SMALL GTP-BINDING PROTEIN ASSOCIATED WITH GOLGI CISTERNAE

EUKARYOTIC cells seem to use GTP hydrolysis to regulate vesicular traffic in exocytosis and endocytosis. The best evidence for this comes from studies on the yeast Saccharomyces cerevisiae that have identified two small Ras-related GTP-binding proteins, Sec4p and Yptlp, which control distinct stages of the secretory pathway1-6. In mammalian cells the effects of a non-hydrolysable GTP analogue, GTP-γS, on different transport events have suggested that they also have proteins functionally related to yeast Sec4p and Yptlp7-10. The rab genes have recently been cloned and sequenced for rat and human and their proteins have highly conserved domains in common with Sec4p and Yptlp (including a putative effector binding site). They are therefore good candidates for GTP-binding proteins involved in intracellular transport in mammalian cells11,12. One of the Rab proteins (Rab1p) is the mammalian counterpart of Ypt1p (ref. 13). Here we report the localization of the protein Rab6p to the Golgi apparatus in several cell types. By immunolabelling and electron microscopy, Rab6p appears to be concentrated predominantly on the medial and trans cisternae and distributed over their entire surface. © 1990 Nature Publishing Group.