The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps 15 protein - PubMed (original) (raw)

. 1996 May 17;271(20):12111-6.

doi: 10.1074/jbc.271.20.12111.

Affiliations

• PMID: 8662627
• DOI: 10.1074/jbc.271.20.12111

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The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps 15 protein

A Benmerah et al. J Biol Chem. 1996.

Free article

Abstract

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.

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