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The Golgi apparatus lies in the centre of the secretory pathway, a complex membrane system conserved in all eukaryotic cells. It is similar to a compartmentalised conveyor belt system in a factory: it processes, distributes and stores a wide range of important proteins such as storage proteins in cereal grains or proteins involved in plant stress responses. In animal cells the Golgi apparatus is organised as a single large ribbon. A plant cell however can have up to hundreds of small mobile Golgi bodies which move along the cytoskeleton over the endoplasmic reticulum (ER). Golgi bodies contain enzymes that attach sugars to proteins, they pack and ship protein cargo and lipids and produce material for the cell wall.
In animal cells a family of proteins, the golgins, functions in the regulation of protein transport between the ER and the Golgi. It also acts as a structural scaffold, or Golgi matrix, for Golgi cisternae. We are studying arabidopsis homologues of these proteins to see if they take over similar functions in plants. My special research interest lies in plant Golgi tethering factors and their possible roles in Golgi biogenesis, structure and regulation of protein trafficking.
To characterise these proteins we are using advanced confocal laser scanning microscopy methods such as fluorescence lifetime imaging (FLIM) to study interactions between golgins and small GTPases or optical laser tweezers to pull Golgi bodies away from the ER in living plant cells.