ArticleOncogene2008
Protein kinase CK2 interacts with the splicing factor hPrp3p.
Article in Oncogene, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- The G-patch protein Cwf28 interacts with the RNA helicase Cdc28 in catalytically active spliceosomes in Schizosaccharomyces pombe.PloS one · 2026Article
- Protein kinase CK2 - diverse roles in cancer cell biology and therapeutic promise.Molecular and cellular biochemistry · 2023Review
- Review
- Phosphoproteomics revealed cellular signals immediately responding to disruption of cancer amino acid homeostasis induced by inhibition of L-type amino acid transporter 1.Cancer & metabolism · 2022Article
- A human kinase yeast array for the identification of kinases modulating phosphorylation-dependent protein-protein interactions.Molecular systems biology · 2022Article
- Splicing factor USP39 promotes ovarian cancer malignancy through maintaining efficient splicing of oncogenic HMGA2.Cell death & disease · 2021Article
- Identification of Candidate Casein Kinase 2 Substrates in Mitosis by Quantitative Phosphoproteomics.Frontiers in cell and developmental biology · 2017Article
- RSR-2, the Caenorhabditis elegans ortholog of human spliceosomal component SRm300/SRRM2, regulates development by influencing the transcriptional machinery.PLoS genetics · 2013Article
- Protein kinase CK2 and new binding partners during spermatogenesis.Cellular and molecular life sciences : CMLS · 2010Article
- CK2 phosphorylation of Pdx-1 regulates its transcription factor activity.Cellular and molecular life sciences : CMLS · 2010Article
- Contribution of the individual subunits of protein kinase CK2 and of hPrp3p to the splicing process.Molecular and cellular biochemistry · 2008Article
- Ability of CK2beta to selectively regulate cellular protein kinases.Molecular and cellular biochemistry · 2008Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Numerous signalling pathways in cells are influenced by the ubiquitous Ser/Thr protein kinase CK2. Protein kinase CK2 is composed of two regulatory beta-subunits and two catalytic alpha- or alpha'-subunits. Several of the known CK2 substrates are proteins known to regulate transcriptional events. Here, we describe that protein kinase CK2 interacts with the splicing factor hPrp3p, which is important for the assembly of the spliceosome. In a two-hybrid screen hPrp3p is exclusively bound to the catalytic alpha- or alpha'-subunits of CK2 but not to the regulatory beta-subunit. The interaction was confirmed by coimmunoprecipitation experiments in vitro and in vivo. Moreover, both proteins colocalized in nuclear speckles which is typical for splicing factor compartments within the nucleus. Phosphorylation experiments revealed that hPrp3p is also a substrate of protein kinase CK2. The main phosphorylation site was mapped to C-terminal residues. In vitro and in vivo splicing assays showed that the splicing activity is significantly influenced by the CK2-hPrp3p interaction. Thus, these data showed that CK2 is involved in the regulation of RNA processing.
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