Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNA

Kaneko, Syuzo; Li, Gang; Son, Jaesung; Xu, Chong-Feng; Margueron, Raphaël; Neubert, Thomas A.; Reinberg, Danny

doi:10.1101/gad.1983810

Cited by 350 publications

(416 citation statements)

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“…Surprisingly, the interaction with nascent transcripts does not result in local H3K27 methylation nor in Polycomb mediated gene silencing, suggesting that a nascent transcript may be acting as an inhibitor/evictor for PRC2 or as a decoy for 'functional' RNA-protein interaction. Similar to HP1, interaction between Ezh2 and RNAs seems to involve a domain containing a short stretch of basic amino acids [53]. While HP1 has longer and denser patches of K/Rs, short stretches of K/Rs are present in most nuclear proteins as part of nuclear localization signals.…”

Section: Rna and Histone Modification Binding Can Influence Each Othermentioning

confidence: 99%

“…As discussed above, sumoylation of lysine residues in the hinge region of mouse HP1α controls its binding to major satellite transcripts [34]. Besides, phosphorylation of Ezh2 is known to enhance its binding to HOTAIR lncRNA [53]. Secondly, the histone modification binding proteins may use different interaction modes or surfaces for the promiscuous vs. specific RNA interaction.…”

Section: Rna and Histone Modification Binding Can Influence Each Othermentioning

confidence: 99%

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RNAs — Physical and functional modulators of chromatin reader proteins

Hiragami-Hamada

Fischle

2014

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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The regulatory role of histone modifications with respect to the structure and function of chromatin is well known. Proteins and protein complexes establishing, erasing and binding these marks have been extensively studied. RNAs have only recently entered the picture of epigenetic regulation with the discovery of a vast number of long non-coding RNAs. Fast growing evidence suggests that such RNAs influence all aspects of histone modification biology. Here, we focus exclusively on the emerging functional interplay between RNAs and proteins that bind histone modifications. We discuss recent findings of reciprocally positive and negative regulations as well as summarize the current insights into the molecular mechanism directing these interactions. This article is part of a Special Issue entitled: Molecular mechanisms of histone modification function.

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Section: Rna and Histone Modification Binding Can Influence Each Othermentioning

confidence: 99%

Section: Rna and Histone Modification Binding Can Influence Each Othermentioning

confidence: 99%

RNAs — Physical and functional modulators of chromatin reader proteins

Hiragami-Hamada

Fischle

2014

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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“…The importance of PcG proteins in X-inactivation is suggested by the fact that the inactive X chromosome is enriched with H3K27me3 and H2AK119u1, which are posttranslational modifications mediated by Polycomb repressive complex (PRC) 2 and 1, respectively [48][49][50][51]. The recruitment of PRC2 complex in X-inactivation has been attributed to direct biochemical interaction of the catalytic subunit of the complex, Ezh2, with the A-repeats of Xist RNA [52] Mapping of the candidate RNA interaction domain of Ezh2 suggested that RNA binding requires site specific phosphorylation of Ezh2 [53]. Further to this, others have described an interaction between a different subunit of PRC2, Suz12, and Xist A-repeats [54].…”

Section: Rstbroyalsocietypublishingorg Phil Trans R Soc B 368: 2011mentioning

confidence: 99%

Advances in understanding chromosome silencing by the long non-coding RNA Xist

Sado

Brockdorff

2013

Phil. Trans. R. Soc. B

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In female mammals, one of the two X chromosomes becomes genetically silenced to compensate for dosage imbalance of X-linked genes between XX females and XY males. X chromosome inactivation (X-inactivation) is a classical model for epigenetic gene regulation in mammals and has been studied for half a century. In the last two decades, efforts have been focused on the X inactive-specific transcript ( Xist ) locus, discovered to be the master regulator of X-inactivation. The Xist gene produces a non-coding RNA that functions as the primary switch for X-inactivation, coating the X chromosome from which it is transcribed in cis . Significant progress has been made towards understanding how Xist is regulated at the onset of X-inactivation, but our understanding of the molecular basis of silencing mediated by Xist RNA has progressed more slowly. A picture has, however, begun to emerge, and new tools and resources hold out the promise of further advances to come. Here, we provide an overview of the current state of our knowledge, what is known about Xist RNA and how it may trigger chromosome silencing.

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“…28 Further, CDK1-mediated phosphorylation of Thr345 on mouse Ezh2 (human Thr350) controls interaction with HOTAIR and Xist non coding (nc) RNAs and recruitment to specific target genes. 29 Target amino acid residues of Ezh2 can therefore be envisaged as chromatin sensors for different extra-cellular conditions, acting by modulating several properties of the protein such as chromatin binding, interaction with other PRC components or transcription factors and enzymatic activity.…”

confidence: 99%