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Science  15 Aug 2003:
Vol. 301, Issue 5635, pp. 897
DOI: 10.1126/science.301.5635.897c

Inside eukaryotic cells, a panoply of membrane-bound organelles exchange material in a process termed membrane traffic. Two organelles, the endoplasmic reticulum (ER) and the Golgi complex, are key stages in the secretory pathway whereby newly synthesized proteins traverse the ER membrane and are packaged into transport vesicles within the transitional ER (tER) for onward transport to the cell surface via the Golgi. The Golgi complex is composed of a set of tightly apposed cisternae, and there has been a lot of debate about how the architecture of the Golgi is established and maintained in the face of ongoing intracellular membrane traffic.

Using RNA interference, Kondylis and Rabouille looked at the contribution of the protein dp115 in the organization of the Golgi complex and the tER in cultured Drosophila S2 cells. In dp115-depleted cells the Golgi stacks were unable to assemble and appeared instead as clusters of vesicles and tubules; the tER regions also lost their normal focused organization and appeared to be dispersed throughout the cytoplasm. Even so, the secretion of membrane and secretory proteins remained efficient. Thus, dp115 is important in the generation and maintenance of Golgi and tER architecture, but this architecture is not intrinsically required for the secretory pathway to function. — SMH

J. Cell Biol. 162, 185 (2003).

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