Is Casein Kinase 2 Able to Phosphorylate Plant α-Tubulin?
- 作者: Karpov P.A.1, Blume Y.B.1
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隶属关系:
- Institute of Food Biotechnology and Genomics
- 期: 卷 52, 编号 2 (2018)
- 页面: 103-111
- 栏目: Article
- URL: https://journals.rcsi.science/0095-4527/article/view/173846
- DOI: https://doi.org/10.3103/S0095452718020044
- ID: 173846
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详细
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.
作者简介
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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