Abstract
MAMMALIAN cells express many ras-like low molecular mass GTP-binding proteins (rab proteins)1–6 that are highly homologous to the Yptl and Sec4 proteins involved in controlling secretion in yeast7-9. Owing to their structural similarity and to their variety, rab proteins have been postulated to act as specific regulators of membrance traffic in exocytosis and endocytosis10, and rab5 has been shown to be involved in early endosome fusion in vitro11. In agreement with their postulated functions, all rab proteins studied so far have been found in distinct subcompartments along the exocytic or endocytic pathways5,11–13. To define the region mediating their specific localization, we transiently expressed rab2, rab5 and rab7 hybrid proteins in BHK cells, and determined their intracellular localization by immunofluorescence confocal microscopy and subcellular fractionation. Here we present evidence that the highly variable C-terminal domain contains structural elements necessary for the association of rab proteins with their specific target membranes in the endocytic pathway.
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Chavrier, P., Gorvel, JP., Stelzer, E. et al. Hypervariable C-termmal domain of rab proteins acts as a targeting signal. Nature 353, 769–772 (1991). https://doi.org/10.1038/353769a0
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DOI: https://doi.org/10.1038/353769a0
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