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

1
Department of Biological, Chemical and Pharmaceutical Sciences and Technologies (STEBICEF), University of Palermo, Viale delle Scienze, Ed. 16, Palermo, 90128 Sicily, Italy.
2
National Research Council-Istituto per lo studio degli impatti Antropici e Sostenibilità in ambiente marino (IAS-CNR), Laboratory of Molecular Ecology and Biotechnology, Detached Unit of Capo Granitola, Via del mare, Torretta Granitola (TP), 91021 Sicily, Italy
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(9), 2136; https://doi.org/10.3390/ijms20092136
Received: 18 April 2019 / Accepted: 27 April 2019 / Published: 30 April 2019
(This article belongs to the Special Issue Regulatory Mechanisms of Tubulin-Like Proteins)
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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. View Full-Text
Keywords: tubulin; PRMT; post-translational modification; arginine methylation; sea urchin; echinoderms tubulin; PRMT; post-translational modification; arginine methylation; sea urchin; echinoderms
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Ragusa, M.A.; Nicosia, A.; Costa, S.; Casano, C.; Gianguzza, F. 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, 20, 2136.

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