Oxford Events, the new replacement for OxTalks, will launch on 16th March. The two-week OxTalks freeze period starts on Monday 2nd March. During this time, there will be no facility to publish or edit events. The existing OxTalks site will remain available to view during this period. Once Oxford Events launches, you will need a Halo login to submit events. Full details are available on the Staff Gateway.
Recently we determined the first crystal structure for the KDEL trafficking receptor, which functions to maintain the integrity of the ER and Golgi. The receptor functions by selectively retrieving folding chaperones, which contain a C-terminal KDEL retention signal, in a pH dependent manner from the Golgi back to the ER via COPI coated vesicles. The structure and associated functional insights reveal a remarkable and somewhat unexpected similarity to membrane transporters, which in contrast to trafficking receptors, function to shuttle nutrients and small molecules across a single membrane rather than between two separate membrane environments. In this talk I will present how these insights uniquely bring together what where once considered two different themes of cell biology, transport and trafficking, and discuss how these two systems share mechanisms for peptide recognition and proton coupling in the cell.
