Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation
Microtubules (MTs), dynamic polymers of α/β-tubulin heterodimers found in all eukaryotes, are involved in cytoplasm spatial organization, intracellular transport, cell polarity, migration and division, and in cilia biology. MTs functional diversity depends on the differential expression of distinct...
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| Format: | Article |
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MDPI AG
2023-04-01
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| Series: | Biology |
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| Online Access: | https://www.mdpi.com/2079-7737/12/4/561 |
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| author | Bruno Carmona H. Susana Marinho Catarina Lopes Matos Sofia Nolasco Helena Soares |
| author_facet | Bruno Carmona H. Susana Marinho Catarina Lopes Matos Sofia Nolasco Helena Soares |
| author_sort | Bruno Carmona |
| collection | DOAJ |
| description | Microtubules (MTs), dynamic polymers of α/β-tubulin heterodimers found in all eukaryotes, are involved in cytoplasm spatial organization, intracellular transport, cell polarity, migration and division, and in 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 a 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. |
| first_indexed | 2024-03-11T05:13:50Z |
| format | Article |
| id | doaj.art-44da2062fc634e27ba03bf586d535c23 |
| institution | Directory Open Access Journal |
| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-11T05:13:50Z |
| publishDate | 2023-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biology |
| spelling | doaj.art-44da2062fc634e27ba03bf586d535c232023-11-17T18:23:59ZengMDPI AGBiology2079-77372023-04-0112456110.3390/biology12040561Tubulin Post-Translational Modifications: The Elusive Roles of AcetylationBruno Carmona0H. Susana Marinho1Catarina Lopes Matos2Sofia Nolasco3Helena Soares4Centro de Química Estrutural, Institute of Molecular Sciences, Faculdade de Ciências, Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, PortugalCentro de Química Estrutural, Institute of Molecular Sciences, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, PortugalCentro de Química Estrutural, Institute of Molecular Sciences, Faculdade de Ciências, Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, PortugalEscola Superior de Tecnologia da Saúde de Lisboa, Instituto Politécnico de Lisboa, Av. D. João II, Lote 4.69.01, 1990-096 Lisboa, PortugalCentro de Química Estrutural, Institute of Molecular Sciences, Faculdade de Ciências, Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, PortugalMicrotubules (MTs), dynamic polymers of α/β-tubulin heterodimers found in all eukaryotes, are involved in cytoplasm spatial organization, intracellular transport, cell polarity, migration and division, and in 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 a 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.https://www.mdpi.com/2079-7737/12/4/561acetylationtubulinLys40microtubulespost-translational modificationsαTAT1 |
| spellingShingle | Bruno Carmona H. Susana Marinho Catarina Lopes Matos Sofia Nolasco Helena Soares Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation Biology acetylation tubulin Lys40 microtubules post-translational modifications αTAT1 |
| title | Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation |
| title_full | Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation |
| title_fullStr | Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation |
| title_full_unstemmed | Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation |
| title_short | Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation |
| title_sort | tubulin post translational modifications the elusive roles of acetylation |
| topic | acetylation tubulin Lys40 microtubules post-translational modifications αTAT1 |
| url | https://www.mdpi.com/2079-7737/12/4/561 |
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