Residential College | false |
Status | 已發表Published |
Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNA | |
Syuzo Kaneko1,2; Gang Li1,2; Jinsook Son2; Chong-Feng Xu3; Raphael Margueron4; Thomas A. Neubert3; Danny Reinberg1,2 | |
2010 | |
Source Publication | GENES & DEVELOPMENT |
ISSN | 0890-9369 |
Volume | 24Issue:23Pages:2615–2620 |
Abstract | Ezh2 functions as a histone H3 Lys 27 (H3K27) methyltransferase when comprising the Polycomb-Repressive Complex 2 (PRC2). Trimethylation of H3K27 (H3K27me3) correlates with transcriptionally repressed chromatin. The means by which PRC2 targets specific chromatin regions is currently unclear, but noncoding RNAs (ncRNAs) have been shown to interact with PRC2 and may facilitate its recruitment to some target genes. Here we show that Ezh2 interacts with HOTAIR and Xist. Ezh2 is phosphorylated by cyclin-dependent kinase 1 (CDK1) at threonine residues 345 and 487 in a cell cycle-dependent manner. A phospho-mimic at residue 345 increased HOTAIR ncRNA binding to Ezh2, while the phospho-mimic at residue 487 was ineffectual. An Ezh2 domain comprising T345 was found to be important for binding to HOTAIR and the 5′ end of Xist. |
Keyword | Prc2 Ezh2 Phosphorylation Noncoding Rna |
DOI | 10.1101/gad.1983810 |
Indexed By | SCIE |
Language | 英語English |
WOS Research Area | Cell Biology ; Developmental Biology ; Genetics & Heredity |
WOS Subject | Cell Biology ; Developmental Biology ; Genetics & Heredity |
WOS ID | WOS:000284835800005 |
Scopus ID | 2-s2.0-78649807567 |
Fulltext Access | |
Citation statistics | |
Document Type | Journal article |
Collection | Faculty of Health Sciences |
Corresponding Author | Danny Reinberg |
Affiliation | 1.Howard Hughes Medical Institute, New York University School of Medicine, New York, New York 10016, USA 2.Department of Biochemistry, New York University School of Medicine, New York, New York 10016, USA 3.Department of Pharmacology, Kimmel Center for Biology and Medicine, Skirball Institute, New York University School of Medicine, New York, New York 10016, USA 4.Research Center Unité de Génétique et Biologie du Développement, Curie Institute, 75248 Paris Cedex 05, France |
Recommended Citation GB/T 7714 | Syuzo Kaneko,Gang Li,Jinsook Son,et al. Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNA[J]. GENES & DEVELOPMENT, 2010, 24(23), 2615–2620. |
APA | Syuzo Kaneko., Gang Li., Jinsook Son., Chong-Feng Xu., Raphael Margueron., Thomas A. Neubert., & Danny Reinberg (2010). Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNA. GENES & DEVELOPMENT, 24(23), 2615–2620. |
MLA | Syuzo Kaneko,et al."Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNA".GENES & DEVELOPMENT 24.23(2010):2615–2620. |
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