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The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15
Author(s) -
Sengar Ameet S.,
Wang Wei,
Bishay Joseph,
Cohen Samuel,
Egan Sean E.
Publication year - 1999
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/18.5.1159
Subject(s) - dynamin , endocytic cycle , biology , endocytosis , signal transducing adaptor protein , sh3 domain , microbiology and biotechnology , clathrin , amphiphysin , scaffold protein , biochemistry , signal transduction , receptor , proto oncogene tyrosine protein kinase src
Clathrin‐mediated endocytosis is a multistep process which requires interaction between a number of conserved proteins. We have cloned two mammalian genes which code for a number of endocytic adaptor proteins. Two of these proteins, termed Ese1 and Ese2, contain two N‐terminal EH domains, a central coiled‐coil domain and five C‐terminal SH3 domains. Ese1 is constitutively associated with Eps15 proteins to form a complex with at least 14 protein–protein interaction surfaces. Yeast two‐hybrid assays have revealed that Ese1 EH and SH3 domains bind epsin family proteins and dynamin, respectively. Overexpression of Ese1 is sufficient to block clathrin‐mediated endocytosis in cultured cells, presumably through disruption of higher order protein complexes, which are assembled on the endogenous Ese1–Eps15 scaffold. The Ese1–Eps15 scaffold therefore links dynamin, epsin and other endocytic pathway components.