Interactions between EB1, Microtubules and Actin

Over the last several decades much research focused has on furthering our understanding of the function and regulation of the microtubule and actin cytoskeletons. These two major components of the cytoskeleton have been studied for their roles in cell division, migration, and signaling. In studying the cytoskeleton, it has become clear that one must also understand the proteins that are associated with the microtubule and actin cytoskeletons. One of the most important microtubule interacting proteins is end binding protein 1 (EB1). EB1 is a well-studied central component in the cytoskeleton field. This protein, EB1, is the central thread of my dissertation research. This body of work has expanded our knowledge of the +TIP EB1 and contributed to the wealth of scientific information about the function of EB1. We have determined the EB1-MT binding location on the MT lattice as well as raised the possibility for EB1 regulation in vivo through EB1 dimerization. We have shown an entirely new EB1 interaction with actin cytoskeleton, shown than the EB1-actin binding interface partially overlaps the EB1-MT binding interface, and hypothesized an EB1-actin mechanism for controlling MT dynamics in vivo. We have preliminary data supporting the idea the +TIP network can act as a “super protein” to promote MT polymerization in vitro and made suggestions on future work to test further test this hypothesis.