Abstract

Microtubules are structural components in cells that play important functions such as maintaining cell shape and facilitating intracellular transport. Furthermore, there are many microtubule binding proteins that interact with microtubules, expanding microtubule function.There are many studies on these binding proteins, but most of them exclusively interact with the surface of microtubules. However, microtubules are hollow shaped, allowing for the possibility of proteins entering and interacting with the insides or the lumen of microtubules. Only a few proteins have been identified with this behavior. A notable example is alpha-tubulin acetyltransferase (atat). However, there are still questions about the role of acetylation in microtubule dynamics. Here, we describe our efforts toward an alternative method to study atat-lumen interactions. We believe that a novel photocrosslinking amino acid, DiZPK, can be incorporated into the microtubule lumen to capture atat. If successful, our work can also enable the study of other protein-protein interactions within the lumen.