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Updated: Sep 14, 2025

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
Published on: February 21, 2019
Exploring the Cka1 kinase interactome: unveiling novel potential regulatory roles of CKII kinase in S. pombe
Jan Jurcik1, Ingrid Cipakova2, Laura Olivia Karika2
1Department of Genetics, Cancer Research Institute, Biomedical Research Center, Slovak Academy of Sciences, Bratislava, Slovakia; Institute of Plant Genetics and Biotechnology, Plant Science and Biodiversity Centre, Slovak Academy of Sciences, Nitra, Slovakia.
Abstract:
Casein kinase II (CKII) is a highly conserved, constitutively active serine/threonine kinase involved in regulation of diverse cellular processes. In the fission yeast Schizosaccharomyces pombe, Cka1 serves as a catalytic subunit of the CKII complex. To uncover novel Cka1 interactors and potential substrates, we employed RNase-free tandem affinity purification strategy coupled with mass spectrometry. This analysis revealed associations between Cka1 and components of the RSC chromatin remodeling and DNA packaging complexes, Pcs1/Mde4 complex, as well as proteins linked to snoRNA-containing ribonucleoproteins and spliceosomal machinery. Interestingly, in vitro kinase assays unveiled that Cka1 phosphorylates Pcs1 and Mde4, homologues of the Saccharomyces cerevisiae monopolin subunits. These findings suggest for the potential role of Cka1 kinase in regulating chromatin dynamics, pre-mRNA splicing, and mitotic division.
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