The Ear of α-Adaptin Interacts with the COOH-terminal Domain of the Eps15 Protein - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Biological Chemistry Année : 1996

The Ear of α-Adaptin Interacts with the COOH-terminal Domain of the Eps15 Protein

Résumé

The role of Eps15 in clathrin-mediated endocytosis is supported by two observations. First, it interacts specifically and constitutively with the plasma membrane adaptor AP-2. Second, its NH2 terminus shows significant homology to the NH2 terminus of yeast End3p, necessary for endocytosis of alpha-factor. To gain further insight into the role of Eps15-AP-2 association, we have now delineated their sites of interactions. AP-2 binds to a domain of 72 amino acids (767-739) present in the COOH terminus of Eps15. This domain contains 4 of the 15 DPF repeats characteristic of the COOH-terminal domain of Eps15 and shares no homology with known proteins, including the related Epsl5r protein. Precipitation of proteolytic fragments of AP-2 with Eps15-derived fusion proteins containing the binding site for AP-2 showed that Eps15 binds specifically to a 40-kDa fragment corresponding to the ear of alpha-adaptin, a result confirmed by precipitation of Eps15 by alpha-adaptin-derived fusion proteins. Our data indicate that this specific part of AP-2 binds to a cellular component and provide the tools for investigating the functions of the association between AP-2 and Eps15.

Dates et versions

hal-03844282 , version 1 (08-11-2022)

Identifiants

Citer

Alexandre Benmerah, Bernadette Bègue, Alice Dautry-Varsat, Nadine Cerf-Bensussan. The Ear of α-Adaptin Interacts with the COOH-terminal Domain of the Eps15 Protein. Journal of Biological Chemistry, 1996, 271 (20), pp.12111-12116. ⟨10.1074/jbc.271.20.12111⟩. ⟨hal-03844282⟩

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