Simultaneous Binding of PtdIns(4,5)P <sub>2</sub> and Clathrin by AP180 in the Nucleation of Clathrin Lattices on Membranes

  • Marijn G. J. Ford
    Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
  • Barbara M. F. Pearse
    Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
  • Matthew K. Higgins
    Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
  • Yvonne Vallis
    Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
  • David J. Owen
    Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
  • Adele Gibson
    Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
  • Colin R. Hopkins
    Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
  • Philip R. Evans
    Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
  • Harvey T. McMahon
    Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.

抄録

<jats:p> Adaptor protein 180 (AP180) and its homolog, clathrin assembly lymphoid myeloid leukemia protein (CALM), are closely related proteins that play important roles in clathrin-mediated endocytosis. Here, we present the structure of the NH <jats:sub>2</jats:sub> -terminal domain of CALM bound to phosphatidylinositol-4,5- bisphosphate [PtdIns(4,5)P <jats:sub>2</jats:sub> ] via a lysine-rich motif. This motif is found in other proteins predicted to have domains of similar structure (for example, Huntingtin interacting protein 1). The structure is in part similar to the epsin NH <jats:sub>2</jats:sub> -terminal (ENTH) domain, but epsin lacks the PtdIns(4,5)P <jats:sub>2</jats:sub> -binding site. Because AP180 could bind to PtdIns(4,5)P <jats:sub>2</jats:sub> and clathrin simultaneously, it may serve to tether clathrin to the membrane. This was shown by using purified components and a budding assay on preformed lipid monolayers. In the presence of AP180, clathrin lattices formed on the monolayer. When AP2 was also present, coated pits were formed. </jats:p>

収録刊行物

  • Science

    Science 291 (5506), 1051-1055, 2001-02-09

    American Association for the Advancement of Science (AAAS)

被引用文献 (22)*注記

もっと見る

詳細情報 詳細情報について

問題の指摘

ページトップへ