Abstract Rab proteins form the largest branch of the Ras superfamily of GTPases. They are localized to the cytoplasmic face of organelles and vesicles involved in the biosynthetic/secretory and endocytic pathways in eukaryotic cells. It is now well established that Rab proteins play an essential role in the processes that underlie the targeting and fusion of transport vesicles with their appropriate acceptor membranes. However, the recent discovery of several putative Rab effectors, which are not related to each other and which fulfil diverse functions, suggests a more complex role for Rab proteins. At least two Rab proteins act at the level of the Golgi apparatus. Rab1 and its yeast counterpart Ypt1 control transport events through early Golgi compartments. Work from our laboratory points out a role for Rab6 in intra-Golgi transport, likely in a retrograde direction.