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Structural Biological Characteristics of CK1-Like Protein Kinase Isotypes Associated with Regulation of Plant Microtubules

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Abstract

Eighteen isotypes of CK1-like protein kinases were identified in A. thaliana. Comparison of catalytic domains in rat CK1 (α, β, γ1–3, δ, and ε) and 18 plant homologs from A. thaliana confirmed a high structural similarity for 13 CK1-like protein kinases: CKL1 (CK1δ), CKL2, CKL3, CKL4, CKL5, CKL6, CKL7, CKL8, CKL9, CKL10, CKL11, CKL12, and CKL13. It was found that CK1-specific inhibitor D4476 interacts with rat KС1D and 13 plant homologs in a similar ATP-competitive manner. Ligand binding was confirmed based on scoring functions of docking, results of molecular dynamics, and chemogenomic analysis. The specific interaction of CK1-kinases with substrate proteins depends on specific motifs located in their C-end region. The specific motifs of EB1 binding was identified in plant СKL1 and CKL2. The role of the C-end region in CKL6–β-tubulin interaction was also confirmed.

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Authors and Affiliations

  1. Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, 04123, Kyiv, Ukraine

    P. A. Karpov, A. V. Rayevsky, Ya. A. Sheremet, A. I. Yemets & Ya. B. Blume

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  1. P. A. Karpov
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  2. A. V. Rayevsky
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  3. Ya. A. Sheremet
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Translated by M. Batrukova

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Karpov, P.A., Rayevsky, A.V., Sheremet, Y.A. et al. Structural Biological Characteristics of CK1-Like Protein Kinase Isotypes Associated with Regulation of Plant Microtubules. Cytol. Genet. 54, 293–304 (2020). https://doi.org/10.3103/S0095452720040052

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