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MBC in Press, published online ahead of print June 27, 2005
Mol. Biol. Cell 10.1091/mbc.E04-10-0938

A more recent version of this article appeared on September 1, 2005 Originally published as MBC in Press, 10.1091/mbc.E04-10-0938 on June 24, 2005 Originally published as MBC in Press, 10.1091/mbc.E04-10-0938 on June 22, 2005
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Submitted on October 28, 2004
Revised on June 7, 2005
Accepted on June 15, 2005

dGRASP Localization and Function in the Early Exocytic Pathway in Drosophila S2 Cells

Vangelis Kondylis, Kirsten M. Spoorendonk, and Catherine Rabouille

The Cell Microscopy Centre, Department of Cell Biology and Institute of Biomembranes, University Medical Centre Utrecht, AZU, 3584CX Utrecht, The Netherlands

Monitoring Editor: Benjamin Glick

The de novo model for Golgi stack biogenesis predicts that membrane exiting the ER at tER sites contains and recruits all the necessary molecules to form a Golgi stack, including the Golgi matrix proteins, p115, GM130 and GRASP65/55. These proteins leave the tER sites faster than Golgi transmembrane resident enzymes suggesting that they act as a template nucleating the formation of the Golgi apparatus. However, the localisation of the Golgi Matrix proteins at tER sites is only shown under conditions where exit from the ER is blocked. Here, we show in Drosophila S2 cells, that dGRASP, the single Drosophila homologue of GRASP65/55, localises both to the Golgi membranes and the tER sites at steady state, and that the myristoylation of glycine 2 is essential for the localisation to both compartments. Its depletion for 96h by RNAi gave an effect on the architecture of the Golgi stacks in 30% of the cells, but a double depletion of dGRASP and dGM130 led to the quantitative conversion of Golgi stacks into clusters of vesicles and tubules, often featuring single cisternae. This disruption of Golgi architecture was not accompanied by the disorganisation of tER sites or the inhibition of anterograde transport.This shows that at least in Drosophila, the structural integrity of the Golgi stacks is not required for efficient transport. Overall, dGRASP exhibits a dynamic association to the membrane of the early exocytic pathway and is involved in Golgi stack architecture.

Address correspondence to: Catherine Rabouille (C.Rabouille{at}lab.azu.nl)




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