Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. Academic Article uri icon

Overview

abstract

  • The mammalian protein epsin is required for endocytosis. In this study, we have characterized two homologous yeast proteins, Ent1p and Ent2p, which are similar to mammalian epsin. An essential function for the highly conserved N-terminal epsin N-terminal homology (ENTH) domain was revealed using deletions and randomly generated temperature-sensitive ent1 alleles. Changes in conserved ENTH domain residues in ent1(ts) cells revealed defects in endocytosis and actin cytoskeleton structure. The Ent1 protein was localized to peripheral and internal punctate structures, and biochemical fractionation studies found the protein associated with a large, Triton X-100-insoluble pellet. Finally, an Ent1p clathrin-binding domain was mapped to the final eight amino acids (RGYTLIDL*) in the Ent1 protein sequence. Based on these and other data, we propose that the yeast epsin-like proteins are essential components of an endocytic complex that may act at multiple stages in the endocytic pathway.

publication date

  • August 16, 1999

Research

keywords

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • Clathrin
  • Endocytosis
  • Fungal Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins

Identity

PubMed Central ID

  • PMC1171513

Scopus Document Identifier

  • 0033575748

Digital Object Identifier (DOI)

  • 10.1093/emboj/18.16.4383

PubMed ID

  • 10449404

Additional Document Info

volume

  • 18

issue

  • 16