Is Casein Kinase 2 Able to Phosphorylate Plant α-Tubulin?
- Authors: Karpov P.A.1, Blume Y.B.1
-
Affiliations:
- Institute of Food Biotechnology and Genomics
- Issue: Vol 52, No 2 (2018)
- Pages: 103-111
- Section: Article
- URL: https://journal-vniispk.ru/0095-4527/article/view/173846
- DOI: https://doi.org/10.3103/S0095452718020044
- ID: 173846
Cite item
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
About the authors
P. A. Karpov
Institute of Food Biotechnology and Genomics
Author for correspondence.
Email: karpov@nas.gov.ua
Ukraine, Kyiv
Ya. B. Blume
Institute of Food Biotechnology and Genomics
Email: karpov@nas.gov.ua
Ukraine, Kyiv
Supplementary files
