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MBD2 regulates the progression and chemoresistance of cholangiocarcinoma through interaction with WDR5

ABSTRACT: MBD2 regulates the progression and chemoresistance of cholangiocarcinoma through interaction with WDR5

PROVIDER: PRJNA1151029 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR30339980_1.fastq.gz	Fastqsanger.gz
	SRR30339980_2.fastq.gz	Fastqsanger.gz
	SRR30339981_1.fastq.gz	Fastqsanger.gz
	SRR30339981_2.fastq.gz	Fastqsanger.gz

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MBD2 regulates the progression and chemoresistance of cholangiocarcinoma through interaction with WDR5

Project description:Background: Cholangiocarcinoma (CCA) is a high malignancy, rapid progression tumor of bile duct. Due to its chemoresistance, it always has an extremely poor prognosis. Therefore, it is still need to detailed elucidation the mechanisms of chemoresistance and find the therapeutic targets. Methods: We analysis the expression of MBD2 in CCA and normal bile duct tissues through public database and immunohistochemical (IHC). The role of MBD2 in CCA cells’ proliferation, migration, chemoresistance ability was validated through CCK-8, plate clone assay, wound healing assay, xenograft mice models. Besides, we construct a primary CCA mice model to further confirm the effect of MBD2. RNA-seq, co-IP-MS were used to find the mechanisms of MBD2 leading to chemoresistance. Results: MBD2 is up-regulated in CCA. It could promote the proliferation, migration and chemoresistance of CCA cells. Mechanistically, MBD2 could directly interact with WDR5, and binding to the promoter of ABCB1, then promote the tri-methylation of H3K4 in this region through KMT2A, active the expression of ABCB1. Knocking down of WDR5 or KMT2A could block the transcriptional activation of ABCB1 by MBD2. MM-102 is a molecular inhibitor that targets the interaction of WDR5 with KMT2A. MM-102 could inhibit the expression of ABCB1 in CCA cells, and decrease the chemoresistance of CCA to cisplatin. Conclusion: MBD2 promote the progress and chemoresistance of CCA through interact with WDR5. MM-102 could effectively block this procedure and enhance the sensitivity to cisplatin of CCA.

2024-09-30 | GSE275477 | GEO

WDR5 promotes histone deacetylation via direct interaction with HDAC2 in human CCA cells.

Project description:As an essential component of histone methyltransferase complex SET1/MLL, WDR5 participates in histone 3 lysine 4 methylation (H3K4me) and promotes transcription by generating an open chromatin structure and enabling better access to the transcriptional machinery. Moreover, WDR5 interacts with histone deacetylases (HDACs) to promotes histone deacetylation, which induces the compact state of nucleosome, thus represses DNA transcription. However, the modulation of WDR5 on histone methylation and acetylation is tissue- and context-specific, and this function has not been elucidated in cholangiocarcinoma yet.

2021-02-23 | GSE162968 | GEO

Interaction with WDR5 promotes target gene recognition and tumorigenesis by MYC

Project description:We report a comparison of the genome-wide binding patterns of MYC and WDR5, and the effects of a mutation in MYC (WBM) that disrupt the MYC-WDR5 interaction.

2015-03-30 | GSE60897 | GEO

Interaction with WDR5 promotes target gene recognition and tumorigenesis by MYC

Project description:We report a comparison of the genome-wide binding patterns of MYC and WDR5, and the effects of a mutation in MYC (WBM) that disrupt the MYC-WDR5 interaction. The experimental design included two distinct experimental strategies. For comparison of genome-wide binding patters of wild-type (WT) and WDR5 binding-deficient (WBM) MYC, HEK293 cells were engineered by retroviral transduction to express either FLAG-tagged WT-MYC, FLAG-tagged WBM-MYC, or an empty vector control ("vec") ChIP was performed on all samples using the anti-FLAG antibody, and co-precipitating DNAs subject to next-generation sequencing. Samples "2514-WPT-1_1", "2514-WPT-5_1" and "2514-WPT-13_1" are three independent biological replicates of ChIPs performed on the "vec" control cells (i.e., those not expressing any exogenous MYC). Samples "2514-WPT-2_1", "2514-WPT-6_1" and "2514-WPT-10_1" are three independent biological replicates of ChIPs performed on the WT-MYC expressing cells. "2514-WPT-3_1", "2514-WPT-7_1" and "2514-WPT-11_1" are three independent biological replicates of ChIPs performed on the WBM-MYC expressing cells. For comparison of these binding patterns with those of WDR5, we performed ChIP in HEK293 cells with either an antibody against WDR5, or with IgG (negative control). Samples "2514-WPT-23_1", "2514-WPT-25_1", and "2514-WPT-27_1" are independent biological replicates of ChIPs performed with the anti-WDR5 antibody. Samples "2514-WPT-24_1", "2514-WPT-26_1", and "2514-WPT-28_1" are independent biological replicates of ChIPs performed with the negative IgG control.

2015-03-30 | E-GEOD-60897 | biostudies-arrayexpress

Interaction with WDR5 recruits MYC to a small cohort of genes required for tumor onset and maintenance

Project description:The oncoprotein transcription factor MYC is overexpressed in the majority of human cancers. Key to its oncogenic activity is the ability of MYC to bind chromatin and regulate broad gene expression patterns that drive and maintain the tumorigenic state. The interaction of MYC with chromatin is absolutely dependent on interaction with MAX, but may also be facilitated by additional chromatin-resident proteins such as WDR5. If the role of these additional proteins can be understood, they could serve as novel focal points for therapeutically targeting MYC. To stringently challenge the role of WDR5 in MYC function, we developed a Burkitt's Lymphoma system that allows inducible and quantitative exchange of wild-type for mutant forms of MYC defective for interaction with WDR5 or MAX. Using this system, we show that WDR5 recruits MYC to a small cohort of genes, enriched in those encoding ribosome protein subunits, and demonstrate that disrupting the MYC-WDR5 interaction is as effective as disrupting interaction with MAX at preventing tumor initiation and promoting tumor regression in vivo. These findings show that WDR5 is connected to a central tumorigenic function of MYC and forecast that small molecule WDR5 inhibitors could be broadly effective anti-cancer agents.

2019-11-08 | GSE126207 | GEO

The WDR5 WIN site interactome

Project description:The WIN site of WDR5 is a druggable pocket that is crucial for WDR5 protein function and carries therapeutic potential for treating cancer. This study evaluates the protein interactions affected by small molecule blockade of the WIN site of WDR5. We find that PDPK1 directly binds the WIN site of WDR5, and we investigate this newfound interaction through proteomic, biochemical, and genomic methods.

2021-01-19 | GSE150400 | GEO

An ES cell–specific NuRD complex functions through interaction with Wdr5

Project description:The Nucleosome Remodeling and Deacetylase (NuRD) complex is a chromatin regulatory complex that functions as a transcriptional co-repressor in metazoans. The NuRD subunit Mbd3 is essential for targeting and assembly of a functional NuRD complex as well as embryonic stem cell (ESC) pluripotency. Three Mbd3 isoforms (Mbd3a, Mbd3b, and Mbd3c) are expressed in mouse. Here, we find that the Mbd3c isoform contains a unique 50–amino acid N-terminal region that is necessary for Mbd3c to specifically interact with the histone H3 binding protein Wdr5. Domain analyses of Wdr5 reveal that the Wdr5 H3K4/MLL binding pocket is required for interaction with Mbd3c. We find that while Mbd3c KO ESCs differentiate normally, Mbd3c is redundant with the Mbd3a and Mbd3b isoforms in regulation of gene expression and ESC pluripotency, with the unique Mbd3c N-terminus required for this redundancy. Together, our data characterize a novel NuRD complex variant that functions specifically in ESCs

2017-04-27 | GSE80708 | GEO

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Project description:Wdr5

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WDR5 facilitates cholangiocarcinoma metastasis and EMT by promoting HIF-1α accumulation via directly interaction with c-Myc and HDAC2-PHD2 axis

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