Vesicle-mediated traffic to and through the Golgi Apparatus:
The transport of proteins between various compartments of the secretory pathway is mediated by membrane-bound vesicles that bud-off one membrane and are then targeted to and fuse with another. In order to maintain the integrity of the endo-membrane network and its organelles the fusion of transport vesicles with their target compartments must be precisely regulated. The specificity of transport vesicle targeting and fusion likely requires several components including: GTPases of the Ypt family (Rabs), tethering factors as well as SNARE proteins. It is unlikely that any single component is sufficient ensure the precise degree of specificity required. Using a combination of molecular genetics, biochemistry and structural studies Dr Banfield’s laboratory is examining vesicle-mediated traffic to and through the Golgi apparatus using the yeast Saccharomyces cerevisiae as a model system.
Potential research projects include:
Elucidating the role of SNARE proteins in the formation of Golgi-derived transport vesicles; *
Structure and function studies of Golgi-localized SNAREs and peripheral membrane proteins using NMR and or macromolecular crystallography;
The role phosphoinositides in the localization of proteins to the Golgi.
Through these studies Dr Banfield’s group hopes to learn more about the precise mechanism(s) of vesicle targeting and membrane fusion events and in so doing gain insight into the biogenesis and maintenance of the Golgi apparatus.
Chen, L., Lau, S.Y. and Banfield, D.K. (2016) Multiple ER-Golgi SNARE transmembrane domains are dispensible for trafficking but required for SNARE recycling. Molecular Biology of the Cell 27: 2633 – 2641.
Woo, C.H., Gao, C., Yu, P., Tu, L., Meng, Z., Banfield, D.K., Yao, X and Jiang, L (2015) Conserved function of the lysine-based KXD/E motif in Golgi retention for endomembrane proteins among different organisms. Molecular Biology of the Cell 26: 4280 – 4293.
Banfield, David K.; Prinz, Will (2014) Cell Organelles, Current Opinion in Cell Biology: Volume 29, pages 1-142, August 2014.
Tu, L., Chen, L. and Banfield, D.K. (2012) A Conserved N-terminal Arginine-Motif in GOLPH3-Family Proteins Mediates Binding to Coatomer. Traffic13: 1496-1507.
Banfield, D.K. Mechanisms of Protein Retention in the Golgi. in Cold Spring Harbor Perspectives in Biology G. Warren and J. Rothman eds. Cold Spring Harbor Press. (2011) pgs 141-154.