Number of the records: 1  

ABP1 Mediates Auxin Inhibition of Clathrin-Dependent Endocytosis in Arabidopsis

  1. 1.
    0350344 - ÚEB 2011 RIV US eng J - Článek v odborném periodiku
    Robert, S. - Kleine-Vehn, J. - Barbez, E. - Sauer, M. - Paciorek, T. - Baster, P. - Vanneste, S. - Zhang, J. - Simon, Sibu - Čovanová, Milada - Hayashi, K. - Dhonukshe, P. - Yang, Z. - Bednarek, S.Y. - Jones, A.M. - Luschnig, Ch. - Aniento, F. - Zažímalová, Eva - Friml, J.
    ABP1 Mediates Auxin Inhibition of Clathrin-Dependent Endocytosis in Arabidopsis.
    Cell. Roč. 143, č. 1 (2010), s. 111-121. ISSN 0092-8674. E-ISSN 1097-4172
    Grant CEP: GA MŠMT(CZ) LC06034
    Výzkumný záměr: CEZ:AV0Z50380511
    Klíčová slova: auxin * clathrin-mediated endocytosis * PIN proteins
    Kód oboru RIV: ED - Fyziologie
    Impakt faktor: 32.401, rok: 2010DOI: https://doi.org/10.1016/j.cell.2010.09.027

    Spatial distribution of the plant hormone auxin regulates multiple aspects of plant development. These self-regulating auxin gradients are established by the action of PIN auxin transporters, whose activity is regulated by their constitutive cycling between the plasma membrane and endosomes. Here, we show that auxin signaling by the auxin receptor AUXIN-BINDING PROTEIN 1 (ABP1) inhibits the clathrin-mediated internalization of PIN proteins. ABP1 acts as a positive factor in clathrin recruitment to the plasma membrane, thereby promoting endocytosis. Auxin binding to ABP1 interferes with this action and leads to the inhibition of clathrin-mediated endocytosis. Our study demonstrates that ABP1 mediates a nontranscriptional auxin signaling that regulates the evolutionarily conserved process of clathrin-mediated endocytosis and suggests that this signaling may be essential for the developmentally important feedback of auxin on its own transport.
    Trvalý link: http://hdl.handle.net/11104/0190367

     
    Název souboruStaženoVelikostKomentářVerzePřístup
    2010_Robert_CELL_111.pdf42 MBJinápovolen
     
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.