Tubulin Acetylation: A Critical Regulator of Microtubule Function
- PMID: 40593208
- DOI: 10.1007/978-3-031-91459-1_4
Tubulin Acetylation: A Critical Regulator of Microtubule Function
Abstract
The 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.
Keywords: Microtubules; Post-translational modifications; Tubulin acetylation; Tubulin acetylation-related diseases; Tubulin lysine acetyltransferases; Tubulin lysine deacetylases.
© 2025. The Author(s), under exclusive license to Springer Nature Switzerland AG.
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References
-
- Aebersold R, Agar JN, Amster IJ et al (2018) How many human proteoforms are there? Nat Chem Biol 14:206–214. https://doi.org/10.1038/nchembio.2576 - DOI - PubMed - PMC
-
- Ahmad FJ, Pienkowski TP, Baas PW (1993) Regional differences in microtubule dynamics in the axon. J Neurosci 13:856–866. https://doi.org/10.1523/JNEUROSCI.13-02-00856.1993 - DOI - PubMed - PMC
-
- Ahn S, Kwon A, Oh Y et al (2023) Microtubule acetylation-specific inhibitors induce cell death and mitotic arrest via JNK/AP-1 activation in triple-negative breast cancer cells. Mol Cells 46(6):387–398. https://doi.org/10.14348/molcells.2023.2192 - DOI - PubMed - PMC
-
- Aillaud C, Bosc C, Saoudi Y et al (2016) Evidence for new C-terminally truncated variants of α- and β-tubulins. Mol Biol Cell 27:640–653. https://doi.org/10.1091/mbc.E15-03-0137 - DOI - PubMed - PMC
-
- Aillaud C, Bosc C, Peris L et al (2017) Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation. Science 358:1448–1453. https://doi.org/10.1126/science.aao4165 - DOI - PubMed
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