Yeast Two-Hybrid Library Screen Reveals Novel Binding Partners of Vps1 and Links Vps1 to a Novel Role in Budding

Abstract

Vacuolar protein sorting 1 (Vps1) is a dynamin-like GTPase involved in membrane remodeling and protein sorting in multiple cellular trafficking pathways. It appears that Vps1 functions through interaction with a selective group of proteins that reside at eachorganelle. Though Vps1's role in membrane remodeling has been well characterized, a majority of its biochemical interactions at each traffic location still elude us. A yeast two-hybrid library screen was performed in Saccharomyces cerevisiae in search of novel Vps1 binding partners. These results reveal seventeen as-yet-unidentified Vps1 binding proteins implicated in various pathways. Notably, our study present evidence forVps1'sinteraction with Ste24, an ER membrane protein and proteins implicated in chitin distribution, suggesting Vps1's functional association with chitin regulation required for yeast budding.