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Updated: Feb 27, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
Published on: April 29, 2022
Protein phosphatases potentially associated with regulation of microtubules, their spatial structure reconstruction
Dariya O Samofalova1, Pavel A Karpov1, Alexey V Raevsky1
1Institute of Food Biotechnology and Genomics, Natl. Academy of Sci. of Ukraine, Osipovskogo str. 2a, Kyiv, 04123, Ukraine.
Abstract:
According to the sequence and profile comparison with known catalytic domains, where identified protein phosphatases potentially involved in regulation of microtubule dynamics and structure from Arabidopsis thaliana, Nicotiana tabacum, Medicago sativa, Oryza sativa subsp. japonica, Zea mays, and Triticum aestivum. Selected proteins were related to classical non-receptor, serine/threonine-specific and dual protein phosphatases. By application of template structures of human protein phosphatases, it was performed homology modelling of the catalytic domains of 17 plant protein phosphatases. Based on the results of the structural alignment, molecular dynamics, and conservatism in positions of functionally importance, it was confirmed homology of selected plant proteins and known protein phosphatases regulating structure and dynamics of microtubules.
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