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Mutant p53 dysregulates gene transcription in human CD34+ cells [RNA-seq 3]

ABSTRACT: Mutant p53 dysregulates gene transcription in human CD34+ cells [RNA-seq 3]

PROVIDER: PRJNA1089569 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR28387256_1.fastq.gz	Fastqsanger.gz
	SRR28387256_2.fastq.gz	Fastqsanger.gz
	SRR28387257_1.fastq.gz	Fastqsanger.gz
	SRR28387257_2.fastq.gz	Fastqsanger.gz
	SRR28387258_1.fastq.gz	Fastqsanger.gz

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Mutant p53 dysregulates gene transcription in human CD34+ cells [RNA-seq 3]

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Mutant p53 dysregulates gene transcription in hematopoietic stem and progenitor cells [RNA-seq 2]

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Project description:Mutant p53 dysregulates gene transcription in hematopoietic stem and progenitor cells [RNA-seq 2]

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Mutant p53 dysregulates gene transcription in hematopoietic stem and progenitor cells [RNA-seq 1]

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Many ETS family transcription factors can recruit mutant p53, and interaction specificity patterns correlate with ETS gene expression changes in ovarian cancer

Project description:The tumor suppressor transcription factor p53 is mutated in nearly 50% of all cancer cases, and this frequency increases with stage and resistance to therapy. Hotspot p53 mutations lose direct DNA binding activity while gaining oncogenic function. These structural p53 mutants can bind to new regions of the genome via interactions with other transcription factors. One example is the ETS transcription factor ETS2, which was previously reported to bind mutant p53. Yet, a comprehensive understanding of mutant p53 association with the ETS family needs to be understood. Here, we compare mutant p53 interaction across 26 ETS transcription factors. Mutant p53 bound ETS proteins better than wild-type p53. All ETS proteins tested bound to mutant p53 to some extent, yet relative binding differed. The ETS DNA binding domain provided a common interaction interface, but strong binding required a second interaction domain. Genome-wide mapping found that the ETS protein ERG could recruit mutant p53 to regulatory regions of genes necessary for morphogenesis, locomotion, and androgen response in prostate cancer cells. Lastly, ETS factors that interact strongly with mutant p53 tend to be upregulated in p53 mutant ovarian cancer. These results suggest that multiple ETS proteins can work with mutant p53 in cancer.

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Mutant p53 cancers reprogram macrophages to tumor supporting macrophages via exosomal miR-1246

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26S proteasome is conserved, therapeutically relevant mediator of mutant p53 gain-of-function in cancer

Project description:Mutant p53 proteins, resulting form frequent TP53 tumor suppressor missense mutations, possess gain-of-function activities and are among the most widespread and robust oncoproteins in human tumors. They are potentially important but understudied therapeutic targets. No studies to date have distinguished common, therapeutically relevant mutant p53 gain-of-function effects, from effects specific to different mutant variants and cell backgrounds. Here we identify 26S proteasome machinery as the common downstream effector controlled by mutant p53s in Triple Negative Breast Cancer (TNBC - aggressive carcinomas with TP53 as the most frequently mutated locus) and conserved in other human cancers. We have identified this pathway using a combination of single-model, multi-method vertical analysis (whole cell proteome, RNA sequencing an ChIP sequencing) and multi-cell line, horizontal analysis of transcriptiomes. We found that different missense mutant p53s regardless of the cell background transcriptionaly activate whole 26S proteasome machinery. Proteasome activity is significantly increased in p53 mutant versus wild-type or knockdown/null status - in cellular and mouse models as well as in human breast tumors. Increased proteasome activity leads to inhibition of tumor suppressive pathways. The control of mutant p53 over proteasome transcription and activity results in the increased resistance to proteasome inhibitors. By combining the mutant p53 targeting agents and proteasome inhibitor we were able to overcome the “bounce-back” proteasome inhibitor resistance mechanism in mutant p53 bearing TNBC cells and xenografts in vivo.

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