The Eps15 homology (EH) domain

FEBS Letters

Confalonieri, Stefano¹  Di Fiore, Pier Paolo¹ 

[1] IFOM, The FIRC Institute for Molecular Oncology, Via Serio 21, 20139 Milan, Italy

关键词: EH;    Eps15;    Endocytosis;    Actin remodeling;    Signaling;   

DOI  :  10.1016/S0014-5793(01)03241-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The Eps15 homology (EH) domain was originally identified as a motif present in three copies at the NH₂-termini 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 ‘Eps15 homology’ or EH domain [Wong et al. (1994) Oncogene 9, 1591–1597; Wong et al. (1995) Proc. Natl. Acad. Sci. USA 92, 9530–9534; Fazioli et al. (1993) Mol. Cell. Biol. 13, 5814–5828] was derived. The motif was subsequently found in several proteins from yeast to nematode, thus establishing its evolutionary conservation. Initial studies with filter-binding assays and phage-displayed 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-containing and EH-binding proteins have been identified, which establish in the cell a network of protein:protein interactions, defined as the EH network. This network coordinates cellular functions connected with endocytosis, actin remodeling and intracellular transduction of signals.

【 授权许可】

Unknown