VRP1/YLR337C Literature Guide Help

Other names published for VRP1: END5, MDP2, YLR337W, verprolin, YLR337C

VRP1 - Protein-protein Interactions (23)

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
Grotsch H, et al.  (2010) Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites. EMBO J 29(17):2899-914
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
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
Barker SL, et al.  (2007) Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis. Mol Biol Cell 18(8):2893-903
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
Hardwidge PR, et al.  (2006) Proteomic analysis of the binding partners to enteropathogenic Escherichia coli virulence proteins expressed in Saccharomyces cerevisiae. Proteomics 6(7):2174-9
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
Ren G, et al.  (2005) Verprolin cytokinesis function mediated by the Hof one trap domain. Traffic 6(7):575-93
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
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
Naqvi SN, et al.  (2001) Vrp1p functions in both actomyosin ring-dependent and Hof1p-dependent pathways of cytokinesis. Traffic 2(3):189-201
Smith MG, et al.  (2001) The life cycle of actin patches in mating yeast. J Cell Sci 114(Pt 8):1505-13
de Bettignies G, et al.  (2001) Overactivation of the protein kinase C-signaling pathway suppresses the defects of cells lacking the Rho3/Rho4-GAP Rgd1p in Saccharomyces cerevisiae. Genetics 159(4):1435-48
Evangelista M, et al.  (2000) A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. J Cell Biol 148(2):353-62
Geli MI, et al.  (2000) An intact SH3 domain is required for myosin I-induced actin polymerization. EMBO J 19(16):4281-91
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
Madania A, et al.  (1999) The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex. Mol Biol Cell 10(10):3521-38
Anderson BL, et al.  (1998) The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J Cell Biol 141(6):1357-70
Naqvi SN, et al.  (1998) The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast. Curr Biol 8(17):959-62
Vaduva G, et al.  (1997) Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton. J Cell Biol 139(7):1821-33