Date of Graduation

Fall 2015


Master of Science in Biology



Committee Chair

Kyoungtae Kim


Vps1 (Vacuole protein sorting 1), a dynamin-like protein in yeast, is implicated in diverse membrane trafficking pathways and localized to many organelles, including the Golgi. It has been proposed that Vps1 is functionally linked to clathrin heavy chain 1 (Chc1), but the question of how, where, and when they function together remains unknown. Lines of evidence suggest that Chc1 and Vps1 are located at the late Golgi. Therefore, I hypothesized that Vps1 binds to Chc1 and functions together at the Golgi for efficient Golgi-to-endosome membrane trafficking. Using the yeast-two hybrid assay, I present evidence that Vps1 binds to the C-terminal region of the Chc1. Loss of Vps1 resulted in a mislocalization of Chc1, but not Gga1 adaptor, to the late endosome and to the vacuolar rim, suggesting Vps1 is required for Chc1 recruitment to the Golgi. In addition, I found that recruitment of Vps1 to the Golgi requires either the middle or the C-terminal domain of Vps1, but each of these domains showed reduction in the efficiency of targeting to the Golgi. I also found that the mean number of the late Golgi in vps1 mutant cells was drastically increased, probably because Vps1's involvement in the homotypic fusion at the trans-Golgi network might be affected in those mutant cells. Taken together, my results support the hypothesis that Vps1 functions at the Golgi with Chc1 and provide new insights into the activity of Vps1.


Vps1, Chc1, secretory pathway, TGN, endosome

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© Shiva Kumar Goud Gadila

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