VRP1/YLR337C Literature Guide Help

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

VRP1 - Protein Sequence Features (9)

ReferenceOther Genes Addressed
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
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
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
Thanabalu T and Munn AL  (2001) Functions of Vrp1p in cytokinesis and actin patches are distinct and neither requires a WH2/V domain. EMBO J 20(24):6979-89
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
Miki H and Takenawa T  (1998) Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization. Biochem Biophys Res Commun 243(1):73-8
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