RVS167/YDR388W Literature Guide Help

Other names published for RVS167: YDR388W

RVS167 - Function/Process (21)

ReferenceOther Genes Addressed
Kukulski W, et al.  (2012) Plasma Membrane Reshaping during Endocytosis Is Revealed by Time-Resolved Electron Tomography. Cell 150(3):508-20
Kishimoto T, et al.  (2011) Determinants of endocytic membrane geometry, stability, and scission. Proc Natl Acad Sci U S A 108(44):E979-88
Prigent M, et al.  (2011) The RabGAP proteins Gyp5p and Gyl1p recruit the BAR domain protein Rvs167p for polarized exocytosis. Traffic 12(8):1084-97
Gallego O, et al.  (2010) A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Mol Syst Biol 6():430
Youn JY, et al.  (2010) Dissecting BAR Domain Function in the Yeast Amphiphysins Rvs161 and Rvs167 during Endocytosis. Mol Biol Cell 21(17):3054-69
Hess DC, et al.  (2009) Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis. PLoS Genet 5(3):e1000407
Gray JV and Krause SA  (2007) Identifying in vivo pathways using genome-wide genetic networks. Biochem Soc Trans 35(Pt 6):1538-41
Friesen H, et al.  (2005) Interaction of the Saccharomyces cerevisiae cortical actin patch protein Rvs167p with proteins involved in ER to Golgi vesicle trafficking. Genetics 170(2):555-68
Friesen H, et al.  (2003) Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation. Mol Biol Cell 14(7):3027-40
Dimmer KS, et al.  (2002) Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol Biol Cell 13(3):847-53
Young ME, et al.  (2002) The Sur7p family defines novel cortical domains in Saccharomyces cerevisiae, affects sphingolipid metabolism, and is involved in sporulation. Mol Cell Biol 22(3):927-34
Breton AM, et al.  (2001) The yeast Rvs161 and Rvs167 proteins are involved in secretory vesicles targeting the plasma membrane and in cell integrity. Yeast 18(11):1053-68
Lombardi R and Riezman H  (2001) Rvs161p and Rvs167p, the two yeast amphiphysin homologs, function together in vivo. J Biol Chem 276(8):6016-22
Routhier EL, et al.  (2001) Human BIN3 complements the F-actin localization defects caused by loss of Hob3p, the fission yeast homolog of Rvs161p. J Biol Chem 276(24):21670-7
Bon E, et al.  (2000) A network of proteins around Rvs167p and Rvs161p, two proteins related to the yeast actin cytoskeleton. Yeast 16(13):1229-41
Roumanie O, et al.  (2000) Evidence for the genetic interaction between the actin-binding protein Vrp1 and the RhoGAP Rgd1 mediated through Rho3p and Rho4p in Saccharomyces cerevisiae. Mol Microbiol 36(6):1403-14
Breton AM and Aigle M  (1998) Genetic and functional relationship between Rvsp, myosin and actin in Saccharomyces cerevisiae. Curr Genet 34(4):280-6
Lee J, et al.  (1998) Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase complexes may link the cell cycle to the actin cytoskeleton. Curr Biol 8(24):1310-21
Singer-Kruger B and Ferro-Novick S  (1997) Use of a synthetic lethal screen to identify yeast mutants impaired in endocytosis, vacuolar protein sorting and the organization of the cytoskeleton. Eur J Cell Biol 74(4):365-75
Munn AL, et al.  (1995) end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol Biol Cell 6(12):1721-42
Bauer F, et al.  (1993) Alteration of a yeast SH3 protein leads to conditional viability with defects in cytoskeletal and budding patterns. Mol Cell Biol 13(8):5070-84