Epsin 1 is involved in recruitment of ubiquitinated EGF receptors into clathrin-coated pits.

@article{Kazazic2009Epsin1I,
  title={Epsin 1 is involved in recruitment of ubiquitinated EGF receptors into clathrin-coated pits.},
  author={Maja Kazazic and Vibeke Bertelsen and Ketil Winther Pedersen and Tram Thu Vuong and Michael Vibo Grandal and Marianne Skeie R{\o}dland and Linton M Traub and Elden J. Stang and Inger Helene Madshus},
  journal={Traffic},
  year={2009},
  volume={10 2},
  pages={
          235-45
        }
}
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… CONTINUE READING
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Embryonic arrest at midgestation and disruption of Notch signaling produced by the absence of both epsin 1 and epsin 2 in mice.

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