Investigation of AKAP450’s role in microtubule nucleation at the Golgi

Abstract

The microtubule cytoskeleton is essential to establishing the shape and internal organization of cells. Microtubules are also important in enabling a diversity of functions, including cell division, anchorage of organelles, and intracellular transport. How, when, and where microtubules are assembled and organized is a feat involving many molecular players. Understanding how a variety of proteins are orchestrated to form functional microtubule networks first involves functional characterization of individual proteins. The protein AKAP450 is involved in microtubule nucleation and dynamics at the centrosome and the Golgi apparatus. However, its function in these processes is unclear. This study was the first to purify AKAP450 domains for characterization of its role in microtubule nucleation, specifically at the Golgi. Furthermore, this study began by addressing critical questions in the field about how microtubules are nucleated from γ- tubulin ring complexes. Investigation into AKAP450’s function began by testing the protein’s localization, microtubule nucleating-activity, and interactions with γ-tubulin ring complex components. Future directions include confirming the functionality of the purified AKAP450 domains and identifying other microtubule associated proteins that interact with AKAP450. In addition, AKAP450’s role in anchoring γ-tubulin ring complexes or regulating microtubule nucleation will also be determined.