Article
- The EMBO Journal (1999) 18, 1159 - 1171
- doi:10.1093/emboj/18.5.1159
The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15
Ameet S. Sengar1,2,3, Wei Wang1,3, Joseph Bishay1, Samuel Cohen1 and Sean E. Egan1,2
- Programs of Cancer and Blood Research, and Developmental Biology, The Hospital for Sick Children, 555 University Avenue, Toronto, Ontario, M5G 1X8, Canada
- The Department of Molecular and Medical Genetics, The University of Toronto, Toronto, Ontario, Canada
- A.S.Sengar and W.Wang contributed equally to this work
Correspondence to:
Sean E. Egan, E-mail: segan@sickkids.on.ca
Received 30 September 1998; Accepted 31 December 1998; Revised 23 December 1998
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.
Keywords:
- EH domains,
- endocytosis,
- Eps15,
- Ese,
- SH3 domains
