In addition to tubulin glycylation and glutamylation, other tubulin modifications or binding partners could potentially influence the activity and localization of TTLL10 and other glycylation enzymes. For example, tubulin acetylation, phosphorylation, or detyrosination could impact the substrate specificity or catalytic activity of TTLL10. Binding partners such as microtubule-associated proteins (MAPs) or motor proteins could also interact with glycylation enzymes, modulating their activity or recruitment to microtubules. Furthermore, posttranslational modifications on other proteins involved in the glycylation pathway, such as chaperones or regulatory proteins, could affect the function of TTLL10 and the overall glycylation process. Understanding the crosstalk between different tubulin modifications and their regulators is essential for deciphering the complex network of interactions that govern microtubule dynamics and cellular processes.