Fellow

David Owen

Sponsored by Sean Munro

David Owen

All cells are surrounded by a phospholipid membrane and contain within them many membrane-bound compartments, termed organelles. The myriad biological functions that take place on these membranes are driven by the transproteins embedded in them. These transmembrane proteins are moved as cargo between a cell’s membranes in tubular-vesicular carriers. The formation of a carrier, packing of cargo into it and its delivery to the target organelle are carefully orchestrated processes.

Based in the Cambridge Institute for Medical Research, we aim to understand how these processes are orchestrated and coordinated. We use a combination of state-of-the-art atomic resolution structural studies aligned with functional assays carried out in vitro and in live cells.

We have collaborated extensively with former LMB Group Leader John Briggs on determining the architecture of the structure of retromer and AP2/clathrin coats using electron cryotomography. We also work with Sean Munro on the endosome to Golgi trafficking factor and cargo selector TBC1D23. We are currently working with both on aspects of Golgi to ER COPI-dependent vesicle trafficking.

As membrane trafficking and organelle function go awry in many pathophysiological states and are subverted by infectious pathogens, this research has major implications for health and disease.

Selected Publications

Cargo selective vesicle tethering: The structural basis for binding of specific cargo proteins by the Golgi tether component TBC1D23.Cattin-Ortolá J, Kaufman JGG, Gillingham AK, Wagstaff JL, Peak-Chew SY, Stevens TJ, Boulanger J, Owen DJ, Munro SSci Adv 10(13): eadl0608 (2024)
Architecture and mechanism of metazoan retromer:SNX3 tubular coat assembly.Leneva N, Kovtun O, Morado DR, Briggs JAG, Owen DJSci Adv 7(13)
Architecture of the AP2/clathrin coat on the membranes of clathrin-coated vesicles.Kovtun O, Dickson VK, Kelly BT, Owen DJ, Briggs JAGSci Adv 6(30): eaba8381
Structure of the membrane-assembled retromer coat determined by cryo-electron tomography.Kovtun O, Leneva N, Bykov YS, Ariotti N, Teasdale RD, Schaffer M, Engel BD, Owen DJ, Briggs JAG, Collins BMNature 561(7724): 561-564 (2019)