A Survey on Tubulin and Arginine Methyltransferase Families Sheds Light on P. lividus Embryo as Model System for Antiproliferative Drug Development

Int J Mol Sci. 2019 Apr 30;20(9):2136. doi: 10.3390/ijms20092136.

Abstract

Tubulins and microtubules (MTs) represent targets for taxane-based chemotherapy. To date, several lines of evidence suggest that effectiveness of compounds binding tubulin often relies on different post-translational modifications on tubulins. Among them, methylation was recently associated to drug resistance mechanisms impairing taxanes binding. The sea urchin is recognized as a research model in several fields including fertilization, embryo development and toxicology. To date, some α- and β-tubulin genes have been identified in P. lividus, while no data are available in echinoderms for arginine methyl transferases (PRMT). To evaluate the exploiting of the sea urchin embryo in the field of antiproliferative drug development, we carried out a survey of the expressed α- and β-tubulin gene sets, together with a comprehensive analysis of the PRMT gene family and of the methylable arginine residues in P. lividus tubulins. Because of their specificities, the sea urchin embryo may represent an interesting tool for dissecting mechanisms of tubulin targeting drug action. Therefore, results herein reported provide evidences supporting the P. lividus embryo as animal system for testing antiproliferative drugs.

Keywords: PRMT; arginine methylation; echinoderms; post-translational modification; sea urchin; tubulin.

MeSH terms

  • Animals
  • Cytostatic Agents / toxicity*
  • Embryo, Nonmammalian / drug effects
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Methylation
  • Protein Processing, Post-Translational
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Sea Urchins / drug effects*
  • Sea Urchins / embryology
  • Toxicity Tests / methods*
  • Tubulin / metabolism*
  • Tubulin Modulators / toxicity*

Substances

  • Cytostatic Agents
  • Intracellular Signaling Peptides and Proteins
  • Tubulin
  • Tubulin Modulators
  • PRMT2 protein, human
  • Protein-Arginine N-Methyltransferases