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Gene Review

RVS161  -  amphiphysin-like protein RVS161

Saccharomyces cerevisiae S288c

Synonyms: END6, FUS7, Reduced viability upon starvation protein 161, SPE161, YCR009C, ...
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High impact information on RVS161


Biological context of RVS161


Anatomical context of RVS161


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


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].


  1. Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae. Brizzio, V., Gammie, A.E., Rose, M.D. J. Cell Biol. (1998) [Pubmed]
  2. The amphiphysin-like protein 1 (ALP1) interacts functionally with the cABL tyrosine kinase and may play a role in cytoskeletal regulation. Kadlec, L., Pendergast, A.M. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  3. Amphiphysin I antisense oligonucleotides inhibit neurite outgrowth in cultured hippocampal neurons. Mundigl, O., Ochoa, G.C., David, C., Slepnev, V.I., Kabanov, A., De Camilli, P. J. Neurosci. (1998) [Pubmed]
  4. Characterizing the sphingolipid signaling pathway that remediates defects associated with loss of the yeast amphiphysin-like orthologs, Rvs161p and Rvs167p. Germann, M., Swain, E., Bergman, L., Nickels, J.T. J. Biol. Chem. (2005) [Pubmed]
  5. Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin. Sivadon, P., Bauer, F., Aigle, M., Crouzet, M. Mol. Gen. Genet. (1995) [Pubmed]
  6. Functional assessment of the yeast Rvs161 and Rvs167 protein domains. Sivadon, P., Crouzet, M., Aigle, M. FEBS Lett. (1997) [Pubmed]
  7. Characterization of the yeast amphiphysins Rvs161p and Rvs167p reveals roles for the Rvs heterodimer in vivo. Friesen, H., Humphries, C., Ho, Y., Schub, O., Colwill, K., Andrews, B. Mol. Biol. Cell (2006) [Pubmed]
  8. Yeast mutant affected for viability upon nutrient starvation: characterization and cloning of the RVS161 gene. Crouzet, M., Urdaci, M., Dulau, L., Aigle, M. Yeast (1991) [Pubmed]
  9. The yeast Rvs161 and Rvs167 proteins are involved in secretory vesicles targeting the plasma membrane and in cell integrity. Breton, A.M., Schaeffer, J., Aigle, M. Yeast (2001) [Pubmed]
  10. Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae. Navarro, P., Durrens, P., Aigle, M. Biochim. Biophys. Acta (1997) [Pubmed]
  11. Human BIN3 complements the F-actin localization defects caused by loss of Hob3p, the fission yeast homolog of Rvs161p. Routhier, E.L., Burn, T.C., Abbaszade, I., Summers, M., Albright, C.F., Prendergast, G.C. J. Biol. Chem. (2001) [Pubmed]
  12. Distinct morphological phenotypes of cell fusion mutants. Gammie, A.E., Brizzio, V., Rose, M.D. Mol. Biol. Cell (1998) [Pubmed]
  13. Cloning of the multicopy suppressor gene SUR7: evidence for a functional relationship between the yeast actin-binding protein Rvs167 and a putative membranous protein. Sivadon, P., Peypouquet, M.F., Doignon, F., Aigle, M., Crouzet, M. Yeast (1997) [Pubmed]
  14. The complete sequence of a 10.8 kb segment distal of SUF2 on the right arm of chromosome III from Saccharomyces cerevisiae reveals seven open reading frames including the RVS161, ADP1 and PGK genes. Skala, J., Purnelle, B., Goffeau, A. Yeast (1992) [Pubmed]
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