Is Casein Kinase 2 Able to Phosphorylate Plant α-Tubulin?
- Авторлар: Karpov P.A.1, Blume Y.B.1
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Мекемелер:
- Institute of Food Biotechnology and Genomics
- Шығарылым: Том 52, № 2 (2018)
- Беттер: 103-111
- Бөлім: Article
- URL: https://journals.rcsi.science/0095-4527/article/view/173846
- DOI: https://doi.org/10.3103/S0095452718020044
- ID: 173846
Дәйексөз келтіру
Аннотация
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.
Негізгі сөздер
Авторлар туралы
P. Karpov
Institute of Food Biotechnology and Genomics
Хат алмасуға жауапты Автор.
Email: karpov@nas.gov.ua
Украина, Kyiv
Ya. Blume
Institute of Food Biotechnology and Genomics
Email: karpov@nas.gov.ua
Украина, Kyiv
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