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Updated: Jul 10, 2026
11:34
Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
Published on: August 9, 2019
Protein kinase CK2 interacts with the splicing factor hPrp3p.
S Lehnert1, C Götz, S Kartarius
1Universität des Saarlandes, Medizinische Biochemie und Molekularbiologie, Homburg, Germany.
Oncogene
|November 21, 2007
Summary
Protein kinase CK2 interacts with splicing factor hPrp3p, influencing RNA processing. This study reveals CK2
Area of Science:
- Cellular biology
- Molecular biology
- Biochemistry
Background:
- Serine/Threonine protein kinase CK2 (CK2) influences numerous cellular signaling pathways.
- CK2 is a heterotetrameric complex comprising two catalytic alpha/alpha' subunits and two regulatory beta subunits.
- CK2 substrates include proteins involved in transcriptional regulation.
Purpose of the Study:
- To investigate the interaction between protein kinase CK2 and the splicing factor hPrp3p.
- To determine if CK2 affects the function of hPrp3p in RNA processing.
Main Methods:
- Yeast two-hybrid screening to identify interacting partners of CK2 subunits.
- Coimmunoprecipitation assays (in vitro and in vivo) to confirm protein interactions.
- Immunofluorescence microscopy to determine subcellular localization.
- In vitro and in vivo splicing assays to assess functional impact.
Main Results:
- hPrp3p specifically binds to the catalytic alpha/alpha' subunits of CK2, not the beta subunit.
- CK2 and hPrp3p colocalize within nuclear speckles.
- hPrp3p is phosphorylated by CK2, primarily at C-terminal residues.
- CK2-hPrp3p interaction significantly influences splicing activity.
Conclusions:
- Protein kinase CK2 interacts with and phosphorylates the splicing factor hPrp3p.
- CK2 plays a regulatory role in RNA processing through its interaction with hPrp3p.
- This interaction impacts spliceosome assembly and function.
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