Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module

Anna Elisabetta Salcini, Stefano Confalonieri, Margherita Doria, Elisa Santolini, Elena Tassi, Olga Minenkova, Gianni Cesareni, Pier Giuseppe Pelicci, Pier Paolo Di Fiore

Research output: Contribution to journalArticlepeer-review

Abstract

EH is a recently identified protein-protein interaction domain found in the signal transducers Eps15 and Eps15R and several other proteins of yeast nematode. We show that EH domains from Eps15 and Eps15R bind in vitro to peptides containing an asparagine-proline-phenylalanine (NPF) motif. Direct screening of expression libraries with EH domains yielded a number of putative EH interactors, all of which possessed NPF motifs that were shown to be responsible for the interaction. Among these interactors were the human homolog of NUMB, a developmentally reguated gene of Drosophila, and RAB, the cellular cofactor of the HIV REV protein. We demonstrated coimmunoprecipitation of Eps15 with NUMB and RAB. Finally, in vitro binding of NPF-containing peptides to cellular proteins and EST database screening established the existence of a family of EH-containing proteins in mammals. Based on the characteristics of EH-containing and EH-binding proteins, we propose that EH domains are involved in processes connected with the transport and sorting of molecules within the cell.

Original languageEnglish
Pages (from-to)2239-2249
Number of pages11
JournalGenes and Development
Volume11
Issue number17
Publication statusPublished - Sep 1 1997

Keywords

  • EH domain
  • Eps15
  • Internalization
  • Protein interaction
  • Trafficking

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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