Abstract

The Golgi complex of Saccharomyces cerevisiae is required for protein transport, posttranslational modification, and sorting within the secretory pathway. Only in the last few years has it become clear that these events are functionally organized into distinct Golgi compartments analagous to the cis–trans compartments of the plant and animal Golgi complex. The mechanisms by which the Golgi complex maintains its own organization and complement of intrinsic enzymes against the flow of lipid and protein through the secretory pathway are still poorly understood. However, studies using Saccharomyces cerevisiae as a model system are providing insights into mechanisms of Golgi protein localization that appear to be conserved between yeast and mammalian cells. This review describes the structure and organization of the yeast Golgi complex and recent work towards defining localization signals within intrinsic enzymes of this organelle. Key words: Golgi complex, protein sorting, Saccharomyces cerevisiae, α-1,3-mannosyltransferase.

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