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Abstract
Microtubules are hollow tube-like polymeric structures composed of α,β-tubulin heterodimers. They play an important role in numerous cellular processes, including intracellular transport, cell motility and segregation of the chromosomes during cell division. Moreover, microtubule doublets or triplets form a scaffold of a cilium, centriole and basal body, respectively. To perform such diverse functions microtubules have to differ in their properties. Post-translational modifications are one of the factors that affect the properties of the tubulin polymer. Here we focus on the direct and indirect effects of post-translational modifications of tubulin on microtubule dynamics.
Highlights
Microtubules are an essential component of the cytoskeleton of a eukaryotic cell
Three major factors may contribute to the heterogeneity of microtubule properties: (i) composition of the α- and β-tubulin gene-encoded isotypes that are incorporated into microtubule; (ii) post-translational modifications of tubulin that create a pattern on the microtubule surface known as the “tubulin code” [4] and (iii) interactions with diverse microtubule-interacting proteins (MIPs)
Specific tubulin isotypes may differ in the extent of their post-translational modifications depending on the presence or absence of modifiable amino acids
Summary
Microtubules are an essential component of the cytoskeleton of a eukaryotic cell. They support key cellular functions such as maintenance of cell shape, intracellular transport, cell polarity or cell division. Three major factors may contribute to the heterogeneity of microtubule properties: (i) composition of the α- and β-tubulin gene-encoded isotypes that are incorporated into microtubule; (ii) post-translational modifications of tubulin that create a pattern on the microtubule surface known as the “tubulin code” [4] and (iii) interactions with diverse microtubule-interacting proteins (MIPs). Specific tubulin isotypes may differ in the extent of their post-translational modifications depending on the presence or absence of modifiable amino acids (for instance, in Caenorhabditis elegans only Mec-12 α-tubulin isotype has the acetylable lysine residue in position 40 [5]). We focus on the direct and indirect effects of the post-translational modifications of tubulin on microtubule dynamics
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