{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,10]],"date-time":"2026-01-10T18:25:17Z","timestamp":1768069517118,"version":"3.49.0"},"reference-count":53,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2001,12,7]],"date-time":"2001-12-07T00:00:00Z","timestamp":1007683200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[2002,2,20]]},"abstract":"<jats:p>The Eps15 homology (EH) domain was originally identified as a motif present in three copies at the NH<jats:sub>2<\/jats:sub>\u2010termini of Eps15 and of the related molecule Eps15R. Both of these molecules are substrates for the tyrosine kinase activity of the epidermal growth factor receptor and hence the name \u2018Eps15 homology\u2019 or EH domain [Wong et al. (1994) Oncogene 9, 1591\u20131597; Wong et al. (1995) Proc. Natl. Acad. Sci. USA 92, 9530\u20139534; Fazioli et al. (1993) Mol. Cell. Biol. 13, 5814\u20135828] was derived. The motif was subsequently found in several proteins from yeast to nematode, thus establishing its evolutionary conservation. Initial studies with filter\u2010binding assays and phage\u2010displayed libraries demonstrated its protein:protein interaction abilities and identified specific ligands. Subsequently, structural analyses established the molecular bases of recognition between EH domains and cognate peptides. To date, several EH\u2010containing and EH\u2010binding proteins have been identified, which establish in the cell a network of protein:protein interactions, defined as the EH network. 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