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Aurora B and INCENP co-overexpression severely disrupts mitosis and distinctly modifies the global transcriptional landscape [ChIP-seq]

ABSTRACT: Aurora B and INCENP co-overexpression severely disrupts mitosis and distinctly modifies the global transcriptional landscape [ChIP-seq]

PROVIDER: PRJNA1142597 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR30058620_1.fastq.gz	Fastqsanger.gz
	SRR30058620_2.fastq.gz	Fastqsanger.gz
	SRR30058621_1.fastq.gz	Fastqsanger.gz
	SRR30058621_2.fastq.gz	Fastqsanger.gz
	SRR30058622_1.fastq.gz	Fastqsanger.gz

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Aurora B and INCENP co-overexpression severely disrupts mitosis and distinctly modifies the global transcriptional landscape

Project description:Aurora B and INCENP co-overexpression severely disrupts mitosis and distinctly modifies the global transcriptional landscape

| PRJNA1142593 | ENA

Aurora B and INCENP co-overexpression severely disrupts mitosis and distinctly modifies the global transcriptional landscape [RNA-seq]

Project description:Aurora B and INCENP co-overexpression severely disrupts mitosis and distinctly modifies the global transcriptional landscape [RNA-seq]

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Aurora B and INCENP co-overexpression severely disrupts mitosis and distinctly modifies the global transcriptional landscape [ChIP-seq]

Project description:Aurora B kinase, as part of the chromosomal passenger complex (CPC), controls key processes during the cell cycle such as DNA compaction, genome partitioning or cytokinesis. Nonetheless, increased Aurora B levels are a potential threat for the cells and have been linked to different tumor types. We have carried out an exhaustive characterization of the global consequences of the overexpression of Aurora B and INCENP, the scaffold of the CPC and an activator of Aurora B kinase activity, in non-transformed human cells. Our data demonstrate, not only that an individual increase in the levels of Aurora B or INCENP have a different impact on the cells, but more importantly that their simultaneous overexpression stabilizes both CPC components, exacerbates Aurora B activity, severely impairs mitotic progression and chromosome dynamics, and has a distinctive and more dramatic effect on the transcriptional landscape of the cells.

2025-05-06 | GSE273668 | GEO

Aurora B and INCENP co-overexpression severely disrupts mitosis and distinctly modifies the global transcriptional landscape [RNA-seq]

2025-05-06 | GSE273663 | GEO

Aurora B and INCENP co-overexpression severely disrupts mitosis and distinctly modifies the global transcriptional landscape

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

2025-05-06 | GSE273674 | GEO

Aurora B phosphorylates hnRNP U/SAF-A to facilitate XIST RNA removal from the inactive X chromosome during mitosis

Project description:We show that Aurora-B phosphorylates heterogeneous nuclear ribonucleoprotein U (hnRNP U) in the SAP domain to dissociate hnRNP U from chromatin during mitosis. We use RNA-seq to show that hnRNP U associates with hundreds of mRNAs and lncRNAs during interphase and mitosis.

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Aurora A Kinase Inhibition Induces Accumulation of Tumor Cells in Mitosis with Restored Interferon Signaling to Potentiate Response to PD-L1 Immune Checkpoint Blockade [RNA-seq]

Project description:By arresting tumor cells in mitosis, aurora A kinase inhibition restores interferon signaling in small cell lung cancer tumor cells and cooperates with PD-L1 immune checkpoint blockade.

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Aurora A Kinase Inhibition Induces Accumulation of Tumor Cells in Mitosis with Restored Interferon Signaling to Potentiate Response to PD-L1 Immune Checkpoint Blockade [single cell RNA-seq]

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Preferential phosphorylation on old histones during early mitosis in human cells

Project description:How histone posttranslational modifications (PTMs) are inherited through cell cycle remains poorly understood. Canonical histones are made in the S phase of cell cycle. Combining mass spectrometry-based technologies and stable isotope labeling by amino acids in cell culture (SILAC), we interrogate the distributions of multiple major histone PTMs on old versus new histones in synchronized human cells. We show that histone PTMs can be grouped to three categories accordingly to their distributions. Most lysine mono-methylation and acetylation PTMs are either symmetrically distributed on old and new histones, or asymmetric on new histones. In contrast, most di- and tri-methylation PTMs are asymmetric on old histones, suggesting the inheritance of different PTMs is regulated distinctly. Intriguingly, old and new histones are distinguished in their phosphorylation status during early mitosis, in three different human cell types: Hela, 293T and human foreskin fibroblast (HFF) cells. The mitotic hallmark H3S10ph is predominantly associated with old H3 at early mitosis and become symmetric with the progression of mitosis. The same distribution pattern is found on other mitotic histone phosphorylation marks, including H3T3/T6ph, H3.1/2S28ph and H1.4S26ph, excluding S28/S31ph on the H3 variant H3.3. Although H3S10ph often associates with the neighboring K9 di- or tri-methylation, they are not required for the asymmetric distribution of S10ph on the same H3 tail. Inhibition of the kinase Aurora B does not change the distribution pattern despite significant reduction of H3S10ph levels. K9me2 abundance on the new H3 is significantly reduced after Aurora B inhibition, suggesting a crosstalk between H3S10ph and H3K9me2.

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Redox priming promotes Aurora A activation during mitosis

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2020-06-28 | MSV000085641 | MassIVE

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