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.

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.

Yeast dynamin interaction with ESCRT proteins at the endosome.

The dynamin-like protein, Vps1, is a GTPase involved in cargo sorting and membrane remodeling in multiple cellular trafficking pathways. Recently, Vps1 has been shown to genetically interact with ESCRT subunits. We tested the hypothesis that the functional connection of Vps1 with some of these subunits of ESCRT complexes occurs via a physical interaction.

Carbon Nanomaterials Alter Global Gene Expression Profiles.

Carbon nanomaterials (CNMs), which include carbon nanotubes (CNTs) and their derivatives, have diverse technological and biomedical applications. The potential toxicity of CNMs to cells and tissues has become an important emerging question in nanotechnology. To assess the toxicity of CNTs and fullerenol C60(OH)24, we in the present work used the budding yeast Saccharomyces cerevisiae, one of the simplest eukaryotic organisms that share fundamental aspects of eukaryotic cell biology.

TORC2 and eisosomes are spatially interdependent, requiring optimal level of phosphatidylinositol 4, 5-bisphosphate for their integrity.

The elucidation of the organization and maintenance of the plasma membrane has been sought due to its numerous roles in cellular function. In the budding yeast Saccharomyces cerevisiae, a novel paradigm has begun to emerge in the understanding of the distribution of plasma membrane microdomains and how they are regulated. We aimed to investigate the dynamic interdependence between the protein complexes eisosome and TORC2, representing microdomains MCC and MCT, respectively.

Molecular dynamics at the endocytic portal and regulations of endocytic and recycling traffics.

Endocytic and recycling pathways involve the transportation of soluble and transmembrane cargos to destinations within the cell or back to the plasma membrane for reuse. Common mechanistic themes for the traffic pathways in eukaryotic cells from yeast to mammalian cells are well-conserved, manifested by the molecular choreography of cargo segregation, membrane budding and coating, pinching off of the invaginated vesicle, cytoskeleton-mediated vesicle motility and fusion with target compartments. Here, we discuss recent insights into the spatiotemporal dynamics of endocytic machinery at the plasma membrane and the molecular details of bifurcating traffics at the endosome either to the lysosome or to the trans-Golgi network (TGN).