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A PRC2-independent function for EZH2 in regulating rRNA 2′-O methylation and IRES-dependent translation

ABSTRACT: A PRC2-independent function for EZH2 in regulating rRNA 2′-O methylation and IRES-dependent translation

PROVIDER: PRJNA667336 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR10918466.fastq.gz	Fastqsanger.gz
	SRR10918467.fastq.gz	Fastqsanger.gz
	SRR10918468.fastq.gz	Fastqsanger.gz
	SRR10918469.fastq.gz	Fastqsanger.gz
	SRR10918470.fastq.gz	Fastqsanger.gz

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A PRC2-independent function for EZH2 in regulating rRNA 2′-O methylation and IRES-dependent translation

Project description:Overactivated ribosome biogenesis is a common feature of cancer. However, the underlying molecular mechanism remains elusive. Herein, we report enhancer of zeste homolog 2 (EZH2), a histone methyltransferase, could interact with fibrillarin (FBL) directly in the nucleolus. While loss of EZH2 does not impact FBL-mediated histone H2AQ104 methylation (H2AQ104me) and 18S rRNA processing, EZH2 is proved to be involved in rRNA 2′-O methylation in a manner dependent of its interaction with FBL. Mechanistically, EZH2 strengthens the fibrillarin (FBL)-NOP56 interaction by binding to both proteins and thus facilitates the assembly of box C/D small nucleolar ribonucleoprotein (box C/D snoRNP). Strikingly, EZH2 deficiency alters translational efficiency and reduces internal ribosome entry site (IRES) activity of key oncogenes in prostate cancer. In summary, our findings reveal a novel non-methyltransferase role of EZH2 that mediates FBL functions, which may provide more options for the development of EZH2-targeting curative strategies in cancer.

2020-12-10 | GSE143975 | GEO

A PRC2-independent function for EZH2 in regulating rRNA 2′-O methylation and IRES-dependent translation

2020-12-10 | GSE159004 | GEO

A PRC2-independent function for EZH2 in regulating rRNA 2′-O methylation and IRES-dependent translation

Project description:A PRC2-independent function for EZH2 in regulating rRNA 2′-O methylation and IRES-dependent translation

| PRJNA602407 | ENA

A PRC2-independent function for EZH2 in regulating rRNA 2′-O methylation and IRES-dependent translation

Project description:A PRC2-independent function for EZH2 in regulating rRNA 2′-O methylation and IRES-dependent translation

| PRJNA667337 | ENA

A PRC2-independent function for EZH2 in regulating rRNA 2'-O methylation and IRES-dependent translation.

Project description:Dysregulated translation is a common feature of cancer. Uncovering its governing factors and underlying mechanism are important for cancer therapy. Here, we report that enhancer of zeste homologue 2 (EZH2), previously known as a transcription repressor and lysine methyltransferase, can directly interact with fibrillarin (FBL) to exert its role in translational regulation. We demonstrate that EZH2 enhances rRNA 2'-O methylation via its direct interaction with FBL. Mechanistically, EZH2 strengthens the FBL-NOP56 interaction and facilitates the assembly of box C/D small nucleolar ribonucleoprotein. Strikingly, EZH2 deficiency impairs the translation process globally and reduces internal ribosome entry site (IRES)-dependent translation initiation in cancer cells. Our findings reveal a previously unrecognized role of EZH2 in cancer-related translational regulation.

| S-EPMC8162121 | biostudies-literature

A PRC2-independent function for EZH2 in regulating rRNA 2′-O methylation and IRES-dependent translation

Project description:This SuperSeries is composed of the SubSeries listed below.

2020-12-10 | GSE159005 | GEO

Analysis of the methylation state of K510, K514 and K515 of human EZH2 within recombinant PRC2

Project description:Using mass-spectrometry, we are seeking to determine the extent of methylation of EZH2 K510, K514 and K515 in the above mentioned recombinant PRC2 variants, answering the question whether recombinant mutant PRC2 is automethylated to the same or similar extent as the wt PRC2 complex.

2024-09-11 | PXD051876 | Pride

Jarid2 and PRC2, Partner in Regulating Gene Expression

Project description:The Polycomb Group proteins foster gene repression profiles required for proper development and unimpaired adulthood, and comprise the components of the PRC2 complex including the histone H3 lysine 27 (H3K27) methyltransferase Ezh2. How mammalian PRC2 accesses chromatin is unclear. We find that Jarid2 associates with PRC2 and stimulates its enzymatic activity in vitro. Jarid2 contains a Jumonji C domain, but is devoid of detectable histone demethylase activity. Instead, its artificial recruitment to a promoter in vivo resulted in co-recruitment of PRC2 with resultant increased levels of H3K27me2/3. Jarid2 co-localizes with Ezh2 and MTF2, a homologue of Drosophila Pcl, at endogenous genes in ES cells. Jarid2 can itself bind DNA and its recruitment in ES cells is interdependent with that of PRC2 as Jarid2 knockdown reduced PRC2 at its target promoters, and ES cells devoid of the PRC2 component EED are deficient in Jarid2 promoter access. In addition to the well-documented defects in embryonic viability upon down-regulation of Jarid2, ES cell differentiation is impaired, as is Oct4 silencing. Examination of two factors in ES cells

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Affinify Purification of EZH2 and phosphodeficient EZH2 identifies phosphorylation dependent interactions of EZH2

Project description:Overexpression of EZH2 in estrogen receptor negative (ER-) breast cancer promotes metastasis. EZH2 has been mainly studied as the catalytic component of the Polycomb Repressive Complex 2 (PRC2) that mediates gene repression by trimethylating histone H3 at lysine 27 (H3K27me3). However, how EZH2 drives metastasis despite the low H3K27me3 levels observed in ER- breast cancer is unknown. We have shown that in human invasive carcinomas and distant metastases, cytoplasmic EZH2 phosphorylated at T367 is significantly associated with ER- disease and low H3K27me3 levels. Here, we explore the interactome of EZH2 and of a phosphodeficient mutant EZH2_T367A. We identified novel interactors of EZH2, and identified interactions that are dependent on the phosphorylation and cellular localization of EZH2 that may play a role in EZH2 dependent metastatic progression.

2018-07-03 | PXD010073 | Pride

EZH2 inhibition results in genome-wide PRC2 redistribution in cancer cell models

Project description:Upon EZH2 inhibitor treatment, PRC2 components EZH2 and SUZ12 are redistributed across the genome towards a small number of genomic loci that are refractory to H3K27me3 loss. Focal PRC2 accumulation and H3K27me3 retention occur primarily at CpG islands and transcription start sites of genes, with enrichment at canonical PRC2 nucleation sites. EZH2 and SUZ12 are present at low levels at actively transcribed TSSs, and this signal is lost with EZH2 inhibition.

2019-08-09 | GSE134136 | GEO

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