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Volume 272, Number 50, Issue of December 12, 1997
pp. 31230-31234
(Received for publication, September 17, 1997, and in revised form, October 8, 1997)
From the Department of Biochemistry, Tufts University School of
Medicine, Boston, Massachusetts 02111
Ral proteins constitute a family of small GTPases
that can be activated by Ras in cells. In the GTP-bound state, Ral
proteins bind to RalBP1, a GTPase-activating protein for CDC42 and Rac GTPases. We have used the two-hybrid system in yeast to clone a
cDNA for a novel ~85-kDa protein that can bind to an additional site on RalBP1. This newly identified protein contains an Eps homology
(EH) domain, which was first detected in the epidermal growth factor
(EGF) receptor substrate Eps15. Recently, the EH domain of Eps15 has
been shown to bind to proteins containing an
asparagine-proline-phenylalanine motif. Moreover, EH domains have been
found in proteins involved in endocytosis and/or actin cytoskeleton
regulation. The RalBP1 associated Eps-homology
domain protein, Reps1, is tyrosine-phosphorylated in response to EGF stimulation of cells. In addition, Reps1 has the capacity to form a
complex with the SH3 domains of the adapter proteins Crk and Grb2,
which may link Reps1 to an EGF-responsive tyrosine kinase. Thus, Reps1
may coordinate the cellular actions of activated EGF receptors and
Ral-GTPases.
An Eps Homology (EH) Domain Protein That Binds to the
Ral-GTPase Target, RalBP1
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