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Genes and Development
Vol. 11, No. 17,
pp. 2239-2249,
September 1, 1997
1 Department of Experimental Oncology, European Institute
of Oncology, Milan 20140, Italy;
2 Dipartimento di Biologia,
University of Rome "Tor Vergata," Rome 00100, Italy;
3 Istituto di Patologia Speciale Medica, University of Parma,
Parma 43100, Italy;
4 Instituto di Microbiologia, University
of Bari, Bari 70100, Italy
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.
[Key Words: EH domain; protein interaction; Eps15; internalization; trafficking]
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A Benmerah, M Bayrou, N Cerf-Bensussan, and A Dautry-Varsat Inhibit |
