Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins

DOI Web Site 被引用文献1件
  • Rubén C. Aguilar
    Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
  • Silvia A. Longhi
    Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
  • Jonathan D. Shaw
    Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
  • Lan-Yu Yeh
    Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
  • Sean Kim
    Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
  • Arne Schön
    Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
  • Ernesto Freire
    Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
  • Ariel Hsu
    Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
  • William K. McCormick
    Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
  • Hadiya A. Watson
    Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
  • Beverly Wendland
    Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218

抄録

<jats:p> Epsins are endocytic proteins with a structured epsin N-terminal homology (ENTH) domain that binds phosphoinositides and a poorly structured C-terminal region that interacts with ubiquitin and endocytic machinery, including clathrin and endocytic scaffolding proteins. Yeast has two redundant genes encoding epsins, <jats:italic>ENT1</jats:italic> and <jats:italic>ENT2</jats:italic> ; deleting both genes is lethal. We demonstrate that the ENTH domain is both necessary and sufficient for viability of <jats:italic>ent1</jats:italic> Δ <jats:italic>ent2</jats:italic> Δ cells. Mutational analysis of the ENTH domain revealed a surface patch that is essential for viability and that binds guanine nucleotide triphosphatase-activating proteins for Cdc42, a critical regulator of cell polarity in all eukaryotes. Furthermore, the epsins contribute to regulation of specific Cdc42 signaling pathways in yeast cells. These data support a model in which the epsins function as spatial and temporal coordinators of endocytosis and cell polarity. </jats:p>

収録刊行物

被引用文献 (1)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ