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Vol. 15, Issue 10, 4710-4724, October 2004

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Golgi Enzymes Are Enriched in Perforated Zones of Golgi Cisternae but Are Depleted in COPI Vesicles

Hee-Seok Kweon ^* , Galina V. Beznoussenko ^* , Massimo Micaroni ^*, Roman S. Polishchuk ^*, Alvar Trucco ^*, Oliviano Martella ^*, Daniele Di Giandomenico ^*, Pierfrancesco Marra ^*, Aurora Fusella ^*, Alessio Di Pentima ^*, Eric G. Berger ^* , Willie J. C. Geerts ^* , Abraham J. Koster ^* , Koert N. J. Burger ^* , Alberto Luini ^* ||, and Alexander A. Mironov ^* || ¶

^* Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro (Chieti), Italy; Institute of Physiology, University of Zurich, CH-8057 Zurich, Switzerland; and Department of Molecular Cell Biology, Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, The Netherlands

Submitted December 11, 2003; Accepted June 29, 2004
Monitoring Editor: Keith Mostov

In the most widely accepted version of the cisternal maturation/progression model of intra-Golgi transport, the polarity of the Golgi complex is maintained by retrograde transport of Golgi enzymes in COPI-coated vesicles. By analyzing enzyme localization in relation to the three-dimensional ultrastructure of the Golgi complex, we now observe that Golgi enzymes are depleted in COPI-coated buds and 50- to 60-nm COPI-dependent vesicles in a variety of different cell types. Instead, we find that Golgi enzymes are concentrated in the perforated zones of cisternal rims both in vivo and in a cell-free system. This lateral segregation of Golgi enzymes is detectable in some stacks during steady-state transport, but it was significantly prominent after blocking endoplasmic reticulum-to-Golgi transport. Delivery of transport carriers to the Golgi after the release of a transport block leads to a diminution in Golgi enzyme concentrations in perforated zones of cisternae. The exclusion of Golgi enzymes from COPI vesicles and their transport-dependent accumulation in perforated zones argues against the current vesicle-mediated version of the cisternal maturation/progression model.

Abbreviations used: 3D, three-dimensional; Ab, antibody; COP, coat protein; FP, fluorescent protein; GalT, galactosyltransferase; LD, labeling density; Man, mannosidase; PC, procollagen I; STF, sialyl-transferase; VSVG, temperature-sensitive variant of the G protein of vesicular stomatitis virus.

These authors contributed equally to this work.

^|| Principal investigators.

^¶ Corresponding author. E-mail address: mironov{at}negrisud.it.

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