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Advisor(s)
Abstract(s)
The success of the intracellular parasite Toxoplasma gondii in invading host cells relies on the apical complex, a specialized microtubule cytoskeleton structure associated with secretory organelles. The T. gondii genome encodes three isoforms of both α- and β-tubulin, which undergo specific post-translational modifications (PTMs), altering the biochemical and biophysical proprieties of microtubules and modulating their interaction with associated proteins. Tubulin PTMs represent a powerful and evolutionarily conserved mechanism for generating tubulin diversity, forming a biochemical 'tubulin code' interpretable by microtubule-interacting factors. T. gondii exhibits various tubulin PTMs, including α-tubulin acetylation, α-tubulin detyrosination, Δ5α-tubulin, Δ2α-tubulin, α- and β-tubulin polyglutamylation, and α- and β-tubulin methylation. Tubulin glutamylation emerges as a key player in microtubule remodeling in Toxoplasma, regulating stability, dynamics, interaction with motor proteins, and severing enzymes. The balance of tubulin glutamylation is maintained through the coordinated action of polyglutamylases and deglutamylating enzymes. This work reviews and discusses current knowledge on T. gondii tubulin glutamylation. Through in silico identification of protein orthologs, we update the recognition of putative proteins related to glutamylation, contributing to a deeper understanding of its role in T. gondii biology.
Description
This research was funded by FCT-Fundação para a Ciência e Tecnologia, I.P. (Portugal) through CIISA - Centro de Investigação Interdisciplinar em Sanidade Animal, project UIDB/00276/2020 and Laboratório Associado para Ciência Animal e Veterinária (AL4AnimalS) project LA/P/0059/2020.
Keywords
Toxoplasma gondii Apical complex Microtubules Tubulin glutamylation Tubulin post-translational modifications
Citation
Delgado IL, Gonçalves J, Fernandes R, Zúquete S, Soares H, Nolasco S, et al. Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii. Microorganisms. 2024;12(3):488.
Publisher
MDPI