Date of Graduation

Spring 2011

Degree

Master of Science in Biology

Department

Biology

Committee Chair

Kyoungtae Kim

Abstract

Vps1 is a dynamin-like protein that has been implicated in various cellular events, including protein trafficking from the late Golgi-to-endosome, peroxisome fission, vacuole fission and fusion, and retention of Golgi proteins. We recently observed in FM4-64 pulse-chase experiment with vps1 null cells that the levels of accumulated FM4-64-carrying transport vesicles increased significantly, suggesting the involvement of Vps1 on both the endocytic traffic to the vacuole, and the recycling traffic passing the late Golgi. Snc1, a v-SNARE protein required for the fusion of exocytic vesicle with the plasma membrane, follows the recycling traffic from endosome to Golgi. Snc1 is then returned to the plasma membrane from the Golgi. To test whether Vps1 takes part in the recycling traffic to the Golgi, the extent of dephosphorylation and subcellular localization of Snc1-GFP in vps1 mutants were studied. As expected, we show here that Snc1-GFP accumulation in the cytoplasm increased, mainly as an unphosphorylated form. Furthermore, VPS1 is found to genetically interact with several genes implicated in endosome-to-Golgi trafficking. Those genes include YPT6, GYP1, RIC1, and RCY1. The possibility of the physical interaction of Vps1 with those proteins will be tested in the future.

Keywords

vsp1, FM4-64, recycling traffick, vps1 to genetically interact with several genes, Snc1-GEP

Subject Categories

Biology

Copyright

© Chad Allen Highfill

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