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PhD British Columbia

Email: bodkb@ust.hk

The Banfield Lab@HKUST

Research Interests

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.

Representative Publications

  1. Banfield D.K. and Hong, W. (2008) SNAREs in The Golgi Apparatus – the state of the art 110 years after Camillo’s Discovery. A. Mironov, M. Pavelka and A. Luini ed. Springer Publishing (in press)
  2. Bubeck, J., Langhans, M., Scheuring, D., Foresti, O., Banfield, D.K., Denecke, J. and Robinson, D.G. (2008) The Golgi and ER syntaxins control anterograde and retrograde transport through the early secretory pathway. (Traffic, in press)
  3. Tu, L., Tai, W.C.S., Chen, L. and Banfield, D.K. (2008) Signal-mediated dynamic retention of glycosyltransferases in the Golgi. Science 321: 404-407. ( Abstract , Full Text )
  4. Wen, W., Chen, L., Wu, H., Sun, X., Zhang, M. and Banfield, D.K. (2006) Identification of the yeast R-SNARE Nyv1p as a novel longin domain containing protein. Molecular Biology of the Cell 17: 4282 – 4299.
  5. Rossi, V., Banfield, D.K., Vacca, M., Dietrich, L.E.P., Ungermann, C., D’Esposito, M., Galli. T. and Filippini, F. Longins and their longin domains: regulated SNAREs and multifunctional SNARE regulators. (2004) Trends in Biochemical Sciences 29: 682-688.
  6. Tochio, H., Tsui, M.M.K., Banfield, D.K. and Zhang, M. (2001) An auto-inhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p. Science 293:698-702.
  7. Tai, W.C.S. and Banfield, D.K. (2001) AtBS14a and AtBS14b two Bet1 / Sft1-like SNAREs from Arabidopsis thaliana that complement mutations in the yeast SFT1 gene. FEBS Letters 500:177-182.
  8. Tsui, M.M.K., Tai, W.C.S. and Banfield, D.K. (2001) The selective formation of Sed5p-containing SNARE complexes is mediated by combinatorial binding interactions. Molecular Biology of the Cell 12:521-538.
  9. Banfield, D.K. (2001) SNARE complexes – is there sufficient complexity for vesicle targeting specificity? Trends in Biochemical Sciences 26:67-68.
  10. Tsui, M.M.K. and Banfield, D.K. (2000) Yeast Golgi SNARE interactions are promiscuous. Journal of Cell Science 113:145-152.


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