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IPO11 regulates the nuclear import of BZW1/2 and is necessary for AML cells and stem cells

ABSTRACT: IPO11 regulates the nuclear import of BZW1/2 and is necessary for AML cells and stem cells

PROVIDER: PRJNA730535 | ENA |

REPOSITORIES: ENA

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IPO11 regulates the nuclear import of BZW1/2 and is necessary for AML cells and stem cells [ChIP-seq]

Project description:IPO11 regulates the nuclear import of BZW1/2 and is necessary for AML cells and stem cells [ChIP-seq]

| PRJNA730540 | ENA

IPO11 regulates the nuclear import of BZW1/2 and is necessary for AML cells and stem cells [RNA-Seq]

Project description:IPO11 regulates the nuclear import of BZW1/2 and is necessary for AML cells and stem cells [RNA-Seq]

| PRJNA725126 | ENA

IPO11 regulates the nuclear import of BZW1/2 and is necessary for AML cells and stem cells [RNA-Seq]

Project description:Through a comparison between genes that are significant for growth and viability of AML cells by way of a CRISPR screen, with genes that are differentially expressed in leukemia stem cells, we identified importin 11 (IPO11) as a novel target in AML. In AML, knockdown of IPO11 decreased growth, reduced engraftment potential of stem cells and induced differentiation. Mechanistically, we identified the transcription factors BZW1 and BZW2 as novel cargoes of IPO11. We further show that BZW1/2 mediate a transcriptional signature that promotes stemness and survival of LSC.

2022-04-26 | GSE173288 | GEO

IPO11 regulates the nuclear import of BZW1/2 and is necessary for AML cells and stem cells [ChIP-seq]

2022-04-26 | GSE174559 | GEO

Mitochondrial carrier homolog 2 (MTCH2) is necessary for AML survival

Project description:Through a CRISPR screen to identify mitochondrial genes necessary for the growth of AML cells, we identified the mitochondrial outer membrane protein MTCH2 (Mitochondrial Carrier Homolog 2). In AML, knockdown of MTCH2 decreased growth, reduced engraftment potential of stem cells and induced differentiation. Inhibiting MTCH2 altered in AML cells increased nuclear pyruvate and pyruvate dehydrogenase that induced histone acetylation and subsequently promoted the differentiation of AML cells. Thus, we have defined a new mechanism by which mitochondria and metabolism regulate AML stem cells and gene expression.

2020-03-25 | GSE147508 | GEO

AKIRIN2 controls the nuclear import of proteasomes in vertebrates

Project description:Protein expression and turnover are controlled through a complex interplay of transcriptional, post-transcriptional and post-translational mechanisms to enable spatial and temporal regulation of cellular processes. To systematically elucidate such gene regulatory networks, we developed a CRISPR screening assay based on time-controlled Cas9 mutagenesis, intracellular immunostaining and fluorescence-activated cell sorting that enables the identification of regulatory factors independent of their effects on cellular fitness. We pioneered this approach by systematically probing the regulation of the transcription factor MYC, a master regulator of cell growth. Our screens uncover a highly conserved protein, AKIRIN2, that is essentially required for nuclear protein degradation. We found that AKIRIN2 forms homodimers that directly bind to fully assembled 20S proteasomes to mediate their nuclear import. During mitosis, proteasomes are excluded from condensing chromatin and re-imported into newly formed daughter nuclei in a highly dynamic, AKIRIN2-dependent process. Cells undergoing mitosis in the absence of AKIRIN2 become devoid of nuclear proteasomes, rapidly causing accumulation of MYC and other nuclear proteins. Collectively, our study reveals a dedicated pathway controlling the nuclear import of proteasomes in vertebrates and establishes a scalable approach to decipher regulators in essential cellular processes.

2021-08-27 | GSE157663 | GEO

AKIRIN2 controls the nuclear import of proteasomes in vertebrates

Project description:AKIRIN2 controls the nuclear import of proteasomes in vertebrates

| PRJNA662348 | ENA

Lower nuclear pore numbers in cardiomyocytes decrease nuclear import of signaling proteins, which restricts adaptive gene regulation, and improves cardiac stress response in vivo

Project description:Nuclear pores are essential pathways for nuclear-cytoplasmic transport of molecules. Whether and how cells change nuclear pores to alter nuclear transport and cellular function is unknown. Here, we show that heart muscle cells (cardiomyocytes) undergo a 63% decrease in nuclear pore numbers during differentiation, which alters their response to extracellular signals. This maturation-associated decline in nuclear pore numbers per nucleus is associated with lower nuclear levels and import of Mitogen-activated Protein Kinase (MAPK) signaling proteins. Experimental reduction of nuclear pore numbers decreased nuclear import of MAPK signaling proteins. In a mouse model of high blood pressure, reduction of cardiomyocyte nuclear pore numbers reduced adverse heart remodeling and gene regulation, which reduced progression to lethal heart failure. The observed decrease in nuclear pore numbers in cardiomyocyte differentiation and resulting functional changes suggest a paradigm by which terminally differentiated cells could permanently alter their handling of information flux across the nuclear envelope and, with that, their behavior.

2022-09-26 | GSE186949 | GEO

Transcriptomic analysis of mutant yeast strains deficient in Xrn1 nuclear import

Project description:The goal of the project was to study the transcription rates and mRNA levels, genome-wide, in several mutants in Xrn1 defetive in nuclear import. We used Genomic Run-On (GRO) experiment in wild type and xrn1 mutant strains.

2022-09-30 | GSE158250 | GEO

Nuclear Localization of Hog1 MAPK is Not Necessary for Resistance to Hyperosmotic Stress

Project description:In budding yeast, this signaling pathway— the high-osmolarity glycerol (HOG) response —culminates in dual phosphorylation and nuclear translocation of the MAPK, Hog1 (ortholog of mammalian p38/SAPK). Induction of at least 50 genes requires nuclear Hog1, implying that transcriptional up-regulation is necessary to cope with hyperosmotic stress. Contrary to this expectation, we found that cells lacking the karyopherin (Nmd5) required for Hog1 nuclear import or in which Hog1 was permanently anchored at the plasma membrane(HOG1-CCAAX) (or both) withstood hyperosmotic challenge by three different solutes (1 M sorbitol, KCl or NaCl). In cells where activated Hog1 is excluded from the nucleus, there was little change in transcriptional program after exposure to hyperosmotic shock (comparable to hog1∆ cells), as judged by examining several diagnostic mRNAs and by global transcript measurements using microarrays. Systematic genetic analysis ruled out the need for any transcription factor known to be influenced by Hog1 (Hot1, Msn2, Msn4, Sko1 and Smp1). Keywords: Time course of stress response gene expression array

2008-06-01 | GSE8703 | GEO

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