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

Maria Antonietta Ragusa1, Aldo Nicosia2, Salvatore Costa3

  • 1Department of Biological, Chemical and Pharmaceutical Sciences and Technologies (STEBICEF), University of Palermo, Viale delle Scienze, Ed. 16, Palermo, 90128 Sicily, Italy.. maria.ragusa@unipa.it.

International Journal of Molecular Sciences
|May 5, 2019
PubMed

Insights

Sea urchin embryos can help test anti-cancer drugs targeting tubulins and microtubules. Methylation of tubulin may affect drug resistance, and sea urchins offer a model to study this.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Developmental Biology

Background:

  • Tubulins and microtubules are key targets for taxane chemotherapy.
  • Tubulin post-translational modifications, like methylation, influence drug effectiveness and resistance.
  • The sea urchin embryo is a valuable model for biological research.

Purpose of the Study:

  • To investigate the potential of the sea urchin embryo (P. lividus) for antiproliferative drug development.
  • To survey expressed α- and β-tubulin gene sets in P. lividus.
  • To analyze the protein arginine methyltransferase (PRMT) gene family and methylable arginine residues in P. lividus tubulins.

Main Methods:

  • Gene set surveys for α- and β-tubulins in P. lividus.
  • Comprehensive analysis of the PRMT gene family in P. lividus.
  • Identification of methylable arginine residues in P. lividus tubulins.

Main Results:

  • Identification and characterization of α- and β-tubulin gene sets in P. lividus.
  • Comprehensive analysis of the PRMT gene family in P. lividus.
  • Evidence supporting the P. lividus embryo as a model for studying tubulin-targeting drugs.

Conclusions:

  • The P. lividus embryo is a suitable animal system for testing antiproliferative drugs.
  • This study provides foundational data for understanding tubulin methylation in drug resistance.
  • Sea urchin embryos offer unique advantages for dissecting mechanisms of tubulin-targeting drug action.
Keywords:
PRMTarginine methylationechinodermspost-translational modificationsea urchintubulin

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