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. 2009 Sep 21;186(6):897–914. doi: 10.1083/jcb.200902096

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© 2009 Sumakovic et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 1. — UNC-108 is a homologue of human Rab2. (A) Sequence alignment of Rab2 from C. elegans, Homo sapiens, and Drosophila. Domains responsible for phosphate and Mg²⁺ binding (orange boxes) and guanine moiety binding (yellow boxes) are shown. Arrowheads indicate point mutations within RAB-2. Mutations rendering RAB-2 constitutively inactive (S20N) and constitutively active (Q65L) are shown (Tisdale, 1999). (B) Western blot of protein extracts from different unc-108 alleles probed with polyclonal RAB-2 antibodies. Tubulin loading control is also shown. (C) Quantification of normalized RAB-2 protein levels. Error bars = SEM (*, P < 0.05; Student's t test; n = 4).