Is Casein Kinase 2 Able to Phosphorylate Plant α-Tubulin?


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Results of classical and structural bioinformatical research allow to predict casein kinase 2 dependent phosphorylation of conservative residues of Ser94 and Ser419 in Trypanosoma and Arabidopsis α-tubulin. Location of these residues in the region of internal contact of α-/β-tubulin heterodimer has been demonstrated. It is hypothesized that phosphorylation of Ser94 can affect dimerization of α-/β-tubulin in Trypanosoma and Arabidopsis. Most likely, potential phosphorylation of Ser419 does not have a direct effect on microtubule structure but is related to interaction with associated proteins, in particular with kinesins.

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P. Karpov

Institute of Food Biotechnology and Genomics

编辑信件的主要联系方式.
Email: karpov@nas.gov.ua
乌克兰, Kyiv

Ya. Blume

Institute of Food Biotechnology and Genomics

Email: karpov@nas.gov.ua
乌克兰, Kyiv

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