Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii
Autor(a) principal: | |
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Data de Publicação: | 2024 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.21/17104 |
Resumo: | The success of Toxoplasma gondii (intracellular parasite) host cell invasion relies on the apical complex, a specialized microtubule cytoskeleton structure associated with secretory organelles. The genome encodes three isoforms of both α- and β-tubulin which are altered by specific post-translational modifications (PTMs), changing the biochemical/biophysical proprieties of microtubules, and modulating their interaction with associated proteins. Tubulin PTMs are a powerful and evolutionarily conserved mechanism to generate tubulin diversity, forming a biochemical ‘tubulin code’ that can be ‘read’ by microtubule-interacting factors. The T. gondii tubulin PTMs are: α-tubulin acetylation, α-tubulin detyrosination, Δ5α-tubulin, Δ2α-tubulin, α- and β-tubulin polyglutamylation, and α- and α-tubulin methylation. Tubulin glutamylation is a key candidate to assist microtubule remodeling in Toxoplasma, being involved in the regulation of microtubule stability, dynamics, interaction with motor proteins, and severing enzymes. The correct balance of tubulin glutamylation is achieved by the coordinated action of polyglutamylases and deglutamylating enzymes. In this work, we will review and discuss the current knowledge on T. gondii tubulin glutamylation. By in silico identification of mammalian protein orthologs, we explored and updated the identification of putative proteins related to glutamylation, contributing to a better understanding of the role of tubulin glutamylation in T. gondii. |
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Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondiiToxoplasma gondiiTubulin glutamylationTubulin post-translational modificationsApical complexMicrotubulesThe success of Toxoplasma gondii (intracellular parasite) host cell invasion relies on the apical complex, a specialized microtubule cytoskeleton structure associated with secretory organelles. The genome encodes three isoforms of both α- and β-tubulin which are altered by specific post-translational modifications (PTMs), changing the biochemical/biophysical proprieties of microtubules, and modulating their interaction with associated proteins. Tubulin PTMs are a powerful and evolutionarily conserved mechanism to generate tubulin diversity, forming a biochemical ‘tubulin code’ that can be ‘read’ by microtubule-interacting factors. The T. gondii tubulin PTMs are: α-tubulin acetylation, α-tubulin detyrosination, Δ5α-tubulin, Δ2α-tubulin, α- and β-tubulin polyglutamylation, and α- and α-tubulin methylation. Tubulin glutamylation is a key candidate to assist microtubule remodeling in Toxoplasma, being involved in the regulation of microtubule stability, dynamics, interaction with motor proteins, and severing enzymes. The correct balance of tubulin glutamylation is achieved by the coordinated action of polyglutamylases and deglutamylating enzymes. In this work, we will review and discuss the current knowledge on T. gondii tubulin glutamylation. By in silico identification of mammalian protein orthologs, we explored and updated the identification of putative proteins related to glutamylation, contributing to a better understanding of the role of tubulin glutamylation in T. gondii.Preprints.orgRCIPLDelgado, Inês L.S.Gonçalves, JoãoFernandes, RitaZúquete, SaraBasto, Afonso P.Leitão, AlexandreSoares, HelenaNolasco, Sofia2024-02-12T13:08:27Z2024-012024-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.21/17104engDelgado IL, Gonçalves J, Fernandes R, Zúquete S, Soares H, Nolasco S, et al. Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii. Preprints.org. 2024:2024010287.10.20944/preprints202401.0287.v1info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-02-21T02:17:14Zoai:repositorio.ipl.pt:10400.21/17104Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T02:38:13.172198Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii |
title |
Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii |
spellingShingle |
Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii Delgado, Inês L.S. Toxoplasma gondii Tubulin glutamylation Tubulin post-translational modifications Apical complex Microtubules |
title_short |
Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii |
title_full |
Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii |
title_fullStr |
Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii |
title_full_unstemmed |
Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii |
title_sort |
Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii |
author |
Delgado, Inês L.S. |
author_facet |
Delgado, Inês L.S. Gonçalves, João Fernandes, Rita Zúquete, Sara Basto, Afonso P. Leitão, Alexandre Soares, Helena Nolasco, Sofia |
author_role |
author |
author2 |
Gonçalves, João Fernandes, Rita Zúquete, Sara Basto, Afonso P. Leitão, Alexandre Soares, Helena Nolasco, Sofia |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
RCIPL |
dc.contributor.author.fl_str_mv |
Delgado, Inês L.S. Gonçalves, João Fernandes, Rita Zúquete, Sara Basto, Afonso P. Leitão, Alexandre Soares, Helena Nolasco, Sofia |
dc.subject.por.fl_str_mv |
Toxoplasma gondii Tubulin glutamylation Tubulin post-translational modifications Apical complex Microtubules |
topic |
Toxoplasma gondii Tubulin glutamylation Tubulin post-translational modifications Apical complex Microtubules |
description |
The success of Toxoplasma gondii (intracellular parasite) host cell invasion relies on the apical complex, a specialized microtubule cytoskeleton structure associated with secretory organelles. The genome encodes three isoforms of both α- and β-tubulin which are altered by specific post-translational modifications (PTMs), changing the biochemical/biophysical proprieties of microtubules, and modulating their interaction with associated proteins. Tubulin PTMs are a powerful and evolutionarily conserved mechanism to generate tubulin diversity, forming a biochemical ‘tubulin code’ that can be ‘read’ by microtubule-interacting factors. The T. gondii tubulin PTMs are: α-tubulin acetylation, α-tubulin detyrosination, Δ5α-tubulin, Δ2α-tubulin, α- and β-tubulin polyglutamylation, and α- and α-tubulin methylation. Tubulin glutamylation is a key candidate to assist microtubule remodeling in Toxoplasma, being involved in the regulation of microtubule stability, dynamics, interaction with motor proteins, and severing enzymes. The correct balance of tubulin glutamylation is achieved by the coordinated action of polyglutamylases and deglutamylating enzymes. In this work, we will review and discuss the current knowledge on T. gondii tubulin glutamylation. By in silico identification of mammalian protein orthologs, we explored and updated the identification of putative proteins related to glutamylation, contributing to a better understanding of the role of tubulin glutamylation in T. gondii. |
publishDate |
2024 |
dc.date.none.fl_str_mv |
2024-02-12T13:08:27Z 2024-01 2024-01-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.21/17104 |
url |
http://hdl.handle.net/10400.21/17104 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Delgado IL, Gonçalves J, Fernandes R, Zúquete S, Soares H, Nolasco S, et al. Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondii. Preprints.org. 2024:2024010287. 10.20944/preprints202401.0287.v1 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Preprints.org |
publisher.none.fl_str_mv |
Preprints.org |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799137432684199936 |