LAS17/YOR181W Literature Guide Help

Other names published for LAS17: BEE1, YOR181W

LAS17 - Protein-protein Interactions (39)

ReferenceOther Genes Addressed
Feliciano D and Di Pietro SM  (2012) SLAC, a complex between Sla1 and Las17, regulates actin polymerization during clathrin-mediated endocytosis. Mol Biol Cell 23(21):4256-72
Chernova TA, et al.  (2011) Prion induction by the short-lived, stress-induced protein lsb2 is regulated by ubiquitination and association with the actin cytoskeleton. Mol Cell 43(2):242-52
Gorelik M, et al.  (2011) A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function. J Biol Chem 286(22):19470-7
Kaminska J, et al.  (2011) Yeast Rsp5 ubiquitin ligase affects the actin cytoskeleton in vivo and in vitro. Eur J Cell Biol 90(12):1016-28
Liu SL, et al.  (2011) Mechanism of a concentration-dependent switch between activation and inhibition of Arp2/3 complex by coronin. J Biol Chem 286(19):17039-46
Balcer HI, et al.  (2010) The p40/ARPC1 Subunit of Arp2/3 Complex Performs Multiple Essential Roles in WASp-regulated Actin Nucleation. J Biol Chem 285(11):8481-91
Michelot A, et al.  (2010) Reconstitution and protein composition analysis of endocytic actin patches. Curr Biol 20(21):1890-9
Wong MH, et al.  (2010) Vrp1p-Las17p interaction is critical for actin patch polarization but is not essential for growth or fluid phase endocytosis in S. cerevisiae. Biochim Biophys Acta 1803(12):1332-46
Boettner DR, et al.  (2009) The F-BAR protein Syp1 negatively regulates WASp-Arp2/3 complex activity during endocytic patch formation. Curr Biol 19(23):1979-87
Rajmohan R, et al.  (2009) Las17p-Vrp1p but not Las17p-Arp2/3 interaction is important for actin patch polarization in yeast. Biochim Biophys Acta 1793(5):825-35
Robertson AS, et al.  (2009) The WASP homologue Las17 activates the novel actin-regulatory activity of Ysc84 to promote endocytosis in yeast. Mol Biol Cell 20(6):1618-28
Tarassov K, et al.  (2008) An in vivo map of the yeast protein interactome. Science 320(5882):1465-70
Thanabalu T, et al.  (2007) Verprolin function in endocytosis and actin organization. Roles of the Las17p (yeast WASP)-binding domain and a novel C-terminal actin-binding domain. FEBS J 274(16):4103-25
Lehrach WP, et al.  (2006) A regularized discriminative model for the prediction of protein-peptide interactions. Bioinformatics 22(5):532-40
Musi V, et al.  (2006) New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae. Protein Sci 15(4):795-807
Chang FS, et al.  (2005) A WASp-binding type II phosphatidylinositol 4-kinase required for actin polymerization-driven endosome motility. J Cell Biol 171(1):133-42
Costa R, et al.  (2005) Lsb5p interacts with actin regulators Sla1p and Las17p, ubiquitin and Arf3p to couple actin dynamics to membrane trafficking processes. Biochem J 387(Pt 3):649-58
Germann M, et al.  (2005) Characterizing the sphingolipid signaling pathway that remediates defects associated with loss of the yeast amphiphysin-like orthologs, Rvs161p and Rvs167p. J Biol Chem 280(6):4270-8
Friesen H, et al.  (2003) Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation. Mol Biol Cell 14(7):3027-40
Gourlay CW, et al.  (2003) An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast. J Cell Sci 116(Pt 12):2551-64
Rodal AA, et al.  (2003) Negative regulation of yeast WASp by two SH3 domain-containing proteins. Curr Biol 13(12):1000-8
Li H, et al.  (2002) Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth to daughter cells and interact with cis-Golgi protein Kre6p. Yeast 19(13):1097-112
Mochida J, et al.  (2002) The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae. Genetics 160(3):923-34
Roumanie O, et al.  (2002) Functional interactions between the VRP1-LAS17 and RHO3-RHO4 genes involved in actin cytoskeleton organization in Saccharomyces cerevisiae. Curr Genet 40(5):317-25
Soulard A, et al.  (2002) Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro. Mol Cell Biol 22(22):7889-906
Tong AH, et al.  (2002) A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules. Science 295(5553):321-4
Warren DT, et al.  (2002) Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics. J Cell Sci 115(Pt 8):1703-15
Lechler T, et al.  (2001) A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast. J Cell Biol 155(2):261-70
Smith MG, et al.  (2001) The life cycle of actin patches in mating yeast. J Cell Sci 114(Pt 8):1505-13
Volkmann N, et al.  (2001) Structure of Arp2/3 complex in its activated state and in actin filament branch junctions. Science 293(5539):2456-9