High impact information on RVS167

• Yeast complementation studies suggested that AtSH3Ps have similar functions to the yeast Rvs167p protein involved in endocytosis and actin arrangement [1].
• Using this method, we screened 4,250 strains expressing epitope-tagged proteins and identified 24 candidate substrates of the Pho85-Pcl1 cyclin-dependent kinase, including the known substrate Rvs167 [2].
• The amino terminus has homology to two yeast proteins, Rvs167 and Rvs161, which are involved in cell entry into stationary phase and cytoskeletal organization [3].
• This suppression is probably mediated by sphingolipids, since deletion of SUR7, YDL222, and YNL194 altered the sphingolipid content of the yeast plasma membrane, and other SUR genes suppress rvs167 via effects on sphingolipid synthesis [4].
• Our genetic screens also reveal that the interaction between Abp1p and the Rvs167p Src homology 3 (SH3) domain may be important under certain conditions, providing the first genetic evidence for a role for the SH3 domain of Rvs167p [5].

Biological context of RVS167

• 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 [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 [5].
• Mutations in RVS161, just as in RVS167, lead to a random budding pattern in a/alpha diploid cells [7].
• We also show that a site in Abp1p itself is specifically bound by the SH3 domain of the actin-associated protein Rvs167p [8].
• We tested the extent to which the Rvs167p protein domains rescued phenotypes associated with deletion of RVS167: salt sensitivity, random budding, and endocytosis and sporulation defects [9].

Anatomical context of RVS167

• The rvs161 and rvs167 mutant cells exhibit several identical phenotypes including sensitivity to several different growth conditions and morphological defects such as alteration of the actin cytoskeleton and budding patterns [10].
• 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 [5].
• The yeast Rvs161 and Rvs167 proteins are involved in secretory vesicles targeting the plasma membrane and in cell integrity [11].

Associations of RVS167 with chemical compounds

• Complete disruption of the actin cytoskeleton using Latrunculin-A did not affect Rvs167p localization in patches throughout the cell [12].

Physical interactions of RVS167

• Sla1 is similar in domain structure to CIN85 and binds directly to the endophilin-like Rvs167 [13].
• Moreover, Rvs167p functionally interacts with the myosin Myo2p [11].
• Using the two hybrid system, we have shown that Rvs167p interacts with Rvs161p, through its N-terminal domain which contains predicted coiled-coil structures [14].
• The specific SH3 domain of Rvs167p interacted with the N-terminal domain of Gyp5p [15].

Co-localisations of RVS167

• Rvs167p colocalized with actin patches during yeast vegetative growth and mating [12].

Regulatory relationships of RVS167

• We propose that Rvs167p is activated by phosphorylation in its GPA region by the Pcl-Pho85p kinase [9].
• Our results suggest that phosphorylation of Rvs167p by a cyclin-dependent kinase and by a MAP kinase is an important mechanism for regulating protein complexes involved in actin cytoskeleton function [16].
• Phosphorylation of Rvs167p inhibits its interaction in vitro with Las17p, an activator of the Arp2/3 complex, as well as with a novel protein, Ymr192p [16].

Other interactions of RVS167

• Abp1 null mutations, like rvs167 mutations, result in defects in sporulation and reduced viability under certain suboptimal growth conditions [8].
• We showed that the suppressive ability of the overexpressed SUR7 gene concerns all the rvs167 phenotypes [10].
• In the process, we have demonstrated a direct physical interaction between Rvs167p and the two-hybrid interacting proteins, Acf2p, Gdh3p, and Ybr108wp, while also elucidating the Rvs167p amino acid domains to which these proteins bind [6].
• These and other well-established data support the idea that Vrp1, Las17, Rvs167 proteins belong to the same complex [17].
• Combined biochemical, functional, and genetic analysis lead us to propose that End4p may mediate endocytosis through interaction with other actin-associated proteins, perhaps Rvs167p, a protein essential for endocytosis [18].

References