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Tubulin acetylation: a critical regulator of microtubule function

2025-07Book part Embargoed access
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datacite.subject.sdg03:Saúde de Qualidade
dc.contributor.authorDelgado, Inês L.
dc.contributor.authorCarmona, Bruno
dc.contributor.authorNolasco, Sofia
dc.contributor.authorMarques, Rita
dc.contributor.authorGonçalves, João
dc.contributor.authorSoares, Helena
dc.contributor.editorHalasa, M.
dc.contributor.editorWawruszak, A.
dc.date.accessioned2025-08-29T13:27:49Z
dc.date.available2025-08-29T13:27:49Z
dc.date.issued2025-07
dc.descriptionThis work was funded by Instituto Politécnico de Lisboa IPL/IDI&CA2024/HyperCil_ESTeSL and IPL/IDI&CA2024/ENIGMA_ESTeSL, and also by Centro de Química Estrutural is a Research Unit funded by FCT through projects UIDB/00100/2020, and UIDP/00100/2020. Institute of Molecular Sciences is an Associate Laboratory funded by FCT through the project LA/P/0056/2020.
dc.description.abstractThe cytoskeleton is conserved throughout the eukaryotic lineage and consists of a complex dynamic network mainly composed of three distinct polymers: microtubules (MTs), actin filaments, and intermediate filaments. MTs are polymers of α/β-tubulin heterodimers, playing a myriad of distinct cellular functions, and are the main components of complex structures like the mitotic spindle, cilia, and centrioles. Post-translational modifications (PTMs) regulate the function and increase the complexity of the α/β-tubulin heterodimer pools. One of the PTMs that has been extensively studied is the acetylation of lysine 40 (K40) on α-tubulin, which specifically occurs inside the MT lumen. Acetylation plays a crucial role in controlling the stability and function of MTs in response to signals from within and outside the cell. It impacts the cytoplasm's 3D arrangement and important cellular activities like intracellular transport, cell division, polarity, and migration. Recent research has also emphasized the significance of this PTM in regulating the mechanical properties of MTs and cellular sensing. The levels and activity of MT acetyltransferases and deacetylases are tightly regulated through various transcriptional, post-transcriptional, and post-translational mechanisms, including miRNAs, phosphorylation, protein-protein interactions, and regulated localization between the nucleus and cytoplasm. These regulatory processes involve components of diverse signaling pathways, and their deregulation has been implicated in numerous diseases, including neurological disorders, cancer, and cardiac conditions.eng
dc.identifier.citationDelgado IL, Carmona B, Nolasco S, Marques R, Gonçalves J, Soares H. Tubulin acetylation: a critical regulator of microtubule function. In: Halasa M, Wawruszak A, editors. Histone and non-histone reversible acetylation in development, aging and disease. Cham: Springer; 2025. p. 91-140.
dc.identifier.doi10.1007/978-3-031-91459-1_4
dc.identifier.isbn9783031914591
dc.identifier.urihttp://hdl.handle.net/10400.21/22062
dc.language.isoeng
dc.peerreviewedyes
dc.publisherSpringer Nature
dc.relation.hasversionhttps://link.springer.com/chapter/10.1007/978-3-031-91459-1_4
dc.relation.ispartofResults and Problems in Cell Differentiation
dc.relation.ispartofHistone and Non-Histone Reversible Acetylation in Development, Aging and Disease
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectMicrotubules
dc.subjectPost-translational modifications
dc.subjectTubulin acetylation
dc.subjectTubulin acetylation-related diseases
dc.subjectTubulin lysine acetyltransferases
dc.subjectTubulin lysine deacetylases
dc.subjectIPL/IDI&CA2024/HyperCil_ESTeSL
dc.subjectIPL/IDI&CA2024/ENIGMA_ESTeSL
dc.titleTubulin acetylation: a critical regulator of microtubule functioneng
dc.typebook part
dspace.entity.typePublication
oaire.citation.endPage140
oaire.citation.startPage91
oaire.citation.titleHistone and non-histone reversible acetylation in development, aging and disease
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85
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
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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