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Rab5 is a low molecular weight GTP-binding protein that plays a role in endocytic vesicle traffic. Like other Rab proteins, Rab5 has C-terminal cysteine residues that are post-translationally modified by geranylgeranylation, which is critical for its membrane targeting. Rab5 is associated with early endosome and plasma membranes and evidence suggests that Rab5 is involved in regulation of early endosome fusion. The GTP/GDP cycle controls shuttling of Rab proteins between the cytosol and organelle membranes. In vitro, Rab5 proteins are removed from membranes by a GDP dissociation inhibitor protein (rabGDI) which leads to the formation of a cytosolic Rab5-rabGDI complex. Rab5 insertion into membranes is a multistep process in which a transient GDP-Rab5 intermediate is formed and converted into GTP-Rab5 that subsequently enters the acceptor membrane and releases rabGDI into the cytosol.
