Interest in the RAB proteins stems from early work on yeast that identified essential roles for the RABs Ypt1p (Rab1) and Sec4p in pre- and post-Golgi membrane trafficking (Salminen and Novick 1987; Segev et al. 1988). These findings prompted efforts to clone other members of the RAB gene family and it was quickly established that this family had undergone significant expansion in mammals. As each new RAB was discovered, it also became clear that different RAB proteins could adopt specific subcellular localizations, associating with particular membrane compartments and regulating the functions of these organelles. RAB18 was partially cloned in 1992, and then fully cloned in 1993 (Chavrier et al. 1992; Yu et al. 1993). Initial characterization showed that it was widely expressed in different tissues and localized to endosomes in polarized epithelia (Lutcke et...
- Vázquez-Martínez R, Malagón MM. Rab proteins and the secretory pathway: the case of Rab18 in neuroendocrine cells. Front Endocrinol 2011;2:1–9. doi:10.3389/fendo.2011.00001Google Scholar