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Tubulin acetylation and the cellular mechanosensing and stress response

2025-07Book part Embargoed access
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datacite.subject.sdg03:Saúde de Qualidade
dc.contributor.authorCarmona, Bruno
dc.contributor.authorDelgado, Inês L. S.
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.accessioned2025-08-29T11:31:11Z
dc.date.available2025-08-29T11:31:11Z
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 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 project LA/P/0056/2020.
dc.description.abstractMicrotubule (MT) acetylation has emerged as a critical regulator of cellular stress responses, integrating mechanical and oxidative stimuli to support cellular adaptability and survival. This post-translational modification (PTM) enhances MT flexibility and resilience, enabling cells to withstand mechanical challenges such as changes in extracellular matrix stiffness and applied forces. Through its impact on MT physical properties, acetylation minimizes cytoskeletal breakage, reducing the need for constant remodeling and supporting cellular integrity under mechanical stress. Furthermore, tubulin acetylation regulates intracellular trafficking by modulating interactions with molecular motors, allowing for efficient cargo transport and precise spatial organization without disrupting the MT network. In the context of oxidative stress, tubulin acetylation responds to redox imbalances by stabilizing MTs and influencing cellular pathways that regulate reactive oxygen species (ROS). This modification is linked to enhanced antioxidant responses, autophagy regulation, and mitochondrial dynamics, highlighting its role in maintaining cellular homeostasis under oxidative conditions. The dual function of tubulin acetylation, responding to and integrating signals from mechanical and oxidative stress, acts as a bridging mechanism between physical and chemical signaling pathways. Consequently, it has the potential to be a therapeutic target in diseases characterized by dysregulated stress responses, including neurodegenerative disorders, cancer, and cardiovascular conditions. Despite significant progress having been made, unanswered questions persist, particularly regarding the molecular mechanisms by which acetylated MTs encode spatial and functional information and their interplay with other tubulin PTMs.eng
dc.identifier.citationCarmona B, Delgado IL, Nolasco S, Marques R, Gonçalves J, Soares H. Tubulin acetylation and the cellular mechanosensing and stress response. In: Halasa M, Wawruszak A, editors. Histone and non-histone reversible acetylation in development, aging and disease. Cham: Springer; 2025. p. 141-62.
dc.identifier.doi10.1007/978-3-031-91459-1_5
dc.identifier.isbn9783031914591
dc.identifier.urihttp://hdl.handle.net/10400.21/22060
dc.language.isoeng
dc.peerreviewedyes
dc.publisherSpringer Nature
dc.relation.hasversionhttps://link.springer.com/chapter/10.1007/978-3-031-91459-1_5
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.subjectMechanical stress
dc.subjectMicrotubule
dc.subjectOxidative stress
dc.subjectTubulin acetylation
dc.subjectTubulin post-translational modifications
dc.subjectIPL/IDI&CA2024/HyperCil_ESTeSL
dc.subjectIPL/IDI&CA2024/ENIGMA_ESTeSL
dc.titleTubulin acetylation and the cellular mechanosensing and stress responseeng
dc.typebook part
dspace.entity.typePublication
oaire.citation.endPage162
oaire.citation.startPage141
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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