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Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii

2024-02Journal article Open access
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dc.contributor.authorDelgado, Inês
dc.contributor.authorGonçalves, João
dc.contributor.authorFernandes, Rita
dc.contributor.authorZúquete, Sara
dc.contributor.authorBasto, Afonso P.
dc.contributor.authorLeitão, Alexandre
dc.contributor.authorSoares, Helena
dc.contributor.authorNolasco, Sofia
dc.date.accessioned2024-04-01T10:24:53Z
dc.date.available2024-04-01T10:24:53Z
dc.date.issued2024-02
dc.descriptionThis 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.pt_PT
dc.description.abstractThe 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.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationDelgado 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.pt_PT
dc.identifier.doi10.3390/microorganisms12030488pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.21/17232
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relation.publisherversionhttps://www.mdpi.com/2076-2607/12/3/488pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/pt_PT
dc.subjectToxoplasma gondiipt_PT
dc.subjectApical complexpt_PT
dc.subjectMicrotubulespt_PT
dc.subjectTubulin glutamylationpt_PT
dc.subjectTubulin post-translational modificationspt_PT
dc.titleBalancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondiipt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.issue3pt_PT
oaire.citation.startPage488pt_PT
oaire.citation.titleMicroorganismspt_PT
oaire.citation.volume12pt_PT
person.familyNameAntunes Soares
person.givenNameMaria Helena
person.identifierG-3065-2010
person.identifier.ciencia-id131B-F0E1-572C
person.identifier.orcid0000-0001-6180-7041
person.identifier.scopus-author-id55932139400
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication267fae06-39c1-4b12-a246-39e0b1dde34a
relation.isAuthorOfPublication.latestForDiscovery267fae06-39c1-4b12-a246-39e0b1dde34a

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