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Proteomic study identifies Aurora-A mediated regulation of alternative splicing through multiple splicing factors

ABSTRACT: Proteomic study identifies Aurora-A mediated regulation of alternative splicing through multiple splicing factors

PROVIDER: PRJNA1186114 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR31348802_1.fastq.gz	Fastqsanger.gz
	SRR31348802_2.fastq.gz	Fastqsanger.gz
	SRR31348803_1.fastq.gz	Fastqsanger.gz
	SRR31348803_2.fastq.gz	Fastqsanger.gz
	SRR31348804_1.fastq.gz	Fastqsanger.gz

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Proteomic study identifies Aurora-A mediated regulation of alternative splicing through multiple splicing factors

Project description:The cell cycle regulator Aurora-A kinase presents an attractive target for cancer therapies, though its inhibition is also associated with toxic side effects. To gain a more nuanced understanding of Aurora-A function, we applied shotgun proteomics to identify 407 specific protein partners, including several splicing factors. Supporting a role in alternative splicing, we found that Aurora-A localizes to nuclear speckles, the storehouse of splicing proteins. Aurora-A interacts with and phosphorylates splicing factors both in vitro and in vivo, suggesting that it regulates alternative splicing by modulating the activity of these splicing factors. Consistently, Aurora-A inhibition significantly impacts the alternative splicing of 505 genes, with RNA motif analysis revealing an enrichment for Aurora-A interacting splicing factors. Additionally, we observed a significant positive correlation between the splicing events regulated by Aurora-A and those modulated by its interacting splicing factors. An interesting example is represented by CLK1 exon 4, which appears to be regulated by Aurora-A through SRSF3. Collectively, our findings highlight a broad role of Aurora-A in the regulation of alternative splicing.

2024-12-10 | GSE281881 | GEO

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 phosphorylates splicing factors and regulates alternative splicing

Project description:Aurora-A phosphorylates splicing factors and regulates alternative splicing

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Nitric oxide drives proteomic diversity through alternative splicing

Project description:Nitric oxide drives proteomic diversity through alternative splicing

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Proteomic study identifies Aurora-A-mediated regulation of alternative splicing through multiple splicing factors.

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Nitric oxide drives proteomic diversity through alternative splicing [CLIP-Seq]

Project description:Nitric oxide drives proteomic diversity through alternative splicing [CLIP-Seq]

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Nitric oxide drives proteomic diversity through alternative splicing [HEK RNA-Seq]

Project description:Nitric oxide drives proteomic diversity through alternative splicing [HEK RNA-Seq]

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Nitric oxide drives proteomic diversity through alternative splicing [Fibroblast RNA-Seq]

Project description:Nitric oxide drives proteomic diversity through alternative splicing [Fibroblast RNA-Seq]

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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

CCAR-1 regulates the alternative splicing of multiple genes in Caenorhabditis elegans

Project description:The Cell Division Cycle and Apoptosis Regulator (CCAR) protein family members have recently emerged as regulators of alternative splicing and transcription, as well as having other key physiological functions. For example, mammalian CCAR2/DBC1 forms a complex with the zinc factor protein ZNF326 to integrate alternative splicing with RNA polymerase II transcriptional elongation in AT-rich regions of the DNA. Additionally, Caenorhabditis elegans CCAR-1, a homolog to mammalian CCAR2, facilitates the alternative splicing of the perlecan unc-52 gene. However, much about the CCAR family's role in alternative splicing is unknown. We are interested in uncovering the role of the CCAR family in alternative splicing in vivo using Caenorhabditis elegans. We examined the role of CCAR-1 in genome-wide alternative splicing and identified new alternative splicing targets of CCAR-1 using RNA sequencing. Also, we found that CCAR-1 interacts with the spliceosome factors UAF-1 and UAF-2 using mass spectrometry, and that knockdown of ccar-1 affects alternative splicing patterns, motility, and proteostasis of UAF-1 mutant worms. Collectively, we demonstrate a role for CCAR-1 in the regulation of global alternative splicing in C. elegans and in conjunction with UAF-1

2024-02-26 | PXD043100 | Pride

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