A protein-binding domain, EH, identified in the receptor tyrosine kinase substrate Eps15 and conserved in evolution

W. T. Wong, C. Schumacher, A. E. Salcini, A. Romano, P. Castagnino, P. Giuseppe, P. P. Di Fiore

Research output: Contribution to journalArticlepeer-review

Abstract

In this report we structurally and functionally define a binding domain that is involved in protein association and that we have designated EH (for Eps15 homology domain). This domain was identified in the tyrosine kinase substrate Eps15 on the basis of regional conservation with severed heterogeneous proteins of yeast and nematode. The EH domain spans about 70 amino acids and shows ≃60% overall amino acid conservation. We demonstrated the ability of the EH domain to specifically bind cytosolic proteins in normal and malignant cells of mesenchymal, epithelial, and hematopoietic origin. These observations prompted our search for additional EH-containing proteins in mammalian cells. Using an EH domain-specific probe derived from the eps15 cDNA, we cloned and characterized a cDNA encoding an EH-containing protein with overall similarity to Eps15; we designated this protein Eps15r (for Eps15-related). Structural comparison of Eps15 and Eps15r defines a family of signal transducers possessing extensive networking abilities including EH-mediated binding and association with Src homology 3-containing proteins.

Original languageEnglish
Pages (from-to)9530-9534
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number21
DOIs
Publication statusPublished - 1995

ASJC Scopus subject areas

  • General
  • Genetics

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