Gene Symbol: RVS161
Description: amphiphysin-like protein RVS161
Alias: END6, FUS7, SPE161, amphiphysin-like protein RVS161
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Henry K, D hondt K, Chang J, Newpher T, Huang K, Hudson R, et al. Scd5p and clathrin function are important for cortical actin organization, endocytosis, and localization of sla2p in yeast. Mol Biol Cell. 2002;13:2607-25 pubmed
    ..Therefore, Scd5p and clathrin are important for actin organization and endocytosis, and Sla2p may provide a critical link between clathrin and the actin cytoskeleton in yeast, similar to HIP1(R) in animal cells. ..
  2. Germann M, Swain E, Bergman L, Nickels J. Characterizing the sphingolipid signaling pathway that remediates defects associated with loss of the yeast amphiphysin-like orthologs, Rvs161p and Rvs167p. J Biol Chem. 2005;280:4270-8 pubmed
    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...
  3. Lombardi R, Riezman H. Rvs161p and Rvs167p, the two yeast amphiphysin homologs, function together in vivo. J Biol Chem. 2001;276:6016-22 pubmed
    Mutations in RVS161 and RVS167, the two yeast amphiphysin homologs, cause very similar growth phenotypes, a depolarized actin cytoskeleton, and a defect in the internalization step of endocytosis...
  4. Colwill K, Field D, Moore L, Friesen J, Andrews B. In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions. Genetics. 1999;152:881-93 pubmed
    ..Upon activation, Rvs167p enters a multiprotein complex, making critical contacts in its BAR domain and redundant or minor contacts with its SH3 domain. ..
  5. Kaksonen M, Toret C, Drubin D. A modular design for the clathrin- and actin-mediated endocytosis machinery. Cell. 2005;123:305-20 pubmed
  6. Brizzio V, Gammie A, Rose M. Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae. J Cell Biol. 1998;141:567-84 pubmed
    ..Here we show that FUS7 is allelic to RVS161/END6, a gene implicated in a variety of processes including viability after starvation, endocytosis, and actin ..
  7. Sivadon P, Bauer F, Aigle M, Crouzet M. Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin. Mol Gen Genet. 1995;246:485-95 pubmed
    The actin cytoskeleton cells is altered in rvs161 mutant yeast, with the defect becoming more pronounced under unfavorable growth conditions, as described for the rvs167 mutant...
  8. Navarro P, Durrens P, Aigle M. Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae. Biochim Biophys Acta. 1997;1343:187-92 pubmed
    As previous studies indicated that the RVS161 and RVS167 gene products of Saccharomyces cerevisiae seem to be involved in the same cellular function, we considered the possibility of a complex between the proteins encoded by these two ..
  9. Munn A, Stevenson B, Geli M, Riezman H. end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol Biol Cell. 1995;6:1721-42 pubmed
    ..end5-1, end6-1, and end7-1 are allelic to VRP1, RVS161, and ACT1, respectively. VRP1 and RVS161 are required for correct actin localization and ACT1 encodes actin...

More Information


  1. McCourt P, Morgan J, Nickels J. Stress-induced ceramide-activated protein phosphatase can compensate for loss of amphiphysin-like activity in Saccharomyces cerevisiae and functions to reinitiate endocytosis. J Biol Chem. 2009;284:11930-41 pubmed publisher
    Saccharomyces cerevisiae cells lacking the amphiphysin-like orthologs, Rvs161 or Rvs167, are unable to thrive under many stress conditions...
  2. Morgan J, McCourt P, Rankin L, Swain E, Rice L, Nickels J. Altering sphingolipid metabolism in Saccharomyces cerevisiae cells lacking the amphiphysin ortholog Rvs161 reinitiates sugar transporter endocytosis. Eukaryot Cell. 2009;8:779-89 pubmed publisher
    ..Saccharomyces cerevisiae cells lacking the amphiphysin ortholog Rvs161 are inviable when starved for glucose...
  3. Desfarges L, Durrens P, Juguelin H, Cassagne C, Bonneu M, Aigle M. Yeast mutants affected in viability upon starvation have a modified phospholipid composition. Yeast. 1993;9:267-77 pubmed
    Selection of mutations, based on the suppression of rvs161 delta defects, was performed. Ten mutants were obtained, ranged amongst four complementation groups, named SUR1, SUR2, SUR3 and SUR4...
  4. Balguerie A, Bagnat M, Bonneu M, Aigle M, Breton A. Rvs161p and sphingolipids are required for actin repolarization following salt stress. Eukaryot Cell. 2002;1:1021-31 pubmed
    ..bud emergence and septa, and was found to be associated with lipid rafts. An important link between sphingolipids and actin polarization is that Rvs161p was required for actin repolarization and was found to be located in lipid rafts. ..
  5. Crouzet M, Urdaci M, Dulau L, Aigle M. Yeast mutant affected for viability upon nutrient starvation: characterization and cloning of the RVS161 gene. Yeast. 1991;7:727-43 pubmed
    ..Among them the rvs161 mutant (RVS for Reduced Viability upon Starvation) is sensitive to carbon, nitrogen and sulphur starvation...
  6. Bari V, Sharma S, Alfatah M, Mondal A, Ganesan K. Plasma Membrane Proteolipid 3 Protein Modulates Amphotericin B Resistance through Sphingolipid Biosynthetic Pathway. Sci Rep. 2015;5:9685 pubmed publisher
    ..Moreover, AmB sensitivity of strains deleted in PMP3 can be suppressed by the addition of phytosphingosine, a sphingolipid pathway intermediate, confirming the importance of this pathway in modulation of AmB resistance by PMP3. ..
  7. Murphy E, Boxberger J, Colvin R, Lee S, Zahn G, Loor F, et al. Pil1, an eisosome organizer, plays an important role in the recruitment of synaptojanins and amphiphysins to facilitate receptor-mediated endocytosis in yeast. Eur J Cell Biol. 2011;90:825-33 pubmed publisher
    ..Pil1 also greatly affected both the scission efficiency and the frequency of formation of endocytic sites carrying Rvs161- and Rvs167-GFP...
  8. Talarek N, Balguerie A, Aigle M, Durrens P. A novel link between a rab GTPase and Rvs proteins: the yeast amphiphysin homologues. Cell Biochem Funct. 2005;23:253-66 pubmed
    ..Altogether, these data support the hypothesis that both Rvsp proteins act in vesicular traffic through physical and functional interactions with Ypt/Rab regulators. ..
  9. Gammie A, Brizzio V, Rose M. Distinct morphological phenotypes of cell fusion mutants. Mol Biol Cell. 1998;9:1395-410 pubmed
    ..pathway of cell fusion, we phenotypically and genetically characterized four cell fusion mutants, fus6/spa2, fus7/rvs161, fus1, and fus2. First, we examined the complete array of single and double mutants...
  10. Stein R, Smith J, Rose M. An Amphiphysin-Like Domain in Fus2p Is Required for Rvs161p Interaction and Cortical Localization. G3 (Bethesda). 2015;6:337-49 pubmed publisher
    ..We conclude that the Fus2p CTD mediates an additional, Rvs161p-independent interaction at the shmoo tip. ..
  11. Smaczynska de Rooij I, Allwood E, Mishra R, Booth W, Aghamohammadzadeh S, Goldberg M, et al. Yeast dynamin Vps1 and amphiphysin Rvs167 function together during endocytosis. Traffic. 2012;13:317-28 pubmed publisher
    ..In vitro, an Rvs161/Rvs167 heterodimer can disassemble Vps1 oligomers...
  12. Nelson B, Parsons A, Evangelista M, Schaefer K, Kennedy K, Ritchie S, et al. Fus1p interacts with components of the Hog1p mitogen-activated protein kinase and Cdc42p morphogenesis signaling pathways to control cell fusion during yeast mating. Genetics. 2004;166:67-77 pubmed
    ..Taken together, our results suggest that Fus1p acts as a scaffold for the assembly of a cell surface complex involved in polarized secretion of septum-degrading enzymes and inhibition of HOG pathway signaling to promote cell fusion. ..
  13. Orlando K, Sun X, Zhang J, Lu T, Yokomizo L, Wang P, et al. Exo-endocytic trafficking and the septin-based diffusion barrier are required for the maintenance of Cdc42p polarization during budding yeast asymmetric growth. Mol Biol Cell. 2011;22:624-33 pubmed publisher
    ..Collectively, membrane trafficking and septins function synergistically to maintain the dynamic polarization of Cdc42p during asymmetric growth in yeast. ..
  14. Clark M, Teply J, Haarer B, Viggiano S, Sept D, Amberg D. A genetic dissection of Aip1p's interactions leads to a model for Aip1p-cofilin cooperative activities. Mol Biol Cell. 2006;17:1971-84 pubmed
    ..We theorize that Aip1p-severing activity may involve simultaneous binding to two actin subunits with cofilin wedged between the two actin binding sites of the N- and C-terminal propeller domains. ..
  15. Fitch P, Gammie A, Lee D, de Candal V, Rose M. Lrg1p Is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Genetics. 2004;168:733-46 pubmed
    ..We conclude that Lrg1p is a Rho1p-GAP involved in cell fusion and speculate that it acts to locally inhibit cell wall synthesis to aid in the close apposition of the plasma membranes of mating cells. ..
  16. Youn J, Friesen H, Kishimoto T, Henne W, Kurat C, Ye W, et al. Dissecting BAR domain function in the yeast Amphiphysins Rvs161 and Rvs167 during endocytosis. Mol Biol Cell. 2010;21:3054-69 pubmed publisher
    ..The only known N-BAR-domain proteins in the budding yeast Saccharomyces cerevisiae, Rvs161 and Rvs167, are required for endocytosis...
  17. Myers M, Ryazantsev S, Hicke L, Payne G. Calmodulin Promotes N-BAR Domain-Mediated Membrane Constriction and Endocytosis. Dev Cell. 2016;37:162-73 pubmed publisher
    ..These studies reveal a conserved role for calmodulin in regulating the intrinsic membrane-sculpting activity of endocytic N-BAR domains. ..
  18. Breton A, Schaeffer J, Aigle M. The yeast Rvs161 and Rvs167 proteins are involved in secretory vesicles targeting the plasma membrane and in cell integrity. Yeast. 2001;18:1053-68 pubmed
    The Rvs161 and Rvs167 proteins are known to play a role in actin cytokeleton organization and endocytosis. Moreover, Rvs167p functionally interacts with the myosin Myo2p...