016_bib21) 2006; 125 Endoh (10.1016/j.molcel.2013.01.016_bib13) 2012; 8 Dietrich (10.1016/j.molcel.2013.01.016_bib11) 2012; 8 Leeb (10.1016/j.molcel.2013.01.016_bib23) 2010; 24 Stock (10.1016/j.molcel.2013.01.016_bib41) 2007; 9 Schoeftner (10.1016/j.molcel.2013.01.016_bib34) 2006; 25 Yuan (10.1016/j.molcel.2013.01.016_bib49) 2011; 286 Lynch (10.1016/j.molcel.2013.01.016_bib26) 2012; 31 Leeb (10.1016/j.molcel.2013.01.016_bib22) 2007; 178 Tavares (10.1016/j.molcel.2013.01.016_bib42) 2012; 148 Gao (10.1016/j.molcel.2013.01.016_bib14) 2012; 45 Lagarou (10.1016/j.molcel.2013.01.016_bib20) 2008; 22 Mendenhall (10.1016/j.molcel.2013.01.016_bib28) 2010; 6 Wang (10.1016/j.molcel.2013.01.016_bib45) 2004; 431 Mikkelsen (10.1016/j.molcel.2013.01.016_bib29) 2007; 448 Marson (10.1016/j.molcel.2013.01.016_bib27) 2008; 134 van der Stoop (10.1016/j.molcel.2013.01.016_bib44) 2008; 3 Pasini (10.1016/j.molcel.2013.01.016_bib32) 2007; 27 Bibel (10.1016/j.molcel.2013.01.016_bib3) 2007; 2 Lienert (10.1016/j.molcel.2013.01.016_bib25) 2011; 43 Buchwald (10.1016/j.molcel.2013.01.016_bib9) 2006; 25 Bernstein (10.1016/j.molcel.2013.01.016_bib2) 2006; 125 Schuettengruber (10.1016/j.molcel.2013.01.016_bib35) 2009; 136 Blackledge (10.1016/j.molcel.2013.01.016_bib4) 2011; 6 Lienert (10.1016/j.molcel.2013.01.016_bib24) 2011; 7 Bracken (10.1016/j.molcel.2013.01.016_bib7) 2009; 9 Schmitz (10.1016/j.molcel.2013.01.016_bib33) 2011; 30 Thomson (10.1016/j.molcel.2013.01.016_bib43) 2010; 464 Sparmann (10.1016/j.molcel.2013.01.016_bib40) 2006; 6 Williams (10.1016/j.molcel.2013.01.016_bib46) 2011; 473 Wu (10.1016/j.molcel.2013.01.016_bib47) 2008; 36 Schwartz (10.1016/j.molcel.2013.01.016_bib37) 2006; 38 Bracken (10.1016/j.molcel.2013.01.016_bib50) 2006; 20 Schuettengruber (10.1016/j.molcel.2013.01.016_bib36) 2009; 7 Bartke (10.1016/j.molcel.2013.01.016_bib1) 2010; 143 Ku (10.1016/j.molcel.2013.01.016_bib19) 2008; 4 Brookes (10.1016/j.molcel.2013.01.016_bib8) 2012; 10 Deaton (10.1016/j.molcel.2013.01.016_bib10) 2011; 25 Silva (10.1016/j.molcel.2013.01.016_bib38) 2008; 6 Koyama-Nasu (10.1016/j.molcel.2013.01.016_bib18) 2007; 9 Wu (10.1016/j.molcel.2013.01.016_bib48) 2011; 473 Mohn (10.1016/j.molcel.2013.01.016_bib30) 2008; 30 23541037 - Mol Cell. 2013 Mar 28;49(6):1019-20
References_xml	– volume: 441 start-page: 349 year: 2006 end-page: 353 ident: bib6 article-title: Polycomb complexes repress developmental regulators in murine embryonic stem cells publication-title: Nature – volume: 130 start-page: 77 year: 2007 end-page: 88 ident: bib16 article-title: A chromatin landmark and transcription initiation at most promoters in human cells publication-title: Cell – volume: 143 start-page: 470 year: 2010 end-page: 484 ident: bib1 article-title: Nucleosome-interacting proteins regulated by DNA and histone methylation publication-title: Cell – volume: 464 start-page: 1082 year: 2010 end-page: 1086 ident: bib43 article-title: CpG islands influence chromatin structure via the CpG-binding protein Cfp1 publication-title: Nature – volume: 10 start-page: 157 year: 2012 end-page: 170 ident: bib8 article-title: Polycomb associates genome-wide with a specific RNA polymerase II variant, and regulates metabolic genes in ESCs publication-title: Cell Stem Cell – volume: 178 start-page: 219 year: 2007 end-page: 229 ident: bib22 article-title: Ring1B is crucial for the regulation of developmental control genes and PRC1 proteins but not X inactivation in embryonic cells publication-title: J. Cell Biol. – volume: 24 start-page: 265 year: 2010 end-page: 276 ident: bib23 article-title: Polycomb complexes act redundantly to repress genomic repeats and genes publication-title: Genes Dev. – volume: 9 start-page: 1074 year: 2007 end-page: 1080 ident: bib18 article-title: The F-box protein Fbl10 is a novel transcriptional repressor of c-Jun publication-title: Nat. Cell Biol. – volume: 45 start-page: 344 year: 2012 end-page: 356 ident: bib14 article-title: PCGF homologs, CBX proteins, and RYBP define functionally distinct PRC1 family complexes publication-title: Mol. Cell – volume: 286 start-page: 7983 year: 2011 end-page: 7989 ident: bib49 article-title: H3K36 methylation antagonizes PRC2-mediated H3K27 methylation publication-title: J. Biol. Chem. – volume: 136 start-page: 3531 year: 2009 end-page: 3542 ident: bib35 article-title: Recruitment of polycomb group complexes and their role in the dynamic regulation of cell fate choice publication-title: Development – volume: 20 start-page: 1123 year: 2006 end-page: 1136 ident: bib50 article-title: Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions publication-title: Genes Dev – volume: 43 start-page: 1091 year: 2011 end-page: 1097 ident: bib25 article-title: Identification of genetic elements that autonomously determine DNA methylation states publication-title: Nat. Genet. – volume: 6 start-page: 147 year: 2011 end-page: 152 ident: bib4 article-title: CpG island chromatin: a platform for gene regulation publication-title: Epigenetics – volume: 38 start-page: 700 year: 2006 end-page: 705 ident: bib37 article-title: Genome-wide analysis of Polycomb targets in Drosophila melanogaster publication-title: Nat. Genet. – volume: 15 start-page: 1169 year: 2008 end-page: 1175 ident: bib17 article-title: The H3K36 demethylase Jhdm1b/Kdm2b regulates cell proliferation and senescence through p15(Ink4b) publication-title: Nat. Struct. Mol. Biol. – volume: 6 start-page: e1001244 year: 2010 ident: bib28 article-title: GC-rich sequence elements recruit PRC2 in mammalian ES cells publication-title: PLoS Genet. – volume: 26 start-page: 6880 year: 2006 end-page: 6889 ident: bib15 article-title: Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets publication-title: Mol. Cell. Biol. – volume: 30 start-page: 4586 year: 2011 end-page: 4600 ident: bib33 article-title: Jarid1b targets genes regulating development and is involved in neural differentiation publication-title: EMBO J. – volume: 8 start-page: e1002494 year: 2012 ident: bib11 article-title: REST-mediated recruitment of polycomb repressor complexes in mammalian cells publication-title: PLoS Genet. – volume: 431 start-page: 873 year: 2004 end-page: 878 ident: bib45 article-title: Role of histone H2A ubiquitination in Polycomb silencing publication-title: Nature – volume: 25 start-page: 1010 year: 2011 end-page: 1022 ident: bib10 article-title: CpG islands and the regulation of transcription publication-title: Genes Dev. – volume: 6 start-page: 846 year: 2006 end-page: 856 ident: bib40 article-title: Polycomb silencers control cell fate, development and cancer publication-title: Nat. Rev. Cancer – volume: 22 start-page: 2799 year: 2008 end-page: 2810 ident: bib20 article-title: dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing publication-title: Genes Dev. – volume: 134 start-page: 521 year: 2008 end-page: 533 ident: bib27 article-title: Connecting microRNA genes to the core transcriptional regulatory circuitry of embryonic stem cells publication-title: Cell – volume: 448 start-page: 553 year: 2007 end-page: 560 ident: bib29 article-title: Genome-wide maps of chromatin state in pluripotent and lineage-committed cells publication-title: Nature – volume: 9 start-page: 1428 year: 2007 end-page: 1435 ident: bib41 article-title: Ring1-mediated ubiquitination of H2A restrains poised RNA polymerase II at bivalent genes in mouse ES cells publication-title: Nat. Cell Biol. – volume: 125 start-page: 315 year: 2006 end-page: 326 ident: bib2 article-title: A bivalent chromatin structure marks key developmental genes in embryonic stem cells publication-title: Cell – volume: 6 start-page: e253 year: 2008 ident: bib38 article-title: Promotion of reprogramming to ground state pluripotency by signal inhibition publication-title: PLoS Biol. – volume: 125 start-page: 301 year: 2006 end-page: 313 ident: bib21 article-title: Control of developmental regulators by Polycomb in human embryonic stem cells publication-title: Cell – volume: 7 start-page: e1002090 year: 2011 ident: bib24 article-title: Genomic prevalence of heterochromatic H3K9me2 and transcription do not discriminate pluripotent from terminally differentiated cells publication-title: PLoS Genet. – volume: 38 start-page: 179 year: 2010 end-page: 190 ident: bib5 article-title: CpG islands recruit a histone H3 lysine 36 demethylase publication-title: Mol. Cell – volume: 473 start-page: 389 year: 2011 end-page: 393 ident: bib48 article-title: Dual functions of Tet1 in transcriptional regulation in mouse embryonic stem cells publication-title: Nature – volume: 3 start-page: e2235 year: 2008 ident: bib44 article-title: Ubiquitin E3 ligase Ring1b/Rnf2 of polycomb repressive complex 1 contributes to stable maintenance of mouse embryonic stem cells publication-title: PLoS ONE – volume: 30 start-page: 755 year: 2008 end-page: 766 ident: bib30 article-title: Lineage-specific polycomb targets and de novo DNA methylation define restriction and potential of neuronal progenitors publication-title: Mol. Cell – volume: 28 start-page: 107 year: 2007 end-page: 120 ident: bib12 article-title: A phosphorylated form of Mel-18 targets the Ring1B histone H2A ubiquitin ligase to chromatin publication-title: Mol. Cell – volume: 36 start-page: 3590 year: 2008 end-page: 3599 ident: bib47 article-title: Cooperation between EZH2, NSPc1-mediated histone H2A ubiquitination and Dnmt1 in HOX gene silencing publication-title: Nucleic Acids Res. – volume: 9 start-page: 773 year: 2009 end-page: 784 ident: bib7 article-title: Polycomb group proteins: navigators of lineage pathways led astray in cancer publication-title: Nat. Rev. Cancer – volume: 2 start-page: 1034 year: 2007 end-page: 1043 ident: bib3 article-title: Generation of a defined and uniform population of CNS progenitors and neurons from mouse embryonic stem cells publication-title: Nat. Protoc. – volume: 10 start-page: 47 year: 2012 end-page: 62 ident: bib31 article-title: Nonoverlapping functions of the Polycomb group Cbx family of proteins in embryonic stem cells publication-title: Cell Stem Cell – volume: 31 start-page: 317 year: 2012 end-page: 329 ident: bib26 article-title: An interspecies analysis reveals a key role for unmethylated CpG dinucleotides in vertebrate Polycomb complex recruitment publication-title: EMBO J. – volume: 473 start-page: 343 year: 2011 end-page: 348 ident: bib46 article-title: TET1 and hydroxymethylcytosine in transcription and DNA methylation fidelity publication-title: Nature – volume: 10 start-page: 697 year: 2009 end-page: 708 ident: bib39 article-title: Mechanisms of polycomb gene silencing: knowns and unknowns publication-title: Nat. Rev. Mol. Cell Biol. – volume: 25 start-page: 3110 year: 2006 end-page: 3122 ident: bib34 article-title: Recruitment of PRC1 function at the initiation of X inactivation independent of PRC2 and silencing publication-title: EMBO J. – volume: 25 start-page: 2465 year: 2006 end-page: 2474 ident: bib9 article-title: Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b publication-title: EMBO J. – volume: 7 start-page: e13 year: 2009 ident: bib36 article-title: Functional anatomy of polycomb and trithorax chromatin landscapes in Drosophila embryos publication-title: PLoS Biol. – volume: 27 start-page: 3769 year: 2007 end-page: 3779 ident: bib32 article-title: The polycomb group protein Suz12 is required for embryonic stem cell differentiation publication-title: Mol. Cell. Biol. – volume: 4 start-page: e1000242 year: 2008 ident: bib19 article-title: Genomewide analysis of PRC1 and PRC2 occupancy identifies two classes of bivalent domains publication-title: PLoS Genet. – volume: 148 start-page: 664 year: 2012 end-page: 678 ident: bib42 article-title: RYBP-PRC1 complexes mediate H2A ubiquitylation at polycomb target sites independently of PRC2 and H3K27me3 publication-title: Cell – volume: 8 start-page: e1002774 year: 2012 ident: bib13 article-title: Histone H2A mono-ubiquitination is a crucial step to mediate PRC1-dependent repression of developmental genes to maintain ES cell identity publication-title: PLoS Genet. – volume: 6 start-page: e1001244 year: 2010 ident: 10.1016/j.molcel.2013.01.016_bib28 article-title: GC-rich sequence elements recruit PRC2 in mammalian ES cells publication-title: PLoS Genet. doi: 10.1371/journal.pgen.1001244 – volume: 10 start-page: 157 year: 2012 ident: 10.1016/j.molcel.2013.01.016_bib8 article-title: Polycomb associates genome-wide with a specific RNA polymerase II variant, and regulates metabolic genes in ESCs publication-title: Cell Stem Cell doi: 10.1016/j.stem.2011.12.017 – volume: 2 start-page: 1034 year: 2007 ident: 10.1016/j.molcel.2013.01.016_bib3 article-title: Generation of a defined and uniform population of CNS progenitors and neurons from mouse embryonic stem cells publication-title: Nat. Protoc. doi: 10.1038/nprot.2007.147 – volume: 464 start-page: 1082 year: 2010 ident: 10.1016/j.molcel.2013.01.016_bib43 article-title: CpG islands influence chromatin structure via the CpG-binding protein Cfp1 publication-title: Nature doi: 10.1038/nature08924 – volume: 45 start-page: 344 year: 2012 ident: 10.1016/j.molcel.2013.01.016_bib14 article-title: PCGF homologs, CBX proteins, and RYBP define functionally distinct PRC1 family complexes publication-title: Mol. Cell doi: 10.1016/j.molcel.2012.01.002 – volume: 27 start-page: 3769 year: 2007 ident: 10.1016/j.molcel.2013.01.016_bib32 article-title: The polycomb group protein Suz12 is required for embryonic stem cell differentiation publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.01432-06 – volume: 134 start-page: 521 year: 2008 ident: 10.1016/j.molcel.2013.01.016_bib27 article-title: Connecting microRNA genes to the core transcriptional regulatory circuitry of embryonic stem cells publication-title: Cell doi: 10.1016/j.cell.2008.07.020 – volume: 431 start-page: 873 year: 2004 ident: 10.1016/j.molcel.2013.01.016_bib45 article-title: Role of histone H2A ubiquitination in Polycomb silencing publication-title: Nature doi: 10.1038/nature02985 – volume: 9 start-page: 1074 year: 2007 ident: 10.1016/j.molcel.2013.01.016_bib18 article-title: The F-box protein Fbl10 is a novel transcriptional repressor of c-Jun publication-title: Nat. Cell Biol. doi: 10.1038/ncb1628 – volume: 125 start-page: 301 year: 2006 ident: 10.1016/j.molcel.2013.01.016_bib21 article-title: Control of developmental regulators by Polycomb in human embryonic stem cells publication-title: Cell doi: 10.1016/j.cell.2006.02.043 – volume: 8 start-page: e1002774 year: 2012 ident: 10.1016/j.molcel.2013.01.016_bib13 article-title: Histone H2A mono-ubiquitination is a crucial step to mediate PRC1-dependent repression of developmental genes to maintain ES cell identity publication-title: PLoS Genet. doi: 10.1371/journal.pgen.1002774 – volume: 473 start-page: 343 year: 2011 ident: 10.1016/j.molcel.2013.01.016_bib46 article-title: TET1 and hydroxymethylcytosine in transcription and DNA methylation fidelity publication-title: Nature doi: 10.1038/nature10066 – volume: 31 start-page: 317 year: 2012 ident: 10.1016/j.molcel.2013.01.016_bib26 article-title: An interspecies analysis reveals a key role for unmethylated CpG dinucleotides in vertebrate Polycomb complex recruitment publication-title: EMBO J. doi: 10.1038/emboj.2011.399 – volume: 10 start-page: 47 year: 2012 ident: 10.1016/j.molcel.2013.01.016_bib31 article-title: Nonoverlapping functions of the Polycomb group Cbx family of proteins in embryonic stem cells publication-title: Cell Stem Cell doi: 10.1016/j.stem.2011.12.006 – volume: 25 start-page: 3110 year: 2006 ident: 10.1016/j.molcel.2013.01.016_bib34 article-title: Recruitment of PRC1 function at the initiation of X inactivation independent of PRC2 and silencing publication-title: EMBO J. doi: 10.1038/sj.emboj.7601187 – volume: 4 start-page: e1000242 year: 2008 ident: 10.1016/j.molcel.2013.01.016_bib19 article-title: Genomewide analysis of PRC1 and PRC2 occupancy identifies two classes of bivalent domains publication-title: PLoS Genet. doi: 10.1371/journal.pgen.1000242 – volume: 7 start-page: e1002090 year: 2011 ident: 10.1016/j.molcel.2013.01.016_bib24 article-title: Genomic prevalence of heterochromatic H3K9me2 and transcription do not discriminate pluripotent from terminally differentiated cells publication-title: PLoS Genet. doi: 10.1371/journal.pgen.1002090 – volume: 473 start-page: 389 year: 2011 ident: 10.1016/j.molcel.2013.01.016_bib48 article-title: Dual functions of Tet1 in transcriptional regulation in mouse embryonic stem cells publication-title: Nature doi: 10.1038/nature09934 – volume: 178 start-page: 219 year: 2007 ident: 10.1016/j.molcel.2013.01.016_bib22 article-title: Ring1B is crucial for the regulation of developmental control genes and PRC1 proteins but not X inactivation in embryonic cells publication-title: J. Cell Biol. doi: 10.1083/jcb.200612127 – volume: 20 start-page: 1123 year: 2006 ident: 10.1016/j.molcel.2013.01.016_bib50 article-title: Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions publication-title: Genes Dev doi: 10.1101/gad.381706 – volume: 6 start-page: 147 year: 2011 ident: 10.1016/j.molcel.2013.01.016_bib4 article-title: CpG island chromatin: a platform for gene regulation publication-title: Epigenetics doi: 10.4161/epi.6.2.13640 – volume: 448 start-page: 553 year: 2007 ident: 10.1016/j.molcel.2013.01.016_bib29 article-title: Genome-wide maps of chromatin state in pluripotent and lineage-committed cells publication-title: Nature doi: 10.1038/nature06008 – volume: 143 start-page: 470 year: 2010 ident: 10.1016/j.molcel.2013.01.016_bib1 article-title: Nucleosome-interacting proteins regulated by DNA and histone methylation publication-title: Cell doi: 10.1016/j.cell.2010.10.012 – volume: 6 start-page: 846 year: 2006 ident: 10.1016/j.molcel.2013.01.016_bib40 article-title: Polycomb silencers control cell fate, development and cancer publication-title: Nat. Rev. Cancer doi: 10.1038/nrc1991 – volume: 38 start-page: 700 year: 2006 ident: 10.1016/j.molcel.2013.01.016_bib37 article-title: Genome-wide analysis of Polycomb targets in Drosophila melanogaster publication-title: Nat. Genet. doi: 10.1038/ng1817 – volume: 7 start-page: e13 year: 2009 ident: 10.1016/j.molcel.2013.01.016_bib36 article-title: Functional anatomy of polycomb and trithorax chromatin landscapes in Drosophila embryos publication-title: PLoS Biol. doi: 10.1371/journal.pbio.1000013 – volume: 286 start-page: 7983 year: 2011 ident: 10.1016/j.molcel.2013.01.016_bib49 article-title: H3K36 methylation antagonizes PRC2-mediated H3K27 methylation publication-title: J. Biol. Chem. doi: 10.1074/jbc.M110.194027 – volume: 30 start-page: 755 year: 2008 ident: 10.1016/j.molcel.2013.01.016_bib30 article-title: Lineage-specific polycomb targets and de novo DNA methylation define restriction and potential of neuronal progenitors publication-title: Mol. Cell doi: 10.1016/j.molcel.2008.05.007 – volume: 9 start-page: 773 year: 2009 ident: 10.1016/j.molcel.2013.01.016_bib7 article-title: Polycomb group proteins: navigators of lineage pathways led astray in cancer publication-title: Nat. Rev. Cancer doi: 10.1038/nrc2736 – volume: 6 start-page: e253 year: 2008 ident: 10.1016/j.molcel.2013.01.016_bib38 article-title: Promotion of reprogramming to ground state pluripotency by signal inhibition publication-title: PLoS Biol. doi: 10.1371/journal.pbio.0060253 – volume: 9 start-page: 1428 year: 2007 ident: 10.1016/j.molcel.2013.01.016_bib41 article-title: Ring1-mediated ubiquitination of H2A restrains poised RNA polymerase II at bivalent genes in mouse ES cells publication-title: Nat. Cell Biol. doi: 10.1038/ncb1663 – volume: 38 start-page: 179 year: 2010 ident: 10.1016/j.molcel.2013.01.016_bib5 article-title: CpG islands recruit a histone H3 lysine 36 demethylase publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.04.009 – volume: 130 start-page: 77 year: 2007 ident: 10.1016/j.molcel.2013.01.016_bib16 article-title: A chromatin landmark and transcription initiation at most promoters in human cells publication-title: Cell doi: 10.1016/j.cell.2007.05.042 – volume: 30 start-page: 4586 year: 2011 ident: 10.1016/j.molcel.2013.01.016_bib33 article-title: Jarid1b targets genes regulating development and is involved in neural differentiation publication-title: EMBO J. doi: 10.1038/emboj.2011.383 – volume: 26 start-page: 6880 year: 2006 ident: 10.1016/j.molcel.2013.01.016_bib15 article-title: Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.00630-06 – volume: 25 start-page: 2465 year: 2006 ident: 10.1016/j.molcel.2013.01.016_bib9 article-title: Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b publication-title: EMBO J. doi: 10.1038/sj.emboj.7601144 – volume: 24 start-page: 265 year: 2010 ident: 10.1016/j.molcel.2013.01.016_bib23 article-title: Polycomb complexes act redundantly to repress genomic repeats and genes publication-title: Genes Dev. doi: 10.1101/gad.544410 – volume: 10 start-page: 697 year: 2009 ident: 10.1016/j.molcel.2013.01.016_bib39 article-title: Mechanisms of polycomb gene silencing: knowns and unknowns publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm2763 – volume: 8 start-page: e1002494 year: 2012 ident: 10.1016/j.molcel.2013.01.016_bib11 article-title: REST-mediated recruitment of polycomb repressor complexes in mammalian cells publication-title: PLoS Genet. doi: 10.1371/journal.pgen.1002494 – volume: 36 start-page: 3590 year: 2008 ident: 10.1016/j.molcel.2013.01.016_bib47 article-title: Cooperation between EZH2, NSPc1-mediated histone H2A ubiquitination and Dnmt1 in HOX gene silencing publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkn243 – volume: 43 start-page: 1091 year: 2011 ident: 10.1016/j.molcel.2013.01.016_bib25 article-title: Identification of genetic elements that autonomously determine DNA methylation states publication-title: Nat. Genet. doi: 10.1038/ng.946 – volume: 25 start-page: 1010 year: 2011 ident: 10.1016/j.molcel.2013.01.016_bib10 article-title: CpG islands and the regulation of transcription publication-title: Genes Dev. doi: 10.1101/gad.2037511 – volume: 28 start-page: 107 year: 2007 ident: 10.1016/j.molcel.2013.01.016_bib12 article-title: A phosphorylated form of Mel-18 targets the Ring1B histone H2A ubiquitin ligase to chromatin publication-title: Mol. Cell doi: 10.1016/j.molcel.2007.08.009 – volume: 441 start-page: 349 year: 2006 ident: 10.1016/j.molcel.2013.01.016_bib6 article-title: Polycomb complexes repress developmental regulators in murine embryonic stem cells publication-title: Nature doi: 10.1038/nature04733 – volume: 3 start-page: e2235 year: 2008 ident: 10.1016/j.molcel.2013.01.016_bib44 article-title: Ubiquitin E3 ligase Ring1b/Rnf2 of polycomb repressive complex 1 contributes to stable maintenance of mouse embryonic stem cells publication-title: PLoS ONE doi: 10.1371/journal.pone.0002235 – volume: 125 start-page: 315 year: 2006 ident: 10.1016/j.molcel.2013.01.016_bib2 article-title: A bivalent chromatin structure marks key developmental genes in embryonic stem cells publication-title: Cell doi: 10.1016/j.cell.2006.02.041 – volume: 22 start-page: 2799 year: 2008 ident: 10.1016/j.molcel.2013.01.016_bib20 article-title: dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing publication-title: Genes Dev. doi: 10.1101/gad.484208 – volume: 136 start-page: 3531 year: 2009 ident: 10.1016/j.molcel.2013.01.016_bib35 article-title: Recruitment of polycomb group complexes and their role in the dynamic regulation of cell fate choice publication-title: Development doi: 10.1242/dev.033902 – volume: 15 start-page: 1169 year: 2008 ident: 10.1016/j.molcel.2013.01.016_bib17 article-title: The H3K36 demethylase Jhdm1b/Kdm2b regulates cell proliferation and senescence through p15(Ink4b) publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.1499 – volume: 148 start-page: 664 year: 2012 ident: 10.1016/j.molcel.2013.01.016_bib42 article-title: RYBP-PRC1 complexes mediate H2A ubiquitylation at polycomb target sites independently of PRC2 and H3K27me3 publication-title: Cell doi: 10.1016/j.cell.2011.12.029 – reference: 23541037 - Mol Cell. 2013 Mar 28;49(6):1019-20
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Snippet	Polycomb repressive complex 1 (PRC1) catalyzes lysine 119 monoubiquitylation on H2A (H2AK119ub1) and regulates pluripotency in embryonic stem cells (ESCs)....
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SubjectTerms	active sites Animals catalytic activity Cell Differentiation Cell Line CpG Islands DNA embryonic stem cells Embryonic Stem Cells - enzymology Embryonic Stem Cells - physiology Epigenesis, Genetic F-Box Proteins - physiology genes genetic techniques and protocols Genome genomic islands Histones - metabolism Humans Jumonji Domain-Containing Histone Demethylases - physiology lysine Mice Models, Molecular mutants Polycomb Repressive Complex 1 - metabolism Protein Binding Protein Structure, Tertiary Protein Transport Transcription Initiation Site Transcription, Genetic Ubiquitin-Protein Ligases - metabolism Ubiquitination
Title	Fbxl10/Kdm2b Recruits Polycomb Repressive Complex 1 to CpG Islands and Regulates H2A Ubiquitylation
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