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.

Inactivation of Tor proteins affects the dynamics of endocytic proteins in early stage of endocytosis.

Tor2 is an activator of the Rom2/Rho1 pathway that regulates alpha-factor internalization. Since the recruitment of endocytic proteins such as actin-binding proteins and the amphiphysins precedes the internalization of alpha-factor, we hypothesized that loss of Tor function leads to an alteration in the dynamics of the endocytic proteins. We report here that endocytic proteins, Abp1 and Rvs167, are less recruited to endocytic sites not only in tor2 but also tor1 mutants.

Vps1 in the late endosome-to-vacuole traffic.

Vacuolar protein sorting 1 (Vps1), the yeast homolog to human dynamin, is a GTP hydrolyzing protein, which plays an important role in protein sorting and targeting between the Golgi and late endosomal compartments. In this study, we assessed the functional significance of Vps1 in the membrane traffic towards the vacuole. We show here that vps1 delta cells accumulated FM4-64 to a greater extent than wild-type (WT))cells, suggesting slower endocytic degradation traffic toward the vacuole.

Yeast dynamin implicated in endocytic scission and the disassembly of endocytic components.

The yeast dynamin-related GTPase Vps1 has been implicated in a range of cellular functions including vacuolar protein sorting, protein trafficking, organization of peroxisome and endocytosis.1,2 Vps1 is present at endocytic sites and may be directly involved in endocytic vesicle invagination through its membrane-tubulating activity. Here, evidence supporting the functional link between Vps1 and the yeast amphiphysin Rvs167 in vesicle invagination is discussed.