RESUMO
Due to their elongated and polarized morphology, neurons rely on the microtubule (MT) cytoskeleton for their shape, as well as for efficient intracellular transport that maintains neuronal function, survival, and connectivity. Although all MTs are constructed from α- and ß-tubulins that are highly conserved throughout eukaryotes, different MT networks within neurons exhibit different dynamics and functions. For example, molecular motors must be able to differentially recognize the axonal and dendritic MTs to deliver appropriate cargos to sensory endings and synaptic regions. The Tubulin Code hypothesis proposes that MTs can be specialized in form and function by chemical differences in their composition by inclusion of different α- and ß-tubulins into the MT lattice, as well as differences in post-translational enzymatic modifications. The chemical differences encode information that allow MTs to regulate interactions with various microtubule-based molecular motors such as kinesins and dyneins as well as with structural microtubule-associated proteins (MAPs), which can, in turn, modify the function or stability of MTs. Here, we review studies involving C. elegans, a model organism with a relatively simple nervous system that is amenable to genetic analysis, that have contributed to our understanding of how the Tubulin Code can specialize neuronal MT networks to establish differences in neuronal morphology and function. Such studies have revealed molecules and mechanisms that are conserved in vertebrates and have the potential to inform our understanding of neurological diseases involving defects in the cytoskeleton and intracellular transport.