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The MLL-Menin interaction is a molecular dependency in NUP98-rearranged AML [BioChIP-seq]

ABSTRACT: The MLL-Menin interaction is a molecular dependency in NUP98-rearranged AML [BioChIP-seq]

PROVIDER: PRJNA733037 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14664002_1.fastq.gz	Fastqsanger.gz
	SRR14664002_2.fastq.gz	Fastqsanger.gz
	SRR14664003_1.fastq.gz	Fastqsanger.gz
	SRR14664003_2.fastq.gz	Fastqsanger.gz
	SRR14664004_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

The MLL-Menin interaction is a molecular dependency in NUP98-rearranged AML

Project description:The MLL-Menin interaction is a molecular dependency in NUP98-rearranged AML

| PRJNA733040 | ENA

The Histone Acetyltransferase MOZ is a Molecular Dependency and Therapeutic Target in NUP98-Rearranged Acute Myeloid Leukemia

Project description:NUP98 fusion oncoproteins (FOs) are a hallmark of childhood acute myeloid leukemia (AML), and drive leukemogenesis through liquid-liquid phase separation-mediated nuclear condensate formation. However, the composition and consequences of NUP98 FO-associated condensates are incompletely understood. Here we show that histone acetyltransferase (HAT) complex proteins including MOZ associate with NUP98 FOs, and that BRPF1, an epigenetic writer that associates with MOZ is a molecular dependency in NUP98::KDM5A AML. Inactivation of Brpf1 as well as HAT complex member Moz, Hbo1, Brd1 or Meaf6 in Nup98::Kdm5a;Vav-Cre cells impaired fitness of NUP98-rearranged cells. MOZ inhibition decreased global H3K23ac levels, displaced FO from chromatin at the Meis1 locus, and led to myeloid cell differentiation. Additionally, MOZ inhibition decreased leukemic burden in multiple NUP98-rearranged leukemia xenograft models, synergized with Menin inhibitor treatment, and was efficacious in Menin inhibitor-resistant cells. In summary, we show that MOZ is a potentially targetable dependency in NUP98-rearranged AMLs. SIGNIFICANCE STATEMENT MOZ is a member of NUP98 FO condensates with key roles in leukemia phenotypes. MOZ inhibition is effective in multiple preclinical models, including those non-responsive to Menin inhibition. MOZ and Menin inhibition are synergistic in some NUP98-rearranged models, supporting clinical translation to improve outcomes of NUP98 FO-driven leukemias.

2025-06-03 | PXD058286 | Pride

The MLL-Menin interaction is a molecular dependency in NUP98-rearranged AML [RNA-Seq]

Project description:Using mouse and human models of NUP98-rearrranged leukemia, we demonstrate that inhibition of MLL-Menin impairs leukemogenic gene expression and disrupts chromatin binding of MLL1 and NUP98 fusion proteins at a critical subset of genes that is essential for sustaining the undifferentiated leukemia phenotype.

2022-06-01 | GSE175596 | GEO

The MLL-Menin interaction is a molecular dependency in NUP98-rearranged AML [ChIP-Seq]

2022-06-01 | GSE175595 | GEO

The MLL-Menin interaction is a molecular dependency in NUP98-rearranged AML [BioChIP-seq]

2022-06-01 | GSE175594 | GEO

The MLL-Menin interaction is a molecular dependency in NUP98-rearranged AML [RNA-Seq]

Project description:The MLL-Menin interaction is a molecular dependency in NUP98-rearranged AML [RNA-Seq]

| PRJNA733041 | ENA

The MLL-Menin interaction is a molecular dependency in NUP98-rearranged AML [ChIP-Seq]

Project description:The MLL-Menin interaction is a molecular dependency in NUP98-rearranged AML [ChIP-Seq]

| PRJNA733042 | ENA

The histone acetyltransferase MOZ is a molecular dependency and therapeutic target in NUP98-rearranged acute myeloid leukemia [WGS, ATACseq, CUT&RUN, scRNAseq]

Project description:NUP98 fusion oncoproteins (FOs) are a hallmark of childhood acute myeloid leukemia (AML), and drive leukemogenesis through liquid-liquid phase separation-mediated nuclear condensate formation. However, the composition and consequences of NUP98 FO-associated condensates are incompletely understood. Here we show that histone acetyltransferase (HAT) complex proteins including MOZ associate with NUP98 FOs, and that BRPF1, an epigenetic writer that associates with MOZ, is a molecular dependency in NUP98::KDM5A AML. Inactivation of Brpf1 as well as HAT complex member Moz, Hbo1, Brd1 or Meaf6 in Nup98::Kdm5a;Vav-Cre cells impaired fitness of NUP98-rearranged cells. MOZ acetyltransferase inhibition decreased global H3K23ac levels, displaced FO from chromatin at the Meis1 locus, and led to myeloid cell differentiation. Additionally, MOZ inhibition decreased leukemic burden in multiple NUP98-rearranged leukemia xenograft mouse models, synergized with Menin inhibitor treatment, and was efficacious in Menin inhibitor-resistant cells. In summary, we show that MOZ is a potentially targetable dependency in NUP98-rearranged AMLs.

2025-06-02 | GSE283096 | GEO

The MLL – Menin interaction is a therapeutic vulnerability in NUP98-rearranged AML

Project description:The MLL – Menin interaction is a therapeutic vulnerability in NUP98-rearranged AML

| PRJNA970807 | ENA

The MLL – Menin interaction is a therapeutic vulnerability in NUP98-rearranged AML

Project description:To investigate the effect of Menin inhibitor on patient-derived NUP98-r AML. We treated primary AML cells with Menin inhibitor in a Mesenchymal stem cell co-Culture platform. Then we charachterized global gene expression in treated AML cells upon treatment in two different time points, day7 and day12.

2023-05-14 | GSE232091 | GEO

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