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

ABSTRACT: 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.

ORGANISM(S): Homo sapiens

PROVIDER: GSE87200 | GEO | 2020/09/02

REPOSITORIES: GEO

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hnRNP C is a key regulator of protein synthesis in mitosis

Project description:Purpose: The goal of this study is to characterize the role of hnRNP C in translation regulation of a specific set of mRNAs during mitosis. Methods: mitotic HeLa S3 cells expressing a Dox-inducible shRNA against hnRNP C were used and profiles of total mRNAs and ribosome footprints (RFs) of either untreated (wild type) cells or hnRNP C-knockdown cells were generated by deep sequencing, using Illumina HiSeq 2500. The sequence reads that passed quality filters were aligned to a reference set of human curated protein‐coding transcripts (plus the five human rRNA transcripts) using bowtie2. Expression estimates were further normalized using quantile normalization. qRT–PCR validation was performed using SYBR Green assays. Results: RNA‐seq and Ribo/RF‐seq datasets were combined according to gene ID. Only genes with expression level of at least 1.0 RPKM in both datasets were included in subsequent analyses. The combined dataset includes 10,996 genes. Transcripts encoding components of the translation machinery (Gene Ontology Biological Process [GOBP] “Translation” annotation) show reduced ribosome occupancy during mitosis under hnRNP C knockdown (p-value = 1.07 x 10-13) although their total mRNA levels are increased (p-value = 1.78 x 10-5). Translation efficiency (TE) calculations of ribosome occupancy per mRNA level showed a statistically-significant reduction for mRNAs encoding ribosomal proteins (Gene Ontology Cellular Compartment [GOCC] “Ribosome” annotation; p-value = 9.92 x 10-12). In particular, the TE of 5’ TOP-containing mRNAs was found to be significantly reduced under hnRNP C knockdown (p-value = 5.16 x 10-4). Conclusions: Our study represents the first detailed analysis of the translation effeciency of mRNAs in wild type and hnRNP C knockdown HeLa S3 cells during mitosis using RNA-Seq and Ribo-Seq. Our results show that the translation of a specific subset of mRNAs (5' TOP mRNAs) is regulated by hnRNP C in mitosis.

2017-06-23 | GSE83493 | GEO

Aurora A kinase phosphorylates Hec1 to regulate metaphase kinetochore-microtubule dynamics.

Project description:Precise regulation of kinetochore-microtubules is essential for successful chromosome segregation. Central to this regulation is Aurora B kinase, which phosphorylates kinetochore substrates to promote microtubule turnover. A critical target of Aurora B is the N-terminal “tail” domain of Hec1/NDC80, which is a component of the NDC80 complex, a force-transducing link between kinetochores and microtubules. While Aurora B is regarded as the “master regulator” of kinetochore-microtubule attachment, it is likely that other mitotic kinases contribute to Hec1phosphorylation. Here we show that Aurora A kinase phosphorylates the tail domain of Hec1 at Serine 69, a previously uncharacterized phosphorylation target site, and plays an important role in controlling kinetochore-microtubule attachment dynamics. Using phospho-specific antibodies, Hec1 phospho-deficient mutants, and kinase inhibitors, we demonstrate that Aurora A is required for the regulation of kinetochore-microtubule dynamics of metaphase chromosomes and identify Hec1 Serine 69 as a critical Aurora A substrate for this regulation. Additionally, we demonstrate that Aurora A kinase associates with INCENP during mitosis and that INCENP is competent to drive accumulation of the kinase to the centromere region of mitotic chromosomes. These findings reveal that both Aurora A and Aurora B contribute to kinetochore-microtubule attachment dynamics, and they uncover an unexpected role for Aurora A in mitosis.

2017-11-28 | PXD006892 | Pride

hnRNP C is a key regulator of protein synthesis in mitosis

Project description:Stringent post-transcriptional regulation of mRNA fate is critical for proper cell division. To detect proteins involved in such regulation, we analyzed the composition of intact polysomal complexes from mitotic and interphase cells by quantitative mass-spectrometry. Using this approach, we detected increased association of several mRNA-binding proteins, including heterogeneous nuclear ribonucleoprotein C (hnRNP C), with mitotic polysomes. Immunofluorescence analysis, puromycin-sensitivity assays and nascent-chain pulldowns confirmed that hnRNP C interacts with polysome-bound mRNA during mitosis. Using a combination of pulsed SILAC and metabolic labeling, we found that knockdown of hnRNP C has a pervasive effect on both global and transcript-specific translation rates. Furthermore, ribosome profiling revealed that hnRNP C is involved in translation of mRNAs encoding components of the translation machinery and other mRNAs harboring a 5' terminal oligopyrimidine tract (5’ TOP). Taken together, these results suggest that hnRNP C is crucial for ribogenesis during mitosis; in its absence, production of ribosomal proteins and translation factors is impaired and translation rates are reduced during subsequent phases of the cell cycle.

2017-07-11 | PXD004244 | Pride

Aurora-A phosphorylates splicing factors and regulates alternative splicing

Project description:The goal of this study is to identify the effect of inhibition of Aurora-A kinase activity on gene expression and RNA splicing. The perturbation of Aurora-A is well known to affect cell cycle distribution. Therefore, we coupled the inhibition of Aurora-A with cell synchronization procedure in order to avoid the indirect effect of cell cycle perturbation on splicing changes. The mRNA -seq libraries were prepared and subjected to paired-end sequencing on Illumina HiSeq 2500 lanes. Differential gene expression and splicing analysis were carried using the edgeR tool and VAST-tools respectively. The RNA seq analysis identified that pharmacological inhibition of Aurora-A affects alternative splicing of 505 genes while having a marginal effect on gene expression. Overall our work identified Aurora-A as a novel splicing kinase and for the first time, describes a broad role of Aurora-A in regulating alternative splicing.

2024-11-21 | GSE160733 | GEO

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.

2023-09-26 | GSE214613 | GEO

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]

2023-09-26 | GSE214485 | GEO

Aurora kinase A phosphorylates histone methyltransferase NSD2 to promote drug resistance in multiple myeloma [RNA-Seq]

Project description:The epigenetic plasticity, such as DNA methylation and histone modification, has been suggested to be a potential mechanism controlling MM progression and drug resistance, but the underlying mechanisms are not fully understood. Here we demonstrate that some drug resistant genes were activated during myeloma resistance to bortezomib. Mechanistically, Aurora A can interact with NSD2, whose SET domain is responsible to H3K36me2 to enhance the transcriptional activity of Aurora A target gene. Once Aurora A is knocked out, H3K36me2 activity will change, changing the transcription activity of those drug resistant genes.

2020-12-22 | GSE163589 | GEO

Redox priming promotes Aurora A activation during mitosis

Project description:Samples of Aurora A kinase domain were covalently labeled with disulfide-containing compounds and analyzed by mass spectrometry to determine the extent of covalent labeling.

2020-06-28 | MSV000085641 | MassIVE

Heteractis aurora

Project description:Heteractis aurora

| PRJNA1138220 | ENA

pre-mRNA splicing is regulated by an Aurora-A-mediated phopsho-signaling network

Project description:In this study, we identified many new potential interactors of the Aurora-A kinase using a proteomic approach. A significant portion of Aurora-A interaction network is composed of proteins involved in pre-mRNA splicing, implying that Aurora-A signaling extends beyond its canonical function. Aurora-A directly interacts with many of the RRM domain-containing splicing factors such as SR proteins and hnRNP proteins and phosphorylates them in vitro. Aurora-A shows a subcellar distribution to nuclear speckles, the storehouse of splicing factors, consistent with its potential function in pre-mRNA splicing. Moreover, RNA-seq analysis of pharmacologically inhibited Aurora-A cells identified 261 genes whose RNA splicing is dependent on Aurora-A activity. These splicing affected genes are involved in various biological processes such as transcription, GTPase activity, ciliogenesis, DNA repair, RNA splicing and G2/M transition. Here, for the first time, we uncovered a relationship between Aurora-A activity and mRNA processing through a complex network of factors involved in RNA maturation.

2024-12-11 | PXD021093 | Pride

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