High impact information on RVS161

• Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae [1].
• Two lines of evidence indicate that RVS161/END6's endocytic function is not required for cell fusion [1].
• Second, we isolated five function-specific alleles of RVS161/FUS7 that were defective for endocytosis, but not mating, and three alleles that were defective for cell fusion but not endocytosis [1].
• The amino terminus has homology to two yeast proteins, Rvs167 and Rvs161, which are involved in cell entry into stationary phase and cytoskeletal organization [2].
• Rvs167 and Rvs161, the yeast homologs of amphiphysin I, have been implicated in endocytosis, actin function, and cell polarity [3].

Biological context of RVS161

• Loss of function of either the RVS161 or RVS167 Saccharomyces cerevisiae amphiphysin-like gene confers similar growth phenotypes that can be suppressed by mutations in sphingolipid biosynthesis [4].
• Mutations in RVS161, just as in RVS167, lead to a random budding pattern in a/alpha diploid cells [5].
• Functional assessment of the yeast Rvs161 and Rvs167 protein domains [6].
• RVS161 and RVS167 have an identical set of 49 synthetic lethal interactions, revealing functions for the Rvs proteins in cell polarity, cell wall synthesis, and vesicle trafficking as well as a shared role in mating [7].
• Moreover, Southern analysis revealed the presence of other sequences homologous to the RVS161 gene in the yeast genome [8].

Anatomical context of RVS161

• Mutations in RVS161 and RVS167 yeast genes induce identical phenotypes associated to actin cytoskeleton disorders [6].
• Consistent with these roles, we show that the Rvs167p-Rvs161p heterodimer, like its amphiphysin homologues, can bind to phospholipid membranes in vitro, suggesting a role in vesicle formation and/or fusion [7].
• The yeast Rvs161 and Rvs167 proteins are involved in secretory vesicles targeting the plasma membrane and in cell integrity [9].

Physical interactions of RVS161

• Using the two hybrid system, we have shown that Rvs167p interacts with Rvs161p, through its N-terminal domain which contains predicted coiled-coil structures [10].

Regulatory relationships of RVS161

• The BAR adaptor proteins encoded by the RVS167 and RVS161 genes from Saccharomyces cerevisiae form a complex that regulates actin, endocytosis, and viability following starvation or osmotic stress [11].

Other interactions of RVS161

• Characterizing the sphingolipid signaling pathway that remediates defects associated with loss of the yeast amphiphysin-like orthologs, Rvs161p and Rvs167p [4].
• In contrast, Fus2p and Rvs161p appeared to act after vesicle positioning [12].
• By using subcellular fractionation, we demonstrate that Rvs167p, Ybr108wp, Gdh3p, and Acf2p all localize to Rvs161p-containing lipid rafts, thus placing them within a single compartment that should facilitate their interactions [4].
• Taken together, these results strongly suggest that the Rvs161 and Rvs167 proteins act together in relation with Sur7p [13].
• (1986) are located between RVS161 and YCR10C [14].

References