Protein kinase KIN10 from Arabidopsis thaliana as a potential regulator of primary microtubule nucleation centers in plants

Abstract

The nearest plant homologues of animal protein kinase BRSK were identified using the methods of classical and structural bioinformatics. The selection was performed based on the sequence comparison, results of phylogenetic clustering, and analysis of domain architecture. Spatial structures of human BRSK1 and KIN10 from A. thaliana were compared. The relationship between KIN10 and the regulation of primary microtubule nucleation centers in A. thaliana was revealed. Obvious homology of plant KIN10 and mammalian BRSK1 evidence to suggest that this plant protein kinase is associated with the regulation of the structure and function of primary microtubule nucleation centers and is able to phosphorylate γ-tubulin from Arabidopsis (TUBG1 and TUBG2) at Ser131, affecting the γTuSC monomer structure as well as the γTuRC complex assembly. The effect of the modification on the TUBG1-GACP3 interaction was suggested.

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