ArticleMolecular and cellular biochemistry2008
Contribution of the individual subunits of protein kinase CK2 and of hPrp3p to the splicing process.
Article in Molecular and cellular biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 6 citations in OpenAlex.
- In silico investigations identified Butyl Xanalterate to competently target CK2α (CSNK2A1) for therapy of chronic lymphocytic leukemia.Scientific reports · 2022Article
- A human kinase yeast array for the identification of kinases modulating phosphorylation-dependent protein-protein interactions.Molecular systems biology · 2022Article
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4 authors at 1 institution in 1 country.
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Abstract
We have recently shown that protein kinase CK2 binds to the splice factor hPrp3p. Moreover, CK2 phosphorylates hPrp3p in vitro and in vivo. Here we analysed the spliceosome for the presence of individual subunits of CK2. By cell fractionation experiments we found that CK2alpha, CK2alpha', the spliceosome specific SmB/B' and hPrp3p protein co-localize in the nucleus. A sucrose density gradient analysis revealed that the individual subunits of CK2 co-sedimented at least in part with the SmB/B' protein. We further show by co-immune precipitation experiments that CK2alpha is associated with the U4/U6*U5 tri-snRNP specific protein 61K. In vitro splice assays with nuclear extracts depleted from CK2alpha, CK2alpha' and hPrp3p, respectively, revealed that CK2alpha and hPrp3p are absolutely necessary for an efficient splicing whereas CK2alpha' seems to be dispensable. Furthermore, these data support the notion about individual roles for CK2alpha and CK2alpha' in the splicing process.
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