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, Alexander A. Mironov

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)4710-4724
Number of pages15
JournalMolecular Biology of the Cell
Volume15
Issue number10
DOIs
Publication statusPublished - Oct 2004

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

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