Premium
Epsin 1 is Involved in Recruitment of Ubiquitinated EGF Receptors into Clathrin‐Coated Pits
Author(s) -
Kazazic Maja,
Bertelsen Vibeke,
Pedersen Ketil Winther,
Vuong Tram Thu,
Grandal Michael Vibo,
Rødland Marianne Skeie,
Traub Linton M.,
Stang Espen,
Madshus Inger Helene
Publication year - 2009
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2008.00858.x
Subject(s) - endocytosis , ubiquitin , internalization , clathrin , biology , microbiology and biotechnology , gene knockdown , signal transducing adaptor protein , immunoprecipitation , receptor , signal transduction , biochemistry , gene
Epsin consists of an epsin NH 2 ‐terminal homology domain that promotes interaction with phospholipids, several AP‐2‐binding sites, two clathrin‐binding sequences and several Eps15 homology domain‐binding motifs. Epsin additionally possesses ubiquitin‐interacting motifs (UIMs) and has been demonstrated to bind ubiquitinated cargo. We therefore investigated whether epsin promoted clathrin‐mediated endocytosis of the ubiquitinated EGF receptor (EGFR). By immunoprecipitation, we found that epsin 1 interacted with ubiquitinated EGFR and that functional UIMs were essential for complex formation. Furthermore, RNA interference‐mediated knockdown of epsin 1 was found to inhibit internalization of the EGFR, while having no effect on endocytosis of the transferrin receptor. Additionally, upon knockdown of epsin 1, translocation of the EGFR to central parts of clathrin‐coated pits was inhibited. This supports the contention that epsin 1 promotes endocytosis of the ubiquitinated EGFR.