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. 2006 Jun 19;173(6):917–926. doi: 10.1083/jcb.200510010

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Copyright © 2006, The Rockefeller University Press

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Figure 3. — The Rab9 hypervariable domain is necessary and sufficient for Rab9 effector binding. (A) Binding of purified, untagged Rab9, Rab1A, Rab9/1, and Rab1/9 to the Rab9 effectors His₆-TIP47(152–434; closed bars) and His₆-p40 (open bars). Data are normalized relative to the binding seen for parental Rabs. (B) Same as in A, with untagged Rab9, Rab5a, Rab9/5, and Rab5/9. (C) Binding of [³⁵S]GTPγS- and [³H]GDP-loaded Rab9, Rab5/9, and Rab1/9 to His₆-TIP47(152–434). 100% binding to p40 or TIP47 represented 3.9 or 1.5 pmol Rab9, respectively, in A and B. This assay measures active Rab molecules only; untagged Rab proteins were all ∼100% active, except for Rab9/5, which contained ∼30% active molecules. Error bars represent the SEM.