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Cover  The Golgi complex functions as a central way station for proteins synthesized at the endoplasmic reticulum, processing these proteins and sorting them for transport to their final destinations in the lysosome, plasma membrane, or extracellular medium. One of the major aspects of protein processing done by the Golgi complex is the modification of N-linked oligosaccharides. The Golgi complex first trims the high-mannose oligosaccharide chains added to proteins in the endoplasmic reticulum, then adds specific sugars, including fucose, to the trimmed chains. One of the first reports of the posttranslational modification of N-linked oligosaccharides by the Golgi complex was contributed by Gary Bennett and Charles Philippe Leblond. The image on the cover shows a striking electron microscopic radioautograph of rat intestinal columnar cells, fixed shortly after intravenous injection of radiolabeled fucose. Tortuous silver grains overlie the Golgi complex, defining the site of fucose addition to proteins passaging through the secretory pathway. Leblond and his colleagues pioneered the use of microscopic radioautography to reveal the dynamic nature not only of cells themselves but of the molecular processes occurring within them. (Reprinted with permission from Bennett, G. and Leblond, C.P. [1970]. Formation of cell coat material for the whole surface of columnar cells in the rat small intestine, as visualized by radioautography with L-fucose-3H. J. Cell Biol. 46, 409-416).Richard Rachubinski