Cytology and Genetics

, Volume 52, Issue 2, pp 103–111 | Cite as

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

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Abstract

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.

Keywords

casein kinase 2 tubulin phosphorylation Trypanosoma Arabidopsis 

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Copyright information

© Allerton Press, Inc. 2018

Authors and Affiliations

  1. 1.Institute of Food Biotechnology and GenomicsNational Academy of Sciences of UkraineKyivUkraine

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