Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 23, Issue 4, Pages 687-700Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E11-04-0380
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Funding
- Japan Society for the Promotion of Science
- Novartis Foundation (Japan)
- Mitsubishi Foundation
- Naito Foundation
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Futaba Electronics Memorial Foundation
- Astellas Foundation for Research on Metabolic Disorders
- Hamaguchi Foundation for the Advancement of Biochemistry
- Takeda Science Foundation
- Kurata Memorial Hitachi Science and Technology Foundation
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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.
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