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Review
. 2017 Feb 7;10(1):21.
doi: 10.3390/ph10010021.

The Link between Protein Kinase CK2 and Atypical Kinase Rio1

Konrad Kubiński  1 , Maciej Masłyk  2
Affiliations
Review

The Link between Protein Kinase CK2 and Atypical Kinase Rio1

Konrad Kubiński et al. Pharmaceuticals (Basel). .

Abstract

The atypical kinase Rio1 is widespread in many organisms, ranging from Archaebacteria to humans, and is an essential factor in ribosome biogenesis. Little is known about the protein substrates of the enzyme and small-molecule inhibitors of the kinase. Protein kinase CK2 was the first interaction partner of Rio1, identified in yeast cells. The enzyme from various sources undergoes CK2-mediated phosphorylation at several sites and this modification regulates the activity of Rio1. The aim of this review is to present studies of the relationship between the two different kinases, with respect to CK2-mediated phosphorylation of Rio1, regulation of Rio1 activity, and similar susceptibility of the kinases to benzimidazole inhibitors.

Keywords: benzimidazoles; phosphorylation; protein kinase CK2; protein kinase Rio1; protein-protein interaction.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Differences and similarities between protein kinases Rio1 and CK2 [6,7,8,9,10,11,12,13,14,15,16]. (A) Comparison of the 3D structures of hRio1 and hCK2α visualised in PyMOL. The N-terminal β-sheets are coloured blue, the β-hairpin is coloured orange, the αC-helix is coloured yellow, the hinge is coloured magenta, the C-lobe α-helices are coloured cyan, the αR-helix is coloured red, the “flexible loop” is represented by blacked dashed line, and the activation loop is coloured green. (B) Comparison of other features of the two kinases.
Figure 2
Figure 2
Alignment of human (Q9BRS2) and yeast Rio1 (Q12196). The alignment was performed using a Clustal Omega tool on the uniprot.org website. CK2 phosphorylation sites are marked in yellow, catalytic amino acid residues are marked in red, and the autophosphorylation site is marked in green. Two putative CK2-phosphorylation sequences in hRio1 are marked with boxes. Identical amino acids are marked with asterisks, similar amino acids are marked with colons, and different amino acids are marked with dots.
Figure 3
Figure 3
Docked binding modes obtained for TIBI in the ATP-binding pocket of (A) Rio1 and (B) CK2 [9].
See this image and copyright information in PMC

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