Date of Graduation

Summer 2015


Master of Science in Biology



Committee Chair

Kyoungtae Kim


Intracellular trafficking from the late endosome to Golgi in cells is termed retrograde transport, essential for recycling of important macromolecules including cell membrane receptors. Retrograde transport is regulated by a family of proteins known as the "Retromer” composed of 5 VPS proteins (Vps5, Vps17, Vps26, Vps29, and Vps35). Retromer acts as the coat proteins for vesicles emerging from late endosomes. Loss of Retromer function has been previously implicated in both Parkinson's and Alzheimer's disease. Vps1, a yeast dynamin-like protein, plays a role in intracellular trafficking. Vps1 has been shown to localize at the endocytic sites to promote pinching off of endocytic vesicles. The goal of this study was to further investigate the relationship between the Retromer and Vps1. My data show colocalization between Vps1 and the Retromer, and that Vps1 knockout cells show a decrease in Retromer targeting to endosomes, a phenotype reminiscent of human Alzheimer's disease. In order to evaluate the functional relationship of the Retromer and Vps1, colocalization and interaction studies, both genetic and physical, were conducted. The data suggest that various Retromer proteins interact with Vps1 on both the genetic and physical levels. I explore this possible relationship, further expanding Vps1's role as an intracellular trafficking mediator.


retromer, retrograde transport, yeast, trafficking, cargo, vps1

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© Christopher Robert Trousdale

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