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Gene Review

RVS167  -  amphiphysin

Saccharomyces cerevisiae S288c

Synonyms: D9509.8, Reduced viability upon starvation protein 167, YDR388W
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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


Anatomical context of RVS167


Associations of RVS167 with chemical compounds


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


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].


  1. Role of SH3 domain-containing proteins in clathrin-mediated vesicle trafficking in Arabidopsis. Lam, B.C., Sage, T.L., Bianchi, F., Blumwald, E. Plant Cell (2001) [Pubmed]
  2. Combining chemical genetics and proteomics to identify protein kinase substrates. Dephoure, N., Howson, R.W., Blethrow, J.D., Shokat, K.M., O'Shea, E.K. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  3. 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]
  4. The Sur7p family defines novel cortical domains in Saccharomyces cerevisiae, affects sphingolipid metabolism, and is involved in sporulation. Young, M.E., Karpova, T.S., Brügger, B., Moschenross, D.M., Wang, G.K., Schneiter, R., Wieland, F.T., Cooper, J.A. Mol. Cell. Biol. (2002) [Pubmed]
  5. 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]
  6. 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]
  7. 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]
  8. Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton. Lila, T., Drubin, D.G. Mol. Biol. Cell (1997) [Pubmed]
  9. In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions. Colwill, K., Field, D., Moore, L., Friesen, J., Andrews, B. Genetics (1999) [Pubmed]
  10. 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]
  11. 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]
  12. Rvs167p, the budding yeast homolog of amphiphysin, colocalizes with actin patches. Balguerie, A., Sivadon, P., Bonneu, M., Aigle, M. J. Cell. Sci. (1999) [Pubmed]
  13. The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167. Stamenova, S.D., Dunn, R., Adler, A.S., Hicke, L. J. Biol. Chem. (2004) [Pubmed]
  14. Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae. Navarro, P., Durrens, P., Aigle, M. Biochim. Biophys. Acta (1997) [Pubmed]
  15. A novel link between a rab GTPase and Rvs proteins: the yeast amphiphysin homologues. Talarek, N., Balguerie, A., Aigle, M., Durrens, P. Cell Biochem. Funct. (2005) [Pubmed]
  16. Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation. Friesen, H., Murphy, K., Breitkreutz, A., Tyers, M., Andrews, B. Mol. Biol. Cell (2003) [Pubmed]
  17. Evidence for the genetic interaction between the actin-binding protein Vrp1 and the RhoGAP Rgd1 mediated through Rho3p and Rho4p in Saccharomyces cerevisiae. Roumanie, O., Peypouquet, M.F., Bonneu, M., Thoraval, D., Doignon, F., Crouzet, M. Mol. Microbiol. (2000) [Pubmed]
  18. End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae. Wesp, A., Hicke, L., Palecek, J., Lombardi, R., Aust, T., Munn, A.L., Riezman, H. Mol. Biol. Cell (1997) [Pubmed]
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