Yeast dynamin and Ypt6 function in parallel for the endosome-to-Golgi retrieval of Snc1.

Protein recycling is an important cellular process required for cell homeostasis. Results from prior studies have shown that vacuolar sorting protein-1 (Vps1), a dynamin homolog in yeast, is implicated in protein recycling from the endosome to the trans-Golgi Network (TGN). However, the function of Vps1 in relation to Ypt6, a master GTPase in the recycling pathway, remains unknown.

trans-Golgi network-bound cargo traffic.

Cargo following the retrograde trafficking are sorted at endosomes to be targeted the trans-Golgi network (TGN), a central receiving organelle. Though molecular requirements and their interaction networks have been somewhat established, the complete understanding of the intricate nature of their action mechanisms in every step of the retrograde traffic pathway remains unachieved. This review focuses on elucidating known functions of key regulators, including scission factors at the endosome and tethering/fusion mediators at the receiving dock, TGN, as well as a diverse range of cargo.

Yeast dynamin associates with the GARP tethering complex for endosome-to-Golgi traffic.

Yeast dynamin, Vacuolar Protein Sorting 1 (Vps1), has been implicated in recycling traffic from the endosome to the trans-Golgi network (TGN). Previous research showed a genetic interaction of Vps1 with all components of the GARP tethering complex, which anchors vesicles at the late Golgi membrane. We used the yeast two-hybrid system and have identified a 33 amino acid segment of Vps51, a GARP subunit, that interacts with Vps1.

Yeast dynamin Vps1 associates with clathrin to facilitate vesicular trafficking and controls Golgi homeostasis.

The yeast dynamin Vps1 acts cooperatively with many proteins at diverse cellular locations for endocytosis, protein sorting, and membrane fusion and fission. 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. Here we report that Vps1 arrives at the Golgi after clathrin, and that loss of Vps1 leads to a shift in the cellular localization of clathrin to the late endosome and vacuole, not vice versa.