Roy Duncan

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External Website:

Roy Duncan Dalhousie University Profile

Research Interests

Dr. Duncan’s research group discovered the reovirus fusion-associated small transmembrane (FAST) proteins, a novel family of virus-encoded fusogens that mediate cell-cell membrane fusion. His interests are focused on biochemical and biophysical analysis of the FAST proteins, cellular pathways involved in cell-cell fusion, and factors that affect actin dynamics during membrane fusion and cell migration.

Selected publications

For a complete list of Dr. Roy Duncan's publications, click here.

  • Parmar, H. and Duncan, R., (2016) A novel tribasic Golgi export signal directs cargo protein interaction with activated Rab11 and AP-1–dependent Golgi–plasma membrane trafficking Mol. Biol. Cell 27:1320-1331

  • Read, J., Clancy, E.K., Sarker, M., de Antueno, R., Langelaan, D.N., Parmar, H.B., Shin, K., Rainey, J.K. and Duncan, R., (2015) Reovirus FAST proteins drive pore formation and syncytiogenesis using a novel helix-loop-helix fusion-inducing lipid packing sensor PLoS Pathog 11(6):e1004962

  • Kai, F., Fawcett, J., and Duncan, R., (2015) Synaptopodin-2 induces assembly of peripheral actin bundles and immature focal adhesions to promote lamellipodia formation and prostate cancer cell migration Oncotarget 6: 11162-11174.

  • Key, T. and Duncan, R., (2014) A compact, multifunctional fusion module directs cholesterol-dependent homomultimerization and syncytiogenic efficiency of reovirus p10 FAST proteins. PLOS Pathogens 10:e1004023

  • Ciechonska, M. and Duncan, R., (2014) Reovirus FAST proteins: virus-encoded cellular fusogens. Trends in Microbiology 22:715-724

  • Parmar, H., Barry, C., Kai, F., and Duncan, R., (2014) Golgi complex-plasma membrane trafficking directed by an autonomous, tri-basic Golgi export signal Mol. Biol. Cell 25:866-878

  • Top, D., Read, J., Dawe, S., Syvitski, R., and Duncan, R.* (2012). Cell-cell membrane fusion induced by the p15 FAST protein requires a novel fusion peptide motif containing a myristoylated polyproline type II helix. J. Biol. Chem. 287: 3403-3414.

  • Top, D., Barry, C., Racine, T., Ellis, C., and Duncan, R.* (2009). Enhanced fusion pore expansion mediated by the trans-acting endodomain of the reovirus FAST proteins. PloS Pathogens 5: e1000331.

  • Salsman, J., Top, D., Barry, C. and Duncan, R.* (2008). A virus-encoded cell-cell fusion machine dependent on surrogate adhesins. PloS Pathogens 4: e1000016.

  • Top, D., de Antueno, R., Salsman, J., Corcoran, J., Mader, J., Hoskin, D., Jerricho, M. and Duncan, R.* (2005). Liposome reconstitution of a minimal protein-mediated membrane fusion machine. EMBO J. 24: 2980-2988.

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