Location: De Sitterzaal
Time: 13:15 - 14:15 hrs

The vast majority of membrane proteins, i.e. about 30% of the cell's proteom, enter the endoplasmic reticulum (ER) during or after translation. In the ER, these mostly unfolded polypeptide chains undergo chaperone-assisted folding before properly folded proteins are allowed to leave the ER via small membraneous vesicles.
These vesicles shuttle proteins through the cytoplasm to the cell's major hub for protein sorting, the Golgi apparatus. The existence and morphology of a Golgi apparatus critically depends on this incoming flux of nascent proteins and membranes. Using light microscopy and simulations, we have addressed the following questions:
(1) How do proteins diffuse in the complex cellular environment,
e.g. in the ER and in the surrounding cytoplasm?
(2) How do proteins sort out in which compartment they are and
which one they want to reach?
(3) What are the generic principles that govern the self-assembly
and morphology of a Golgi apparatus?