Suzuki R, Toshima JY, Toshima J

Clathrin-mediated endocytosis involves a coordinated series of molecular events regulated by interactions between 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 ...

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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 have suggested a role for the EH domains in clathrin-mediated endocytosis, it is still 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 between the EH domains of Pan1p, End3p and Ede1p for endocytosis. Interestingly, the dynamics of several endocytic proteins were differentially affected by various EH domain mutations, suggesting functional diversity of each EH domain.

Date: Dec. 21, 2011

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