Functional domain analysis of type I myosins in clathrin-mediated endocytosis
Clathrin-mediated endocytosis (CME) is a process through which cells internalize pieces of their plasma membrane (PM) and extracellular substances. Cells regulate signal transduction, membrane homeostasis, and nutrient uptake through this ancient and highly-conserved pathway. Previous research demonstrated that type I myosins are critical for endocytic internalization. The yeast type I myosin Myo5 is composed of a motor head linked to a multi-domain tail. Myo5 motor activity is necessary for PM internalization, and its tail domains are predicted to bind various cellular structures. Little is known about the precise role of Myo5 in yeast CME. I will apply a combination of genetic manipulation and fluorescence imaging toward building a functional domain analysis of Myo5 by quantitating the effects of mutations in the Myo5 protein. These studies will increase our understanding of the fundamental mechanisms responsible for the crucial process of endocytosis. Because the endocytic machinery is widely conserved, what we learn in yeast is likely to apply broadly to all eukaryotic organisms, including humans, where defective endocytosis is linked to heart disease, cancer, and neural degeneration.
Message to Sponsor
- Major: Molecular and Cell Biology
- Sponsor: Rose Hills
- Mentor: David Drubin, Molecular and Cell Biology