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Tubulin post-translational modifications: the elusive roles of acetylation

dc.contributor.authorCarmona, Bruno
dc.contributor.authorMarinho, H. Susana
dc.contributor.authorMatos, Catarina Lopes
dc.contributor.authorNolasco, S.
dc.contributor.authorSoares, Helena
dc.date.accessioned2023-04-20T15:23:15Z
dc.date.available2023-04-20T15:23:15Z
dc.date.issued2023-04
dc.descriptionThis work was funded by Instituto Politécnico de Lisboa IPL/2021/ObeCil_ESTeSL and IPL/2022/WintCilGlu_ESTeSL.pt_PT
dc.description.abstractMicrotubules (MTs), dynamic polymers of α/β-tubulin heterodimers found in all eukaryotes, are involved in cytoplasm spatial organization, intracellular transport, cell polarity, migration, division, and cilia biology. MTs functional diversity depends on the differential expression of distinct tubulin isotypes and is amplified by a vast number of different post-translational modifications (PTMs). The addition/removal of PTMs to α- or β-tubulins is catalyzed by specific enzymes and allows combinatory patterns largely enriching the distinct biochemical and biophysical properties of MTs, creating a code read by distinct proteins, including microtubule-associated proteins (MAPs), which allow cellular responses. This review is focused on tubulin-acetylation, whose cellular roles continue to generate debate. We travel through the experimental data pointing to α-tubulin Lys40 acetylation role as being an MT stabilizer and a typical PTM of long-lived MTs, to the most recent data, suggesting that Lys40 acetylation enhances MT flexibility and alters the mechanical properties of MTs, preventing MTs from mechanical aging characterized by structural damage. Additionally, we discuss the regulation of tubulin acetyltransferases/desacetylases and their impacts on cell physiology. Finally, we analyze how changes in MT acetylation levels have been found to be a general response to stress and how they are associated with several human pathologies.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationCarmona B, Marinho HS, Matos CL, Nolasco S, Soares H. Tubulin post-translational modifications: the elusive roles of acetylation. Biology. 2023;12(4):561.pt_PT
dc.identifier.doi10.3390/biology12040561pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.21/15919
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.relationIPL/2021/ObeCil_ESTeSLpt_PT
dc.relationIPL/2022/WintCilGlu_ESTeSLpt_PT
dc.relation.publisherversionhttps://www.mdpi.com/2079-7737/12/4/561pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/pt_PT
dc.subjectAcetylationpt_PT
dc.subjectTubulinpt_PT
dc.subjectLys40pt_PT
dc.subjectMicrotubulespt_PT
dc.subjectPost-translational modificationspt_PT
dc.subjectαTAT1pt_PT
dc.subjectHDAC6pt_PT
dc.subjectSIRT2pt_PT
dc.subjectMicrotubule-associated proteinspt_PT
dc.subjectMicrotubule-mechanical propertiespt_PT
dc.subjectIPL/2021/ObeCil_ESTeSLpt_PT
dc.subjectIPL/2022/WintCilGlu_ESTeSLpt_PT
dc.titleTubulin post-translational modifications: the elusive roles of acetylationpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.issue4pt_PT
oaire.citation.startPage561pt_PT
oaire.citation.titleBiologypt_PT
oaire.citation.volume12pt_PT
person.familyNameSousa Carmona
person.familyNameNolasco
person.familyNameAntunes Soares
person.givenNameBruno Filipe
person.givenNameSofia
person.givenNameMaria Helena
person.identifierG-3065-2010
person.identifier.ciencia-id681F-6045-F8C2
person.identifier.ciencia-id5017-368D-3F71
person.identifier.ciencia-id131B-F0E1-572C
person.identifier.orcid0000-0003-0871-9063
person.identifier.orcid0000-0003-2168-0511
person.identifier.orcid0000-0001-6180-7041
person.identifier.scopus-author-id55932139400
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication908e548e-eaac-4485-97c5-fcbd33fe7e5a
relation.isAuthorOfPublication34a552a4-6414-461d-a5f6-862a175ea812
relation.isAuthorOfPublication267fae06-39c1-4b12-a246-39e0b1dde34a
relation.isAuthorOfPublication.latestForDiscovery908e548e-eaac-4485-97c5-fcbd33fe7e5a

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