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. 1999 Mar 1;18(5):1159–1171. doi: 10.1093/emboj/18.5.1159

The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15.

A S Sengar 1, W Wang 1, J Bishay 1, S Cohen 1, S E Egan 1
PMCID: PMC1171207  PMID: 10064583

Abstract

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.

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Selected References

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