Regulation of clathrin coat assembly by Eps15 homology domain-mediated interactions during endocytosis

Ryohei Suzuki, Junko Y. Toshima, Jiro Toshima

    Research output: Contribution to journalArticle

    8 Citations (Scopus)

    Abstract

    Clathrin-mediated endocytosis involves a coordinated series of molecular events regulated by interactions among a variety of proteins and lipids through specific domains. One such domain is the Eps15 homology (EH) domain, a highly conserved protein-protein interaction domain present in a number of proteins distributed from yeast to mammals. Several lines of evidence suggest that the yeast EH domain-containing proteins Pan1p, End3p, and Ede1p play important roles during endocytosis. Although genetic and cell-biological studies of these proteins suggested a role for the EH domains in clathrin-mediated endocytosis, it was unclear how they regulate clathrin coat assembly. To explore the role of the EH domain in yeast endocytosis, we mutated those of Pan1p, End3p, or Ede1p, respectively, and examined the effects of single, double, or triple mutation on clathrin coat assembly. We found that mutations of the EH domain caused a defect of cargo internalization and a delay of clathrin coat assembly but had no effect on assembly of the actin patch. We also demonstrated functional redundancy among the EH domains of Pan1p, End3p, and Ede1p for endocytosis. Of interest, the dynamics of several endocytic proteins were differentially affected by various EH domain mutations, suggesting functional diversity of each EH domain.

    Original languageEnglish
    Pages (from-to)687-700
    Number of pages14
    JournalMolecular Biology of the Cell
    Volume23
    Issue number4
    DOIs
    Publication statusPublished - 2012 Feb 15

    ASJC Scopus subject areas

    • Molecular Biology
    • Cell Biology

    Fingerprint Dive into the research topics of 'Regulation of clathrin coat assembly by Eps15 homology domain-mediated interactions during endocytosis'. Together they form a unique fingerprint.

  • Cite this