PHOSPHORYLATION OF THE ADAPTER PROTEIN LRAP35A IS INVOLVED IN MICROTUBULE REGULATION

Abstract

My research aimed to better understand the signaling and functional significance shrouding LRAP35a phosphorylation. LRAP35a was previously shown to form a tripartite complex with MRCK and Myosin18A, and together, the trio regulates the lamella actomyosin retrograde flow for efficient cell motility. It was also shown by others to be important for MTOC reorientation, thereby implicating this MRCK-linked signaling in microtubule regulation. However, the mechanism underlying this process remains largely unknown. Interestingly, LRAP35a was found to regulate microtubules in a phosphorylation dependent manner, thereby presenting a potential MRCK-linked event for microtubule regulation. While exploring the signaling regulating LRAP35a, pathway and kinases both positively and negatively regulating LRAP35a role in microtubule regulation were uncovered. The molecular partners that are essential for LRAP35a role in microtubule regulation were also identified. My study pinpoints kinases and pathway regulating LRAP35a phosphorylation states and its associated partners for microtubule regulation.