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Originally published as MBC in Press, 10.1091/mbc.E07-08-0799 on September 12, 2007

Vol. 18, Issue 11, 4637-4647, November 2007

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Analysis of De Novo Golgi Complex Formation after Enzyme-based Inactivation

Florence Jollivet*,{dagger}, Graça Raposo*,{dagger}, Ariane Dimitrov*,{dagger}, Rachid Sougrat{ddagger}, Bruno Goud*,{dagger}, and Franck Perez*,{dagger}

*Centre National de la Recherche Scientifique Unité Mixte de Recherche 144, 75248 Paris Cedex 05, France; {dagger}Institut Curie, 75248 Paris Cedex 05, France; and {ddagger}Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-5430

Submitted August 19, 2007; Accepted August 31, 2007
Monitoring Editor: Sandra Schmid

The Golgi complex is characterized by its unique morphology of closely apposed flattened cisternae that persists despite the large quantity of lipids and proteins that transit bidirectionally. Whether such a structure is maintained through endoplasmic reticulum (ER)-based recycling and auto-organization or whether it depends on a permanent Golgi structure is strongly debated. To further study Golgi maintenance in interphase cells, we developed a method allowing for a drug-free inactivation of Golgi dynamics and function in living cells. After Golgi inactivation, a new Golgi-like structure, containing only certain Golgi markers and newly synthesized cargos, was produced. However, this structure did not acquire a normal Golgi architecture and was unable to ensure a normal trafficking activity. This suggests an integrative model for Golgi maintenance in interphase where the ER is able to autonomously produce Golgi-like structures that need pre-existing Golgi complexes to be organized as morphologically normal and active Golgi elements.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-08-0799) on September 12, 2007.

Address correspondence to: Franck Perez (Franck.Perez{at}curie.fr)

Abbreviations used: BFA, brefeldin A; DAB, 3,3'-diaminobenzidine; EM, electron microscopy; EGFP, enhanced green fluorescent protein; EndoH, endoglycosidase H; ER, endoplasmic reticulum; FACS, fluorescence-activated cell sorting; HRP, horseradish peroxidase; ManII, mannosidase II; TGN, trans-Golgi network; VSV-G, vesicular stomatitis virus G protein.




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