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Is casein kinase 2 аble to phosphorylate plant α-tubulin?

Karpov P.A., Blume Ya.B.

 




SUMMARY. Casein kinase 2-dependent phosphorylation of Trypa-nosoma and Arabidopsis α-tubulin at conservative Ser94 and Ser419 was predicted bioinformatically. It was proved that above-mentioned amino acid residues are located in the inner region of α-/β-tubulin heterodimer contact. It is believed that phos-phorylation at Ser94 may affect formation of α-/β-tubulin dimer in Trypanosoma and Arabidopsis. In addition, phosphorylation on Ser419 probably has no direct impact on the structure of microtubule. At the same time, we assume that phosphorylation on Ser419 can affect MT-interaction with associated proteins, in particular, with kinesin.

Tsitologiya i Genetika 2018, vol. 52, no. 2, pp. 22-32

E-mail: karpov nas.gov.ua, cellbio cellbio.freenet.viaduk.net

Karpov P.A., Blume Ya.B. Is casein kinase 2 аble to phosphorylate plant α-tubulin?, Tsitol Genet., 2018, vol. 52, no. 2, pp. 22-32.

In "Cytology and Genetics":
P. A. Karpov, Ya. B. Blume Is Casein Kinase 2 Able to Phosphorylate Plant α-Tubulin?, Cytol Genet., 2018, vol. 52, no. 2, pp. 103–111
DOI: 10.3103/S0095452718020044


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