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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 PublicationGENES & DEVELOPMENT
ISSN0890-9369
Volume24Issue: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.

KeywordPrc2 Ezh2 Phosphorylation Noncoding Rna
DOIhttps://doi.org/10.1101/gad.1983810
Indexed BySCIE
Language英語English
WOS Research AreaCell Biology ; Developmental Biology ; Genetics & Heredity
WOS SubjectCell Biology ; Developmental Biology ; Genetics & Heredity
WOS IDWOS:000284835800005
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Cited Times [WOS]:299   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionFaculty of Health Sciences
Corresponding AuthorDanny Reinberg
Affiliation1.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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