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Unknown,Transcriptomics,Genomics,Proteomics

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Characterization of the EZH2-MMSET histone methyltransferase regulatory axis in cancer

ABSTRACT: This SuperSeries is composed of the following subset Series: GSE41651: Characterization of the EZH2-MMSET histone methyltransferase regulatory axis in cancer [expression] GSE41652: Characterization of the EZH2-MMSET histone methyltransferase regulatory axis in cancer [ChIP-seq] Refer to individual Series

ORGANISM(S): Homo sapiens

SUBMITTER: Meng Zhao

PROVIDER: E-GEOD-41653 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Characterization of the EZH2-MMSET histone methyltransferase regulatory axis in cancer.

Asangani Irfan A IA Ateeq Bushra B Cao Qi Q Dodson Lois L Pandhi Mithil M Kunju Lakshmi P LP Mehra Rohit R Lonigro Robert J RJ Siddiqui Javed J Palanisamy Nallasivam N Wu Yi-Mi YM Cao Xuhong X Kim Jung H JH Zhao Meng M Qin Zhaohui S ZS Iyer Mathew K MK Maher Christopher A CA Kumar-Sinha Chandan C Varambally Sooryanarayana S Chinnaiyan Arul M AM

Molecular cell 20121115 1

Histone methyltransferases (HMTases), as chromatin modifiers, regulate the transcriptomic landscape in normal development as well in diseases such as cancer. Here, we molecularly order two HMTases, EZH2 and MMSET, that have established genetic links to oncogenesis. EZH2, which mediates histone H3K27 trimethylation and is associated with gene silencing, was shown to be coordinately expressed and function upstream of MMSET, which mediates H3K36 dimethylation and is associated with active transcrip ...[more]

PMID: 23159737

Similar Datasets

Characterization of the EZH2-MMSET histone methyltransferase regulatory axis in cancer [expression]

Project description:Histone methyltransferases (HMTases), as chromatin modifiers, regulate the transcriptomic landscape in normal development as well in diseases such as cancer. Here, we molecularly order two HMTases, EZH2 and MMSET that have established genetic links to oncogenesis. EZH2, which mediates histone H3K27 trimethylation and is associated with gene silencing, was shown to be coordinately expressed and function upstream of MMSET, which mediates H3K36 dimethylation and is associated with active transcription. We found that the EZH2-MMSET HMTase axis is coordinated by a microRNA network and that the oncogenic functions of EZH2 require MMSET activity. Together, these results suggest that the EZH2-MMSET HMTase axis coordinately functions as a master regulator of transcriptional repression, activation, and oncogenesis and may represent an attractive therapeutic target in cancer. LacZ control vs MMSET overexpression or MMSET DeltaSET overexpression in replicates

2012-11-15 | E-GEOD-41651 | biostudies-arrayexpress

Characterization of the EZH2-MMSET histone methyltransferase regulatory axis in cancer [ChIP-seq]

Project description:Histone methyltransferases (HMTases), as chromatin modifiers, regulate the transcriptomic landscape in normal development as well in diseases such as cancer. Here, we molecularly order two HMTases, EZH2 and MMSET that have established genetic links to oncogenesis. EZH2, which mediates histone H3K27 trimethylation and is associated with gene silencing, was shown to be coordinately expressed and function upstream of MMSET, which mediates H3K36 dimethylation and is associated with active transcription. We found that the EZH2-MMSET HMTase axis is coordinated by a microRNA network and that the oncogenic functions of EZH2 require MMSET activity. Together, these results suggest that the EZH2-MMSET HMTase axis coordinately functions as a master regulator of transcriptional repression, activation, and oncogenesis and may represent an attractive therapeutic target in cancer. Examination of H3K36me2 mark in control and stable EZH2 knockdown cells

2012-11-15 | E-GEOD-41652 | biostudies-arrayexpress

Characterization of the EZH2-MMSET histone methyltransferase regulatory axis in cancer [ChIP-seq]

2012-11-15 | GSE41652 | GEO

Characterization of the EZH2-MMSET histone methyltransferase regulatory axis in cancer [expression]

2012-11-15 | GSE41651 | GEO

The Central Role of EED in the Orchestration of Polycomb Group Complexes

Project description:Polycomb Repressive Complexes 1 and 2 (PRC1 and 2) play a critical role in the epigenetic regulation of transcription during cellular differentiation, stem cell pluripotency, and neoplastic progression1-3. Here we show that the Polycomb group protein EED, a core component of PRC2, physically interacts with and functions as part of the PRC1 complex. Components of PRC1 and PRC2 compete for EED binding. EED functions to recruit PRC1 to H3K27me3 loci and enhances PRC1 mediated H2A ubiquitin E3 ligase activity. Taken together, we uncover the integral role of EED as an epigenetic exchange factor coordinating the activities of PRC1 and 2. EED, uH2A, RING1A, RING1B, BMI1 and H3K27Me3 ChIP-seq in EED stable knockdown and control Scramble DU145 prostate cancer cell line

2014-01-23 | E-GEOD-42566 | biostudies-arrayexpress

MMSET alters EZH2 Binding in Myeloma Cells

Project description:We investigated EZH2 binding in the presence and absence of MMSET protein. MMSET overexpression in t(4;14)+ myeloma leads to global loss of H3K27 methylation and redistribution of EZH2 binding throughout the genome ChIP-seq for EZH2 in two cell types

2014-09-01 | E-GEOD-57632 | biostudies-arrayexpress

Therapeutic Targeting of BET Bromodomain Proteins in Castration-Resistant Prostate Cancer

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2014-04-25 | E-GEOD-55064 | biostudies-arrayexpress

MMSET alters EZH2 Binding in Myeloma Cells

2014-09-01 | GSE57632 | GEO

Project description:Characterization of the EZH2-MMSET histone methyltransferase regulatory axis in cancer

| PRJNA177816 | ENA

PCGF Homologs and RYBP Define Functionally Distinct PRC1 Family Complexes

Project description:The heterogeneous nature of mammalian PRC1 complexes has hindered our understanding of their biological functions. Here, we present a comprehensive proteomic and genomic analysis that uncovered six major groups of PRC1 complexes each containing a distinct PCGF subunit, a RING1A/B ubiquitin ligase, and a unique set of associated polypeptides. These PRC1 complexes differ in their genomic localization and only a small subset co-localize with H3K27me3. Further biochemical dissection revealed that the six PCGFM-bM-^@M-^SRING1A/B combinations form multiple complexes through association with RYBP or its homolog YAF2, which prevents the incorporation of other canonical PRC1 subunits such as CBX, PHC and SCM. Although both RYBP/YAF2- and CBX/PHC/SCM-containing complexes compact chromatin, only RYBP stimulates the activity of RING1B toward H2AK119ub1, suggesting a central role in PRC1 function. Knockdown of RYBP in ES cells compromised their ability to form embryoid bodies, likely because of defects in cell proliferation and maintenance of H2AK119ub1 level. ChIP-seq experiments of different PRC1 components were performed either on HA-tagged transgenic stable 293T-REx lines or on endogenous subunits using specific antibodies.

2012-02-09 | E-GEOD-34774 | biostudies-arrayexpress

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