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Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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SMYD2 specificly regulate BIX-01294 induced TP53 target genes revealed by RNA-Seq

ABSTRACT: We characterized expression profilings of SMYD2 knockdown and control cells treated by BIX-01294 and Rapamycin. We used siRNAs to knockdown SMYD2 in HCT116 cells, and NC as control. We treated those cell lines with BIX-01294 and Rapamycin, and the expression profilings were perfomed by Illumina high throughput sequencing.

ORGANISM(S): Homo sapiens

SUBMITTER: Min Wu

PROVIDER: E-GEOD-61255 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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SMYD2 specificly regulate BIX-01294 induced TP53 target genes revealed by RNA-Seq

Project description:We characterized expression profilings of SMYD2 knockdown and control cells treated by BIX-01294 and Rapamycin.

2015-01-01 | GSE61255 | GEO

The effects of SMYD2 overexpression on ectopic RB in SAOS cells

Project description:Expression analysis of wild-type SAOS cells and SAOS cells transiently transfected with RB, SMYD2, or RB and SMYD2.

2011-01-01 | GSE22842 | GEO

Genome-wide maps of chromatin state of Smyd2 binding in renal epithelial cells

Project description:To identify potential transcriptional targets of Smyd2, we performed ChIP-sequencing (ChIP-seq) analysis in renal epithelial cells with an anti-Smyd2 antibody. We identified 91 potential Smyd2 target genes in Pkd1 wild type MEK cells and 116 potential Smyd2 target genes in Pkd1 null MEK cells. There were 14 genes identified in both Pkd1 wild type and null MEK cells. Thus, the number of potential Smyd2 target genes in Pkd1 null MEK cells are 116 - 14 = 102 genes

2017-08-30 | GSE97708 | GEO

The effects of SMYD2 overexpression on ectopic RB in SAOS cells

Project description:Expression analysis of wild-type SAOS cells and SAOS cells transiently transfected with RB, SMYD2, or RB and SMYD2. Four samples of wild-type, rb1, smyd2 and rb1-smyd2 were analyzed on the Human Genome U133 Plus 2.0 array.

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Chip-chip from MDA-MB-231 cells with SMYD2 and EZH2

Project description:The histone methyl transferase EZH2 and SMYD2 are master epigenetic regulators involved in histone methylation and gene transcription repression. Here, we report that SMYD2 and EZH2 may act as a complex in transcriptional regulation and are involved in the progression of breast cancer. ChIP-on-chip assays were performed to find unique promoters co-targeted by EZH2 and SMYD2 in MDA-MB-231 cells.

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Quantitative profiling of the enzymatic activity of the protein lysine mono-methyltransferase SMYD2 using SILAC-based proteomics

Project description:The significance of non-histone lysine methylation in cell biology and human disease is an emerging area of research exploration, and small molecule inhibitors that selectively and potently target “writers” and “erasers” of methyl-lysine, such as the protein lysine mono-methyltransferase SMYD2, are active areas of drug discovery. It is therefore essential to clarify the substrates of these enzymes in cellular contexts in order to advance and to correctly understand the cellular mechanism(s) of action of these targets. Here, using stable isotopic labelling of amino acids in cell culture (SILAC) coupled with immunoaffinity enrichment of mono-methyl-lysine (Kme1) peptides and mass spectrometry, we report the most comprehensive and large-scale proteomic study of protein mono-methylation, comprising a total of 1032 Kme1 sites identified in esophageal squamous cell carcinoma (ESCC) cells and 1861 Kme1 sites in ESCC cells overexpressing SMYD2. Among these sites was a subset of 35 robust Kme1 sites that were potently down-regulated by both shRNA-mediated knockdown of SMYD2 and LLY-507, a small molecule inhibitor of SMYD2. In addition, we report specific protein sequence motifs that were enriched in Kme1 sites and that were also directly regulated by endogenous SMYD2 activity, indicating that the diversity of SMYD2 substrate specificity of SMYD2 exceeds previous expectations. Furthermore, we reveal that BTF3 and PDAP1 are novel and direct substrates of SMYD2, as well as AHNAK and AHNAK2, two large and highly-repetitive proteins directly and extensively mono-methylated by SMYD2 at several lysine residues. Collectively, our findings provide novel quantitative and insights into the cellular activity and substrate recognition of SMYD2 as well as the global landscape and regulation of protein mono-methylation in cells.

2016-01-11 | PXD002405 | Pride

Methylation of the epigenetic regulator KMT2D by SMYD2 contributes to therapeutic response in hormone-dependent breast cancer [SMYD2_KD_RNA]

Project description:Activating mutations in PIK3CA, the gene encoding PI3Kα, are frequently found in estrogen receptor (ER+) breast cancer and the combination of the PI3K inhibitor alpelisib with the anti-ER agent fulvestrant is approved for therapy. We have uncovered a key role for the chromatin modifier KMT2D in regulating the ER-PI3K crosstalk. PI3Kα effectors, AKT and SGK, negatively regulate KMT2D through S1331 phosphorylation. When PI3K is inhibited, this regulatory event is lost, leading to increased chromatin recruitment of KMT2D and an upregulation of ER-dependent transcription. Here we discovered a previously undescribed methylation site on KMT2D, at K1330 directly adjacent to S1331, catalyzed by the lysine methyltransferase SMYD2. SMYD2 loss attenuates alpelisib-induced KMT2D chromatin binding. Accordingly, loss of SMYD2 abrogates alpelisib-induced changes in gene expression, including ER-dependent transcription. Knockdown or pharmacological inhibition of SMYD2 sensitizes breast cancer cells, patient-derived organoids, and tumors to PI3K/AKT inhibition and endocrine therapy in part through KMT2D K1330 methylation. Methyl dead knock-in clones of KMT2D phenocopy many of the effects of SMYD2 inhibition on cell and tumor growth, drug response, and transcriptional output. Together, our findings uncover a regulatory cross-talk between posttranslational modifications that plays an important role in fine-tuning the functions of KMT2D at the chromatin. This provides a rationale for epigenetic therapy using SMYD2 inhibitors in combination with PI3Kα/AKT inhibitors for the treatment of ER+/PIK3CA mutant breast cancer.

2024-05-04 | GSE253957 | GEO

Methylation of the epigenetic regulator KMT2D by SMYD2 contributes to therapeutic response in hormone-dependent breast cancer [KMT2D_ChIP_seq]

2024-05-04 | GSE255295 | GEO

Methylation of the epigenetic regulator KMT2D by SMYD2 contributes to therapeutic response in hormone-dependent breast cancer [KMT2D_KI_RNA]

2024-05-04 | GSE253958 | GEO

Transcription profiling of human embryonic kidney cells overexpressing SMYD2 to identify which genes are regulated by SMYD2 through its histone lysine methylation activity

Project description:Identification of SMYD2 target genes - The objective of this aim is to identify which genes are regulated by SMYD2 through its histone lysine methylation activity. It is well established that post-translational modification of nucleosomal histones (H2A, H2B, H3 and H4), such as methylation, acetylation and phosphorylation are central to the proper control of gene expression

2008-02-05 | E-MEXP-963 | biostudies-arrayexpress

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