The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

APP1  -  phosphatidate phosphatase APP1

Saccharomyces cerevisiae S288c

Synonyms: Actin patch protein 1, N2219, PAP, Phosphatidate phosphatase APP1, YNL094W
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on APP1

  • Furthermore, these cofilin mutants provided an opportunity to distinguish in living cells those actin functions that depend specifically on filament turnover (endocytosis) from those that do not (cortical actin patch motility) [1].
  • Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast [2].
  • Using a strain defective in polarized secretion and actin-patch organization, we showed that a change in actin-patch organization could be a consequence of the fusion of mistargeted vesicles with the plasma membrane [3].
  • These results suggest that Ark1p and Prk1p may be downstream effectors of signaling pathways that control actin patch organization and function [4].
  • Cortical recruitment of Sjl2 requires the actin patch component Abp1 [5].

Biological context of APP1


Other interactions of APP1


  1. Cofilin promotes rapid actin filament turnover in vivo. Lappalainen, P., Drubin, D.G. Nature (1997) [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. The GAP activity of Msb3p and Msb4p for the Rab GTPase Sec4p is required for efficient exocytosis and actin organization. Gao, X.D., Albert, S., Tcheperegine, S.E., Burd, C.G., Gallwitz, D., Bi, E. J. Cell Biol. (2003) [Pubmed]
  4. Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast. Cope, M.J., Yang, S., Shang, C., Drubin, D.G. J. Cell Biol. (1999) [Pubmed]
  5. The phosphoinositide phosphatase Sjl2 is recruited to cortical actin patches in the control of vesicle formation and fission during endocytosis. Stefan, C.J., Padilla, S.M., Audhya, A., Emr, S.D. Mol. Cell. Biol. (2005) [Pubmed]
  6. The yeast V159N actin mutant reveals roles for actin dynamics in vivo. Belmont, L.D., Drubin, D.G. J. Cell Biol. (1998) [Pubmed]
  7. Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth to daughter cells and interact with cis-Golgi protein Kre6p. Li, H., Pagé, N., Bussey, H. Yeast (2002) [Pubmed]
  8. Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology. Ayscough, K.R., Eby, J.J., Lila, T., Dewar, H., Kozminski, K.G., Drubin, D.G. Mol. Biol. Cell (1999) [Pubmed]
  9. The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex. Madania, A., Dumoulin, P., Grava, S., Kitamoto, H., Schärer-Brodbeck, C., Soulard, A., Moreau, V., Winsor, B. Mol. Biol. Cell (1999) [Pubmed]
  10. Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics. Warren, D.T., Andrews, P.D., Gourlay, C.W., Ayscough, K.R. J. Cell. Sci. (2002) [Pubmed]
  11. The Sur7p family defines novel cortical domains in Saccharomyces cerevisiae, affects sphingolipid metabolism, and is involved in sporulation. Young, M.E., Karpova, T.S., Brügger, B., Moschenross, D.M., Wang, G.K., Schneiter, R., Wieland, F.T., Cooper, J.A. Mol. Cell. Biol. (2002) [Pubmed]
  12. Yeast actin patches are networks of branched actin filaments. Young, M.E., Cooper, J.A., Bridgman, P.C. J. Cell Biol. (2004) [Pubmed]
WikiGenes - Universities