The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module

Julie A. Rosenthal, Hong Chen, Vladimir I. Slepnev, Lorenzo Pellegrini, Anna Elisabetta Salcini, Pier Paolo Di Fiore, Pietro De Camilli

Research output: Contribution to journalArticlepeer-review

Abstract

Epsin (epsin 1) is an interacting partner for the EH domain-containing region of Eps15 and has been implicated in conjunction with Eps15 in clathrin-mediated endocytosis. We report here the characterization of a similar protein (epsin 2), which we have cloned from human and rat brain libraries. Epsin 1 and 2 are most similar in their NH2-terminal region, which represents a module (epsin NH2 terminal homology domain, ENTH domain) found in a variety of other proteins of the data base. The multiple DPW motifs, typical of the central region of epsin 1, are only partially conserved in epsin 2. Both proteins, however, interact through this central region with the clathrin adaptor AP-2. In addition, we show here that both epsin 1 and 2 interact with clathrin. The three NPF motifs of the COOH- terminal region of epsin 1 are conserved in the corresponding region of epsin 2, consistent with the binding of both proteins to Eps15. Epsin 2, like epsin 1, is enriched in brain, is present in a brain-derived clathrin-coated vesicle fraction, is concentrated in the peri-Golgi region and at the cell periphery of transfected cells, and partially colocalizes with clathrin. High overexpression of green fluorescent protein-epsin 2 mislocalizes components of the clathrin coat and inhibits clathrin-mediated endocytosis. The epsins define a new protein family implicated in membrane dynamics at the cell surface.

Original languageEnglish
Pages (from-to)33959-33965
Number of pages7
JournalJournal of Biological Chemistry
Volume274
Issue number48
DOIs
Publication statusPublished - Nov 26 1999

ASJC Scopus subject areas

  • Biochemistry

Fingerprint

Dive into the research topics of 'The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module'. Together they form a unique fingerprint.

Cite this