The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15 - PubMed (original) (raw)

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

A S Sengar et al. EMBO J. 1999.

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.

PubMed Disclaimer

Similar articles

Cited by

References

    1. J Cell Biol. 1998 Mar 9;140(5):1055-62 - PubMed
    1. Science. 1996 Mar 15;271(5255):1533-9 - PubMed
    1. Nat Biotechnol. 1996 Jun;14(6):741-4 - PubMed
    1. Mol Cell Biol. 1993 Sep;13(9):5814-28 - PubMed
    1. J Biol Chem. 1995 Jun 23;270(25):15341-7 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources