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CeNS Colloquium

Place: Kleiner Physik-Hörsaal, Geschwister-Scholl-Platz
Date: 09.07.10, Time: 15:30 h

Sorting out protein traffic in the early secretory pathway

Dr. Matthias Weiss
Cellular Biophysics Group (B085), German Cancer Research Center, Heidelberg

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 to the cell's major hub for protein sorting, the Golgi apparatus. Indeed, the existence and morphology of a Golgi apparatus critically depends on this incoming flux of nascent proteins. Using light microscopy and simulations, we have addressed the following questions:
   (1) What are dynamic fingerprints of chaperone-assisted folding in the ER?
   (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?