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Vol. 273, Issue 2, 814-821, January 9, 1998
From the Department of Biochemistry, Hiroshima University School of
Medicine, 1-2-3 Kasumi, Minami-ku, Hiroshima 734, Japan
Ral-binding protein 1 (RalBP1) is a putative
effector protein of Ral and exhibits a GTPase activating activity for
Rac and CDC42. To clarify the function of RalBP1, we isolated a novel protein that interacts with RalBP1 by yeast two-hybrid screening and
designated it POB1 (partner of
RalBP1). POB1 consists of 521 amino acids,
shares a homology with Eps15, which has been identified as an epidermal
growth factor (EGF) receptor substrate, and has two proline-rich
motifs. The POB1 mRNA was expressed in cerebrum, cerebellum, lung,
kidney, and testis. POB1 interacted with RalBP1 in COS cells and the
C-terminal region of POB1 was responsible for this interaction. The
binding domain of RalBP1 to POB1 was distinct from its binding domain
to Ral. Ral and POB1 simultaneously interacted with RalBP1 in COS
cells. The binding of POB1 to RalBP1 did not affect the GTPase
activating activity of RalBP1. Furthermore, POB1 bound to Grb2 but not
to Nck or Crk. POB1 was tyrosine-phosphorylated in COS cells upon
stimulation with EGF and made a complex with EGF receptor. These
results suggest that RalBP1 makes a complex with POB1 and that this
complex may provide a link between tyrosine kinase, Src homology 3 (SH3)-containing protein, and Ral.
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