Small cargo proteins and large aggregates can traverse the Golgi by a common mechanism without leaving the lumen of cisternae
| Autor: | Alvar Trucco, Abraham J. Koster, Alexander A. Mironov, Alberto Luini, Galina V. Beznoussenko, Koert N.J. Burger, Pietro Lupetti, Daniele Di Giandomenico, Eric G. Berger, Willie J. C. Geerts, Paolo Nicoziani, Oliviano Martella, Hee Seok Kweon, Aurora Fusella, Roman S. Polishchuk |
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| Rok vydání: | 2001 |
| Předmět: |
Green Fluorescent Proteins
Golgi Apparatus Article Antibodies Cell Line Cryofixation symbols.namesake Viral Envelope Proteins Skin Physiological Phenomena Freezing Image Processing Computer-Assisted Animals Humans Microscopy Immunoelectron Skin Membrane Glycoproteins biology Vesicle Cell Biology Fibroblasts Golgi apparatus Cisterna biology.organism_classification Recombinant Proteins Transport protein Cell biology Luminescent Proteins Microscopy Electron Protein Transport intracellular traffic Golgi complex transport vesicles procollagen VSVG Vesicular stomatitis virus symbols Golgi cisterna Rabbits Lumen (unit) |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| DOI: | 10.1083/jcb.200108073 |
| Popis: | Procollagen (PC)-I aggregates transit through the Golgi complex without leaving the lumen of Golgi cisternae. Based on this evidence, we have proposed that PC-I is transported across the Golgi stacks by the cisternal maturation process. However, most secretory cargoes are small, freely diffusing proteins, thus raising the issue whether they move by a transport mechanism different than that used by PC-I. To address this question we have developed procedures to compare the transport of a small protein, the G protein of the vesicular stomatitis virus (VSVG), with that of the much larger PC-I aggregates in the same cell. Transport was followed using a combination of video and EM, providing high resolution in time and space. Our results reveal that PC-I aggregates and VSVG move synchronously through the Golgi at indistinguishable rapid rates. Additionally, not only PC-I aggregates (as confirmed by ultrarapid cryofixation), but also VSVG, can traverse the stack without leaving the cisternal lumen and without entering Golgi vesicles in functionally relevant amounts. Our findings indicate that a common mechanism independent of anterograde dissociative carriers is responsible for the traffic of small and large secretory cargo across the Golgi stack. |
| Databáze: | OpenAIRE |
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