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Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer

ABSTRACT: Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer

PROVIDER: PRJNA678634 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR13065900.fastq.gz	Fastqsanger.gz
	SRR13065901.fastq.gz	Fastqsanger.gz
	SRR13065902.fastq.gz	Fastqsanger.gz
	SRR13065903.fastq.gz	Fastqsanger.gz
	SRR13065904.fastq.gz	Fastqsanger.gz

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Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [RNA-Seq]

Project description:FOXA1 transcription factor is essential for the development and maturation of prostate luminal epithelial cells. FOXA1 gene is frequently mutated and its expression is deregulated during prostate cancer progression. We and others have shown that FOXA1 induces androgen-dependent cell growth by transcriptional regulation of target genes related to cell cycle process, DNA replication, cell division, and apoptosis. Despite of its important roles, how FOXA1 expression itself is regulated in prostate cancer cells remains largely unknown. Here we report that EZH2 methylates one of the lysine residues (K295) on FOXA1 protein to reduce its ubiquitination and subsequent degradation. Mechanistically, this EZH2-mediated FOXA1 methylation recruits BUB3/USP7 deubiquitinase complex to remove FOXA1 ubiquitination for increased protein stability.

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Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [ChIP-Seq]

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Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [RNA-Seq]

Project description:Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [RNA-Seq]

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Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [ChIP-Seq]

Project description:Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [ChIP-Seq]

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Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer

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

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Posttranslational regulation of FOXA1 by Polycomb and BUB3/USP7 deubiquitin complex in prostate cancer.

Project description:Forkhead box protein A1 (FOXA1) is essential for androgen-dependent prostate cancer (PCa) growth. However, how FOXA1 levels are regulated remains elusive and its therapeutic targeting proven challenging. Here, we report FOXA1 as a nonhistone substrate of enhancer of zeste homolog 2 (EZH2), which methylates FOXA1 at lysine-295. This methylation is recognized by WD40 repeat protein BUB3, which subsequently recruits ubiquitin-specific protease 7 (USP7) to remove ubiquitination and enhance FOXA1 protein stability. They functionally converge in regulating cell cycle genes and promoting PCa growth. FOXA1 is a major therapeutic target of the inhibitors of EZH2 methyltransferase activities in PCa. FOXA1-driven PCa growth can be effectively mitigated by EZH2 enzymatic inhibitors, either alone or in combination with USP7 inhibitors. Together, our study reports EZH2-catalyzed methylation as a key mechanism to FOXA1 protein stability, which may be leveraged to enhance therapeutic targeting of PCa using enzymatic EZH2 inhibitors.

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Usp7 protects genomic stability by regulating Bub3.

Project description:USP7 (Ubiquitin Specific processing Protease-7) is a deubiquitinase which, over the past decade emerged as a critical regulator of cellular processes. Deregulation of USP7 activity has been linked to cancer, making USP7 inhibition an appealing anti-cancer strategy. The identification of novel USP7 substrates and additional USP7-dependent cellular activities will broaden our knowledge towards potential clinical application of USP7 inhibitors. Results presented in this study uncover a novel and pivotal function of USP7 in the maintenance of genomic stability. Upon USP7 depletion we observed prolonged mitosis and mitotic abnormalities including micronuclei accumulation, lagging chromosomes and karyotype instability. Inhibition of USP7 with small molecule inhibitors stabilizes cyclin B and causes mitotic abnormalities. Our results suggest that these USP7-dependent effects are mediated by decreased levels of spindle assembly checkpoint (SAC) component Bub3, which we characterized as an interacting partner and substrate of USP7. In silico analysis across the NCI-60 panels of cell lines supports our results where lower levels of USP7 strongly correlate with genomic instability. In conclusion, we identified a novel role of USP7 as regulator of the SAC component Bub3 and genomic stability.

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(ChIP-seq) USP7 regulates the ncPRC1 Polycomb axis to stimulate genomic H2AK119ub1 deposition uncoupled from H3K27me3

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