Protein phosphatases potentially associated with regulation of microtubules, their spatial structure reconstruction and analysis

Cell Biol Int. 2019 Sep;43(9):1081-1090. doi: 10.1002/cbin.10810. Epub 2017 Aug 2.

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.

Keywords: PP1; PP2A; PP4; cytoskeleton regulation; microtubules; molecular modeling.

MeSH terms

  • Catalytic Domain
  • Humans
  • Microtubules / metabolism*
  • Phosphoprotein Phosphatases / chemistry*
  • Phosphoprotein Phosphatases / genetics
  • Plant Proteins / chemistry*
  • Plant Proteins / genetics
  • Plants / enzymology*
  • Structural Homology, Protein

Substances

  • Plant Proteins
  • Phosphoprotein Phosphatases