Abstract
Publisher Summary Genetic analysis of the budding yeast Saccharomyces cerevisiae has provided major insight into the role Ras-related GTPases play in the vesicular transport pathways of eukaryotic cells. Like other members of the Ras superfamily, Rab proteins cycle between the GDP-bound form and the GTP-bound form. This cycle is mediated by GTP hydrolysis and the exchange of GDP for GTP, which allows them to act as molecular switches that regulate a variety of functions in eukaryotic cells. The subcellular localization of these proteins is also critical for their function, reflected by the fact that each member of the Rab family is localized to a distinct stage of the endocytic or exocytic pathway. The current model of Rab function is that the cycle of guanine nucleotide binding and hydrolysis is coupled to a cycle of subcellular localization. One of the first pieces of evidence in support of this model was the identification of the regulatory factor Rab-GDI (Rab-GDP dissociation inhibitor), which was isolated from bovine brain by its ability to slow the dissociation of GDP from Rab3A.
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