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J Biol Chem, Vol. 274, Issue 45, 31941-31946, November 5, 1999
From the Burnham Institute, La Jolla, California 92037
The Eph family of receptor tyrosine kinases has
been implicated in many developmental patterning processes, including
cell segregation, cell migration, and axon guidance. The cellular
components involved in the signaling pathways of the Eph receptors,
however, are incompletely characterized. Using a yeast two-hybrid
screen, we have identified a novel signaling intermediate, SHEP1
(SH2 domain-containing Eph receptor-binding
protein 1), which is expressed in the embryonic
and adult brain. SHEP1 contains an Src homology 2 domain that binds to
a conserved tyrosine-phosphorylated motif in the juxtamembrane region
of the EphB2 receptor and may itself be a target of EphB2 kinase
activity, since it becomes heavily tyrosine-phosphorylated in cells
expressing activated EphB2. SHEP1 also contains a domain similar to Ras
guanine nucleotide exchange factor domains and binds to the GTPases
R-Ras and Rap1A, but not Ha-Ras or RalA. Thus, SHEP1 directly links
activated, tyrosine-phosphorylated Eph receptors to small Ras
superfamily GTPases.
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