Tubulin post-translational modifications in protists-Tiny models for solving big questions

Protists are an exceptionally diverse group of mostly single-celled eukaryotes. The organization of the microtubular cytoskeleton in protists from various evolutionary lineages has different levels of sophistication, from a network of microtubules (MTs) supporting intracellular trafficking as in Dictyostelium, to complex structures such as basal bodies and cilia/flagella enabling cell motility, and lineage-specific adaptations such as the ventral disc in Giardia. MTs building these diverse structures have specific properties partly due to the presence of tubulin post-translational modifications (PTMs). Among them there are highly evolutionarily conserved PTMs: acetylation, detyrosination, (poly)glutamylation and (poly)glycylation. In some protists also less common tubulin PTMs were identified, including phosphorylation, methylation, Delta 2-, Delta 5- of alpha-tubulin, polyubiquitination, sumoylation, or S-palmitoylation. Not surprisingly, several single-celled organisms become models to study tubulin PTMs, including their effect on MT properties and discovery of the modifying enzymes. Here, we briefly summarize the current knowledge on tubulin PTMs in unicellular eukaryotes and highlight key findings in protists as model organisms.

Automated summary

Protists, a diverse group of single-celled eukaryotes, have different levels of sophistication in the organization of their microtubular cytoskeleton. The tubulin post-translational modifications (PTMs) in these organisms play a crucial role in building complex structures and have been studied using protists as model organisms. This article provides a brief summary of the current knowledge on tubulin PTMs in unicellular eukaryotes and highlights key findings in protists.