Analysis of de novo Golgi complex formation after enzyme-based inactivation.
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 cargoes, 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.
Jollivet
Florence
F
Centre National de la Recherche Scientifique Unité Mixte de Recherche 144, 75248 Paris Cedex 05, France.
Raposo
Graça
G
Dimitrov
Ariane
A
Sougrat
Rachid
R
Goud
Bruno
B
Perez
Franck
F
D015100:3,3'-Diaminobenzidine / Q000494:pharmacology; D002470:Cell Survival; D004721:Endoplasmic Reticulum / Q000378:metabolism; D004789:Enzyme Activation; D006056:Golgi Apparatus / Q000187:drug effects / Q000201:enzymology* / Q000502:physiology* / Q000648:ultrastructure; D006367:HeLa Cells; D006735:Horseradish Peroxidase / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007399:Interphase; D008854:Microscopy, Electron; D011485:Protein Binding
D015100:3,3'-Diaminobenzidine; D006735:Horseradish Peroxidase