Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Transcriptome analysis of NCC-IT-A3 cells by Barasertib treatment

ABSTRACT: During mitosis, the chromosomal passenger complex (CPC) that is formed by Aurora-B, INCENP, Survivin, and Borealin ensures the faithful segregation of the chromosomes into daughter cells. We previously have shown that CPC activity was terminated by the anaphase promoting complex/cyclosome (APC/C) and its cofactor Cdh1 via ubiquitylation of Borealin and Aurora-B during the G1 phase of somatic cells. On the other hand, protein levels of Borealin and Aurora-B were stable during cell cycle progression due to high levels of Emi1, which keep APC/CCdh1 inactive in embryonal carcinoma (EC) cells. During retinoic acid-induced differentiation of EC cells, these proteins were downregulated by APC/CCdh1-mediated ubiquitylation. Interestingly, CPC proteins form a complex with Aurora-B kinase activity even in interphase of EC cells. Significantly, inhibition of CPC activity by either knockdown of Borealin or Aurora-B and Aurora-B kinase inhibitor treatment induced spontaneous differentiation of EC cells. In conclusion, sustained CPC activity plays a critical role in maintenance of the undifferentiated state of pluripotent stem cells. We therefore propose an interphase role of the CPC in regulating embryonic pluripotency.

ORGANISM(S): Homo sapiens

PROVIDER: GSE179503 | GEO | 2021/07/09

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

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.

2020-09-02 | GSE87200 | GEO

Regulated interaction of ID2 with the anaphase-promoting complex links progression through mitosis with reactivation of cell-type-specific transcription

Project description:Tissue-specific transcriptional activity is silenced in mitotic cells but it remains unclear whether the mitotic regulatory machinery interacts with tissue-specific transcriptional programs. We show that such cross-talk involves the controlled interaction between core subunits of the anaphase-promoting complex (APC) and the ID2 substrate. The N-terminal region of ID2 bound to core APC subunits, which formed an ID2-compatible pocket that optimally oriented ID2 in the APC-CDH1 complex. Phosphorylation of serine-5 by CDK1 prevented the association of ID2 with core APC, impaired ubiquitylation and stabilized ID2 protein at the mitosis-G1 transition leading to inhibition of basic Helix-Loop-Helix (bHLH)-mediated transcription. The serine-5 phosphomimetic mutant of ID2 that inefficiently bound core APC remained stable during mitosis, delayed exit from mitosis and reloading of bHLH transcription factors on chromatin. It also locked cells into a “mitotic stem cell” transcriptional state resembling the pluripotent program of embryonic stem cells. The substrates of APC-CDH1 SKP2 and Cyclin B1 share with ID2 the phosphorylation-dependent, D-box-independent interaction with core APC. These results reveal a new layer of control of the mechanism by which substrates are recognized by APC.

2022-03-11 | GSE181639 | GEO

Inhibitory effect of microRNA on carcinogenesis of colorectal cancer using CDX2P-NLS Cre;Apc+/loxP (CPC-Apc) mice [miRNA]

Project description:To observe the process of carcinogenesis, CPC-Apc mice were used as a mouse model of spontaneous colorectal cancer. MiRNAs (miR-200c, miR-302 (-a,-b,-c,-d), and miR-369 (-3p, -5p)) or negative control miRNA were intravenously injected to CPC-Apc mice from 8 weeks of age 3 times per week for 8 weeks with super carbonate apatite as drug delivery system. To know the therapeutic effect alive, endoscopic study was performed at 9 and 13 weeks. It revealed that tumor incidence was suppressed in mice with miRs compared to control. Mice were sacrificed at 15 weeks of age.

2023-05-03 | GSE92953 | GEO

Inhibitory effect of microRNA on carcinogenesis of colorectal cancer using CDX2P-NLS Cre;Apc+/loxP (CPC-Apc) mice (mRNA)

2023-05-03 | GSE92944 | GEO

H3S10ph broadly marks early-replicating domains in interphase ESCs and shows reciprocal antagonism with H3K9me2

Project description:Pervasive phosphorylation of histone H3 at serine 10 (H3S10ph) by Aurora B/C plays an important role in mitosis; however, this mark has also been observed at specific genic promoters and enhancers in interphase, implicating mitosis-independent functions. Using the FUCCI cell cycle reporter, we found that 30% of the genome is persistently marked with H3S10ph in interphase mouse embryonic stem cells (ESCs). H3S10ph demarcates broad gene-rich euchromatic regions in G1 and shows remarkable correlation with domains of early DNA replication timing (RT). Consistent with mitosis-independent H3S10 kinase activity, this pattern was preserved in ESCs treated with hesperidin, a potent inhibitor of Aurora B/C. Disruption of H3S10ph by expression of non-phosphorylatable H3.3S10A results in ectopic spreading of H3K9me2 into adjacent H3S10ph-enriched euchromatic regions, mimicking the phenotype observed in Drosophila JIL-1 kinase mutants. Conversely, H3S10ph domains expand in interphase Glp-/- ESCs, revealing that H3S10ph expansion is restricted by H3K9me2. Strikingly, spreading of H3S10ph at RT transition regions (TTRs) is accompanied by aberrant strand-biased transcription initiation of genes and repetitive elements co-oriented with the replication fork, indicating that H3K9me2 plays a critical role in establishing repressive chromatin on the leading strand. Finally, we show that H3S10ph is also present in interphase murine embryonic fibroblasts (MEFs), but is restricted to intragenic regions of actively transcribing genes. Our study provides a detailed map of interphase H3S10ph in ESCs and MEFs, uncovering a previously unappreciated crosstalk between the opposing marks H3S10ph and H3K9me2, and a role for the latter in ensuring appropriate transcription at TTRs in ESCs.

2017-11-20 | GSE97947 | GEO

Genomic RNA-DNA duplexes in mitotically arrested cells

Project description:RNA-DNA duplexes have been extensively catalogued in interphase cells, but relatively little is known about the genomic loci of these duplexes in mitotic cells. We compared RNA-DNA duplexes in DLD1 cells arrested in mitosis to libraries previously published in asynchronous HEK293T cells prepared with the same protocols, and processed with the same bioinformatic pipeline. We also observed that Aurora B inhibitors increased the immunofluorescence signal for RNA-DNA duplexes in mitotic cells, so we tested the effect of Aurora B inhibition on genomic enrichment of RNA-DNA duplexes.

2021-02-28 | GSE163197 | GEO

Ordered dephosphorylation initiated by the selective proteolysis of cyclin B drives mitotic exit

Project description:APC/C-mediated proteolysis of cyclin B and securin promotes entry into anaphase, inactivating CDK1 and permitting chromosome segregation, respectively. Reduction of CDK1 activity relieves inhibition of the CDK1-opposing phosphatases PP1 and PP2A-B55 leading to dephosphorylation of substrates crucial for mitotic exit. Meanwhile, continued APC/C activity is required to target various proteins, including Aurora and Polo kinases, for degradation. Together, these activities orchestrate a complex series of events during mitotic exit. However, the relative importance of regulated proteolysis and dephosphorylation in dictating the order and timing of these events remains unclear. Using high temporal-resolution mass spectrometry, we compare the relative extent of proteolysis and protein dephosphorylation. This reveals highly-selective rapid (~5min half-life) proteolysis of cyclin B, securin and geminin at the metaphase to anaphase transition, followed by slow proteolysis (>60 min half-life) of other mitotic regulators. Protein dephosphorylation requires APC/C-dependent destruction of cyclin B and was resolved into PP1-dependent fast, intermediate and slow categories with unique sequence motifs. We conclude that dephosphorylation initiated by the selective proteolysis of cyclin B drives the bulk of changes observed during mitotic exit.

2020-09-04 | PXD019791 | Pride

Ordered dephosphorylation initiated by the selective proteolysis of cyclin B drives mitotic exit

2020-09-04 | PXD019795 | Pride

Ordered dephosphorylation initiated by the selective proteolysis of cyclin B drives mitotic exit

2020-09-04 | PXD019787 | Pride

Ordered dephosphorylation initiated by the selective proteolysis of cyclin B drives mitotic exit

2020-09-04 | PXD019788 | Pride