Research in our lab focuses on the molecular organization of the Golgi apparatus and the biogenesis of this organelle during the cell cycle. In particular, we are interested in studying the proteins that help "glue" the cisternae together to form a stack and the role of ubiquitin in regulation of Golgi membrane dynamics during the cell cycle.
To study the molecular organization and cell cycle regulation of Golgi membrane dynamics, we have been using an in vitro system to reconstitute the process of Golgi fragmentation during mitosis and reassembly at the end of mitosis. We have shown a direct role for these proteins in linking Golgi cisternae.
We could also show that ubiquitination of Golgi membrane proteins during mitosis is essential for subsequent membrane fusion and reassembly. Our aim is to understand the mechanism that fragments the Golgi early in mitosis and rebuilds it in each daughter cell towards the end of cell division.
This will not only help us to understand the mechanisms that generate and maintain the unique architecture of this organelle, but will also shed light on a fundamental cell biological process that enables cells to propagate cellular organelles through future generations.
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Fig. 1. Cell cycle regulated Golgi disassembly and reassembly. A. Fluorecence images using a GFP-tagged Golgi enzyme. Bar: 5 Ám. B. EM images of the in vitro reconstituted Golgi disassembly/reassembly cycle. Bar: 0.5 Ám.