TY - JOUR
T1 - Mapping of the molecular determinants involved in the interaction between eps15 and AP-2.
AU - Iannolo, G
AU - Salcini, A E
AU - Gaidarov, I
AU - Goodman, O B
AU - Baulida, J
AU - Carpenter, G
AU - Pelicci, P G
AU - Di Fiore, P P
AU - Keen, J H
N1 - Keywords: 3T3 Cells; Adaptor Protein Complex alpha Subunits; Adaptor Proteins, Vesicular Transport; Animals; Base Sequence; Binding Sites; Calcium-Binding Proteins; Membrane Proteins; Mice; Molecular Sequence Data; Peptide Fragments; Peptide Mapping; Phosphoproteins; Recombinant Proteins
PY - 1997
Y1 - 1997
N2 - 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 its 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 approximately 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 alpha subunit (alpha-adaptin); in particular, the COOH-terminal region of alpha-adaptin, the so-called alpha-ear, contains the eps15 binding region.
AB - 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 its 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 approximately 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 alpha subunit (alpha-adaptin); in particular, the COOH-terminal region of alpha-adaptin, the so-called alpha-ear, contains the eps15 binding region.
M3 - Journal article
C2 - 9000562
SN - 0008-5472
VL - 57
SP - 240
EP - 245
JO - Cancer Research
JF - Cancer Research
IS - 2
ER -