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Gene Review

VRP1  -  Vrp1p

Saccharomyces cerevisiae S288c

Synonyms: END5, L8300.13, MDP2, Verprolin, YLR337C, ...
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Disease relevance of VRP1


High impact information on VRP1

  • During patch assembly in vivo, Wsp1p and Vrp1p arrive first independent of Myo1p [2].
  • Myo1p is a weaker Arp2/3 complex activator that makes unstable branches and is enhanced by verprolin [2].
  • N-Vrp1 function is not abolished by mutations affecting the WASP homology 2 (WH2) [verprolin homology (V)] actin-binding domain [3].
  • N-Vrp1 exhibits diffuse cytoplasmic localization and functions in cytokinesis without efficiently restoring polarization of cortical actin patches [3].
  • Consistent with this, Myo5p patches assemble but do not localize to sites of polarized cell surface growth in a VRP1 deletion mutant [4].

Biological context of VRP1


Anatomical context of VRP1


Associations of VRP1 with chemical compounds


Physical interactions of VRP1

  • Here, we show the ability of this Vrp1 fragment to bind the Hof1 SH3 domain via its Hof one trap (HOT) domain is critical for cytokinesis [6].
  • Using the two-hybrid system, we show that verprolin binds actin [5].

Co-localisations of VRP1

  • In fixed cells hemagglutinin-tagged Vrp1p often co-localizes with actin in cortical patches [5].

Regulatory relationships of VRP1

  • Previously we reported that additional actin suppresses the temperature-dependent growth defect caused by a mutation in VRP1 [5].
  • The Vrp1 HOT domain promotes cytokinesis by binding to the Hof1 SH3 domain and counteracting its inhibitory effect [6].
  • These results suggest that Mti1p and Vrp1p antagonistically regulate type I myosin functions [1].

Other interactions of VRP1

  • The actin cytoskeleton organization is also aberrant in mdp2 cells [9].
  • Twenty-five mutants defining four complementation groups, mdp1, mdp2, mdp3, and mdp4, were found [9].
  • These and other well-established data support the idea that Vrp1, Las17, Rvs167 proteins belong to the same complex [10].
  • Genetic relationships between either VRP1 or RGD1 and actin cytoskeleton-linked genes were also studied [10].
  • Here, we demonstrate further that these proteins together with Vrp1p form a multivalent Arp2/3-activating complex [11].


  1. 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. Mochida, J., Yamamoto, T., Fujimura-Kamada, K., Tanaka, K. Genetics (2002) [Pubmed]
  2. Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast. Sirotkin, V., Beltzner, C.C., Marchand, J.B., Pollard, T.D. J. Cell Biol. (2005) [Pubmed]
  3. Functions of Vrp1p in cytokinesis and actin patches are distinct and neither requires a WH2/V domain. Thanabalu, T., Munn, A.L. EMBO J. (2001) [Pubmed]
  4. 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. Anderson, B.L., Boldogh, I., Evangelista, M., Boone, C., Greene, L.A., Pon, L.A. J. Cell Biol. (1998) [Pubmed]
  5. Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton. Vaduva, G., Martin, N.C., Hopper, A.K. J. Cell Biol. (1997) [Pubmed]
  6. Verprolin cytokinesis function mediated by the Hof one trap domain. Ren, G., Wang, J., Brinkworth, R., Winsor, B., Kobe, B., Munn, A.L. Traffic (2005) [Pubmed]
  7. Enhanced membrane fusion in sterol-enriched vacuoles bypasses the Vrp1p requirement. Tedrick, K., Trischuk, T., Lehner, R., Eitzen, G. Mol. Biol. Cell (2004) [Pubmed]
  8. Cell wall biogenesis in Chlamydomonas: molecular characterization of a novel protein whose expression is up-regulated during matrix formation. Kurvari, V. Mol. Gen. Genet. (1997) [Pubmed]
  9. Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3' ends and/or protein synthesis in mitochondrial delivery. Zoladek, T., Vaduva, G., Hunter, L.A., Boguta, M., Go, B.D., Martin, N.C., Hopper, A.K. Mol. Cell. Biol. (1995) [Pubmed]
  10. 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]
  11. A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast. Lechler, T., Jonsdottir, G.A., Klee, S.K., Pellman, D., Li, R. J. Cell Biol. (2001) [Pubmed]
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