作者: Haipeng Shao , Douglas A. Andres
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摘要: Abstract The small GTPase Rit is a close relative of Ras, and constitutively active can induce oncogenic transformation. Although the effector loops Ras are highly related, fails to interact with majority known candidate proteins, suggesting that novel cellular targets may be responsible for transforming activity. To gain insight into function Rit, we searched Rit-binding proteins by yeast two-hybrid screening. We identified C-terminal Rit/Ras interaction domain protein have designated RGL3 (RalGEF-like 3) shares 35% sequence identity Ral guanine nucleotide exchange factors (RalGEFs). RGL3, through 99-amino acid domain, interacted in GTP- loop-dependent manner Ras. Importantly, exhibited activity toward was stimulated vivo expression either activated or These data suggest functions as an factor serve downstream both