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First published online February 4, 2009
doi: 10.1242/10.1242/jcs.032581

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Mechanisms of transport through the Golgi complex

Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette, France

e-mail: jackson{at}lebs.cnrs-gif.fr

The Golgi complex is the central sorting and processing station of the secretory pathway, ensuring that cargo proteins, which are synthesized in the endoplasmic reticulum, are properly glycosylated and packaged into carriers for transport to their final destinations. Two recent studies highlight the fact that properties of membrane lipids play key roles in Golgi structural organization and trafficking. The Antonny laboratory has demonstrated the mechanism by which a Golgi tether containing a membrane-curvature-sensing domain at one end can link highly curved and flat membranes together in a reversible manner. In this way, a strong interaction that binds membranes together in an oriented fashion can easily be disrupted as the properties of the membranes change. The Lippincott-Schwartz laboratory has developed a new model for intra-Golgi trafficking, called the rapid-partitioning model, which incorporates lipid trafficking as an integral part. Simulations reveal that the sorting of lipids into processing and export domains that are connected to each Golgi cisterna, and bidirectional trafficking throughout the Golgi to allow proteins to associate with their preferred lipid environment, is sufficient to drive protein transport through the secretory pathway. Although only a proof in principle, this model for the first time invokes lipid sorting as the driving force in intra-Golgi trafficking, and provides a framework for future experimental work.

Key words: Golgi, Secretory pathway, Intra-Golgi trafficking, Membrane curvature, ALPS motif, Tether, Golgin, Sphingolipid, Glycerophospholipid, ADP ribosylation factor, G protein, COPI, Coatomer, Glycosylation

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