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¹ Department of Cell Biology, School of Medicine, University of Murcia, 30071 Murcia, Spain
² Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA
³ Department of Cell Biology, University Medical Center Utrecht, Institute of Biomembranes and Centre for Biomedical Genetics, 3584 CX Utrecht, Netherlands

Address correspondence to Judith Klumperman, Dept. of Cell Biology, University Medical Center Utrecht, Heidelberglaan 100, AZU Rm. G02.525, 3584 CX Utrecht, Netherlands. Tel.: 31-30-2506550. Fax: 31-30-2541797. E-mail: j.klumperman{at}lab.azu.nl

A cisternal progression mode of intra-Golgi transport requires that Golgi resident proteins recycle by peri-Golgi vesicles, whereas the alternative model of vesicular transport predicts anterograde cargo proteins to be present in such vesicles. We have used quantitative immuno-EM on NRK cells to distinguish peri-Golgi vesicles from other vesicles in the Golgi region. We found significant levels of the Golgi resident enzyme mannosidase II and the transport machinery proteins giantin, KDEL-receptor, and rBet1 in coatomer protein I–coated cisternal rims and peri-Golgi vesicles. By contrast, when cells expressed vesicular stomatitis virus protein G this anterograde marker was largely absent from the peri-Golgi vesicles. These data suggest a role of peri-Golgi vesicles in recycling of Golgi residents, rather than an important role in anterograde transport.

Key Words: mannosidase II; COP coats; giantin; KDELr; Golgi complex

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