Mapping of the molecular determinants involved in the interaction between eps15 and AP-2

Gioacchin Iannolo, Anna Elisabetta Salcini, Ibragim Gaidarov, Oscar B. Goodman, Josep Baulida, Graham Carpenter, Pier Giuseppe Pelicci, Pier Paolo Di Fiore, James H. Keen

Research output: Contribution to journalArticlepeer-review


eps15, a substrate for the epidermal growth factor receptor and other receptor tyrosine kinases, possesses a discrete domain structure with protein-binding properties. It interacts with a number of cellular proteins through an evolutionarily conserved protein-binding domain, the eps15 homology domain, located in it NH2-terminal region. In addition, a proline- rich region, located in the COOH-terminal portion of eps15, can bind to the Src homology 3 domain of the crk proto-oncogene product in vitro. Recently, coimmunoprecipitation between eps15 and AP-2, a major component of coated pits, was reported. Here, we characterize the molecular determinants of the eps15/AP-2 interaction. The AP-2 binding region of eps15 is localized in its COOH-terminal region and spans ~80 amino acids. At least three molecular determinants, located at residues 650-660, 680-690, and 720-730, are involved in the binding. AP-2 binds to eps15 through its α subunit (α- adaptin); in particular, the COOH-terminal region of α-adaptin, the so- called α-ear, contains the eps15 binding region.

Original languageEnglish
Pages (from-to)240-245
Number of pages6
JournalCancer Research
Issue number2
Publication statusPublished - 1997

ASJC Scopus subject areas

  • Cancer Research
  • Oncology


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